Antibody-dependent enhancement

Last updated

In antibody-dependent enhancement, sub-optimal antibodies (the blue Y-shaped structures in the graphic) bind to both viruses and Fc gamma receptors (labeled FcgRII) expressed on immune cells, promoting infection of these cells. Antibody dependent enhancement-en.svg
In antibody-dependent enhancement, sub-optimal antibodies (the blue Y-shaped structures in the graphic) bind to both viruses and Fc gamma receptors (labeled FcγRII) expressed on immune cells, promoting infection of these cells.

Antibody-dependent enhancement (ADE), sometimes less precisely called immune enhancement or disease enhancement, is a phenomenon in which binding of a virus to suboptimal antibodies enhances its entry into host cells, followed by its replication. [1] [2] The suboptimal antibodies can result from natural infection or from vaccination. ADE may cause enhanced respiratory disease, but is not limited to respiratory disease. [3] It has been observed in HIV, RSV, and Dengue virus and is monitored for in vaccine development. [4]

Contents

Technical description

In ADE, antiviral antibodies promote viral infection of target immune cells by exploiting the phagocytic FcγR or complement pathway. [5] After interaction with a virus, the antibodies bind Fc receptors (FcR) expressed on certain immune cells or complement proteins. FcγRs bind antibodies via their fragment crystallizable region (Fc).

The process of phagocytosis is accompanied by virus degradation, but if the virus is not neutralized (either due to low affinity binding or targeting to a non-neutralizing epitope), antibody binding may result in virus escape and, therefore, more severe infection. Thus, phagocytosis can cause viral replication and the subsequent death of immune cells. Essentially, the virus “deceives” the process of phagocytosis of immune cells and uses the host's antibodies as a Trojan horse.

ADE may occur because of the non-neutralizing characteristic of an antibody, which binds viral epitopes other than those involved in host-cell attachment and entry. It may also happen when antibodies are present at sub-neutralizing concentrations (yielding occupancies on viral epitopes below the threshold for neutralization), [6] [7] or when the strength of antibody-antigen interaction is below a certain threshold. [8] [9] This phenomenon can lead to increased viral infectivity and virulence.

ADE can occur during the development of a primary or secondary viral infection, as well as with a virus challenge after vaccination. [1] [10] [11] It has been observed mainly with positive-strand RNA viruses, including flaviviruses such as dengue, yellow fever, and Zika; [12] [13] [14] alpha- and betacoronaviruses; [15] orthomyxoviruses such as influenza; [16] retroviruses such as HIV; [17] [18] [19] and orthopneumoviruses such as RSV. [20] [21] [22] The viruses that cause it frequently share common features such as antigenic diversity, replication ability, or ability to establish persistence in immune cells. [1]

The mechanism that involves phagocytosis of immune complexes via the FcγRII/CD32 receptor is better understood compared to the complement receptor pathway. [23] [24] [25] Cells that express this receptor are represented by monocytes, macrophages, and some categories of dendritic cells and B-cells. ADE is mainly mediated by IgG antibodies, [24] but IgM [26] and IgA antibodies [18] [19] have also been shown to trigger it.

Coronavirus

COVID-19

Prior to the COVID-19 pandemic, ADE was observed in animal studies of laboratory rodents with vaccines for SARS-CoV, the virus that causes severe acute respiratory syndrome (SARS). As of 27 January 2022, there have been no observed incidents with vaccines for COVID-19 in trials with nonhuman primates, in clinical trials with humans, or following the widespread use of approved vaccines. [27] [28] [29] [30] [31]

Influenza

Prior receipt of 2008–09 TIV (Trivalent Inactivated Influenza Vaccine) was associated with an increased risk of medically attended pH1N1 illness during the spring-summer 2009 in Canada. The occurrence of bias (selection, information) or confounding cannot be ruled out. Further experimental and epidemiological assessment is warranted. Possible biological mechanisms and immunoepidemiologic implications are considered. [32]

Natural infection and the attenuated vaccine induce antibodies that enhance the update of the homologous virus and H1N1 virus isolated several years later, demonstrating that a primary influenza A virus infection results in the induction of infection enhancing antibodies. [33]

ADE was suspected in infections with influenza A virus subtype H7N9, but knowledge is limited.

Dengue

The most widely known ADE example occurs with dengue virus. [34] Dengue is a single-stranded positive-polarity RNA virus of the family Flaviviridae . It causes disease of varying severity in humans, from dengue fever (DF), which is usually self-limited, to dengue hemorrhagic fever and dengue shock syndrome, either of which may be life-threatening. [35] It is estimated that as many as 390 million individuals contract dengue annually. [36]

ADE may follow when a person who has previously been infected with one serotype becomes infected months or years later with a different serotype, producing higher viremia than in first-time infections. Accordingly, while primary (first) infections cause mostly minor disease (dengue fever) in children, re-infection is more likely to be associated with dengue hemorrhagic fever and/or dengue shock syndrome in both children and adults. [37]

Dengue encompasses four antigenically different serotypes (dengue virus 1–4). [38] In 2013 a fifth serotype was reported. [39] Infection induces the production of neutralizing homotypic immunoglobulin G (IgG) antibodies that provide lifelong immunity against the infecting serotype. Infection with dengue virus also produces some degree of cross-protective immunity against the other three serotypes. [40] Neutralizing heterotypic (cross-reactive) IgG antibodies are responsible for this cross-protective immunity, which typically persists for a period of months to a few years. These heterotypic titers decrease over long time periods (4 to 20 years). [41] While heterotypic titers decrease, homotypic IgG antibody titers increase over long time periods. This could be due to the preferential survival of long-lived memory B cells producing homotypic antibodies. [41]

In addition to neutralizing heterotypic antibodies, an infection can also induce heterotypic antibodies that neutralize the virus only partially or not at all. [42] The production of such cross-reactive, but non-neutralizing antibodies could enable severe secondary infections. By binding to but not neutralizing the virus, these antibodies cause it to behave as a "trojan horse", [43] [44] [45] where it is delivered into the wrong compartment of dendritic cells that have ingested the virus for destruction. [46] [47] Once inside the white blood cell, the virus replicates undetected, eventually generating high virus titers and severe disease. [48]

A study conducted by Modhiran et al. [49] attempted to explain how non-neutralizing antibodies down-regulate the immune response in the host cell through the Toll-like receptor signaling pathway. Toll-like receptors are known to recognize extra- and intracellular viral particles and to be a major basis of the cytokines' production. In vitro experiments showed that the inflammatory cytokines and type 1 interferon production were reduced when the ADE-dengue virus complex bound to the Fc receptor of THP-1 cells. This can be explained by both a decrease of Toll-like receptor production and a modification of its signaling pathway. On the one hand, an unknown protein induced by the stimulated Fc receptor reduces Toll-like receptor transcription and translation, which reduces the capacity of the cell to detect viral proteins. On the other hand, many proteins (TRIF, TRAF6, TRAM, TIRAP, IKKα, TAB1, TAB2, NF-κB complex) involved in the Toll-like receptor signaling pathway are down-regulated, which led to a decrease in cytokine production. Two of them, TRIF and TRAF6, are respectively down-regulated by 2 proteins SARM and TANK up-regulated by the stimulated Fc receptors.

One example occurred in Cuba, lasting from 1977 to 1979. The infecting serotype was dengue virus-1. This epidemic was followed by outbreaks in 1981 and 1997. In those outbreaks; dengue virus-2 was the infecting serotype. 205 cases of dengue hemorrhagic fever and dengue shock syndrome occurred during the 1997 outbreak, all in people older than 15 years. All but three of these cases were demonstrated to have been previously infected by dengue virus-1 during the first outbreak. [50] Furthermore, people with secondary infections with dengue virus-2 in 1997 had a 3-4 fold increased probability of developing severe disease than those with secondary infections with dengue virus-2 in 1981. [41] This scenario can be explained by the presence of sufficient neutralizing heterotypic IgG antibodies in 1981, whose titers had decreased by 1997 to the point where they no longer provided significant cross-protective immunity.

HIV-1

ADE of infection has also been reported in HIV. Like dengue virus, non-neutralizing level of antibodies have been found to enhance the viral infection through interactions of the complement system and receptors. [51] The increase in infection has been reported to be over 350 fold which is comparable to ADE in other viruses like dengue virus. [51] ADE in HIV can be complement-mediated or Fc receptor-mediated. Complements in the presence of HIV-1 positive sera have been found to enhance the infection of the MT-2 T-cell line. The Fc-receptor mediated enhancement was reported when HIV infection was enhanced by sera from HIV-1 positive guinea pig enhanced the infection of peripheral blood mononuclear cells without the presence of any complements. [52] Complement component receptors CR2, CR3 and CR4 have been found to mediate this Complement-mediated enhancement of infection. [51] [53] The infection of HIV-1 leads to activation of complements. Fragments of these complements can assist viruses with infection by facilitating viral interactions with host cells that express complement receptors. [54] The deposition of complement on the virus brings the gp120 protein close to CD4 molecules on the surface of the cells, thus leading to facilitated viral entry. [54] Viruses pre-exposed to non-neutralizing complement system have also been found to enhance infections in interdigitating dendritic cells. Opsonized viruses have not only shown enhanced entry but also favorable signaling cascades for HIV replication in interdigitating dendritic cells. [55]

HIV-1 has also shown enhancement of infection in HT-29 cells when the viruses were pre-opsonized with complements C3 and C9 in seminal fluid. This enhanced rate of infection was almost 2 times greater than infection of HT-29 cells with the virus alone. [56] Subramanian et al., reported that almost 72% of serum samples out of 39 HIV-positive individuals contained complements that were known to enhance the infection. They also suggested that the presence of neutralizing antibody or antibody-dependent cellular cytotoxicity-mediating antibodies in the serum contains infection-enhancing antibodies. [57] The balance between the neutralizing antibodies and infection-enhancing antibodies changes as the disease progresses. During advanced stages of the disease, the proportion of infection-enhancing antibodies are generally higher than neutralizing antibodies. [58] Increase in viral protein synthesis and RNA production have been reported to occur during the complement-mediated enhancement of infection. Cells that are challenged with non-neutralizing levels of complements have been found to have accelerated release of reverse transcriptase and viral progeny. [59] The interaction of anti-HIV antibodies with non-neutralizing complement exposed viruses also aid in binding of the virus and the erythrocytes which can lead to the more efficient delivery of viruses to the immune-compromised organs. [53]

ADE in HIV has raised questions about the risk of infections to volunteers who have taken sub-neutralizing levels of vaccine just like any other viruses that exhibit ADE. Gilbert et al., in 2005 reported that there was no ADE of infection when they used the rgp120 vaccine in phase 1 and 2 trials. [60] It has been emphasized that much research needs to be done in the field of the immune response to HIV-1, information from these studies can be used to produce a more effective vaccine.

Mechanism

Interaction of a virus with antibodies must prevent the virus from attaching to the host cell entry receptors. However, instead of preventing infection of the host cell, this process can facilitate viral infection of immune cells, causing ADE. [1] [5] After binding the virus, the antibody interacts with Fc or complement receptors expressed on certain immune cells. These receptors promote virus-antibody internalization by the immune cells, which should be followed by the virus destruction. However, the virus might escape the antibody complex and start its replication cycle inside the immune cell avoiding the degradation. [5] [26] This happens if the virus is bound to a low-affinity antibody.

Different virus serotypes

There are several possibilities to explain the phenomenon of enhancing intracellular virus survival:

1) Antibodies against a virus of one serotype binds to a virus of a different serotype. The binding is meant to neutralize the virus from attaching to the host cell, but the virus-antibody complex also binds to the Fc-region antibody receptor (FcγR) on the immune cell. The cell internalizes the virus for programmed destruction but the virus avoids it and starts its replication cycle instead. [61]

2) Antibodies against a virus of one serotype binds to a virus of a different serotype, activating the classical pathway of the complement system. The complement cascade system binds C1Q complex attached to the virus surface protein via the antibodies, which in turn bind C1q receptor found on cells, bringing the virus and the cell close enough for a specific virus receptor to bind the virus, beginning infection. [26] This mechanism has been shown for Ebola virus in vitro [62] and some flaviviruses in vivo. [26]

Conclusion

When an antibody to a virus is unable to neutralize the virus, it forms sub-neutralizing virus-antibody complexes. Upon phagocytosis by macrophages or other immune cells, the complex may release the virus due to poor binding with the antibody. This happens during acidification and eventual fusion of the phagosome [63] [64] with lysosomes. [65] The escaped virus begins its replication cycle within the cell, triggering ADE. [1] [5] [6]

See also

Related Research Articles

<span class="mw-page-title-main">Dengue fever</span> Mosquito-borne disease

Dengue fever is a mosquito-borne disease caused by dengue virus, prevalent in tropical and subtropical areas. It is frequently asymptomatic; if symptoms appear they typically begin 3 to 14 days after infection. These may include a high fever, headache, vomiting, muscle and joint pains, and a characteristic skin itching and skin rash. Recovery generally takes two to seven days. In a small proportion of cases, the disease develops into severe dengue with bleeding, low levels of blood platelets, blood plasma leakage, and dangerously low blood pressure.

<span class="mw-page-title-main">DNA vaccine</span> Vaccine containing DNA

A DNA vaccine is a type of vaccine that transfects a specific antigen-coding DNA sequence into the cells of an organism as a mechanism to induce an immune response.

<span class="mw-page-title-main">HIV vaccine development</span> In-progress vaccinations that may prevent or treat HIV infections

An HIV vaccine is a potential vaccine that could be either a preventive vaccine or a therapeutic vaccine, which means it would either protect individuals from being infected with HIV or treat HIV-infected individuals. It is thought that an HIV vaccine could either induce an immune response against HIV or consist of preformed antibodies against HIV.

<span class="mw-page-title-main">Poliovirus</span> Enterovirus

Poliovirus, the causative agent of polio, is a serotype of the species Enterovirus C, in the family of Picornaviridae. There are three poliovirus serotypes, numbered 1, 2, and 3.

<i>Dengue virus</i> Species of virus

Dengue virus (DENV) is the cause of dengue fever. It is a mosquito-borne, single positive-stranded RNA virus of the family Flaviviridae; genus Flavivirus. Four serotypes of the virus have been found, and a reported fifth has yet to be confirmed, all of which can cause the full spectrum of disease. Nevertheless, the mainstream scientific community's understanding of dengue virus may be simplistic as, rather than distinct antigenic groups, a continuum appears to exist. This same study identified 47 strains of dengue virus. Additionally, coinfection with and lack of rapid tests for Zika virus and chikungunya complicate matters in real-world infections.

<span class="mw-page-title-main">Adaptive immune system</span> Subsystem of the immune system

The adaptive immune system, also known as the acquired immune system, or specific immune system is a subsystem of the immune system that is composed of specialized cells, organs, and processes that eliminate pathogens specifically. The acquired immune system is one of the two main immunity strategies found in vertebrates.

<span class="mw-page-title-main">Original antigenic sin</span> Immune phenomenon

Original antigenic sin, also known as antigenic imprinting, the Hoskins effect, immunological imprinting, or primary addiction is the propensity of the immune system to preferentially use immunological memory based on a previous infection when a second slightly different version of that foreign pathogen is encountered. This leaves the immune system "trapped" by the first response it has made to each antigen, and unable to mount potentially more effective responses during subsequent infections. Antibodies or T-cells induced during infections with the first variant of the pathogen are subject to repertoire freeze, a form of original antigenic sin.

Following infection with HIV-1, the rate of clinical disease progression varies between individuals. Factors such as host susceptibility, genetics and immune function, health care and co-infections as well as viral genetic variability may affect the rate of progression to the point of needing to take medication in order not to develop AIDS.

<span class="mw-page-title-main">Envelope glycoprotein GP120</span> Glycoprotein exposed on the surface of the HIV virus

Envelope glycoprotein GP120 is a glycoprotein exposed on the surface of the HIV envelope. It was discovered by Professors Tun-Hou Lee and Myron "Max" Essex of the Harvard School of Public Health in 1984. The 120 in its name comes from its molecular weight of 120 kDa. Gp120 is essential for virus entry into cells as it plays a vital role in attachment to specific cell surface receptors. These receptors are DC-SIGN, Heparan Sulfate Proteoglycan and a specific interaction with the CD4 receptor, particularly on helper T-cells. Binding to CD4 induces the start of a cascade of conformational changes in gp120 and gp41 that lead to the fusion of the viral membrane with the host cell membrane. Binding to CD4 is mainly electrostatic although there are van der Waals interactions and hydrogen bonds.

<span class="mw-page-title-main">Antibody-dependent cellular cytotoxicity</span> Cell-mediated killing of other cells mediated by antibodies

Antibody-dependent cellular cytotoxicity (ADCC), also referred to as antibody-dependent cell-mediated cytotoxicity, is a mechanism of cell-mediated immune defense whereby an effector cell of the immune system kills a target cell, whose membrane-surface antigens have been bound by specific antibodies. It is one of the mechanisms through which antibodies, as part of the humoral immune response, can act to limit and contain infection.

Antigenic variation or antigenic alteration refers to the mechanism by which an infectious agent such as a protozoan, bacterium or virus alters the proteins or carbohydrates on its surface and thus avoids a host immune response, making it one of the mechanisms of antigenic escape. It is related to phase variation. Antigenic variation not only enables the pathogen to avoid the immune response in its current host, but also allows re-infection of previously infected hosts. Immunity to re-infection is based on recognition of the antigens carried by the pathogen, which are "remembered" by the acquired immune response. If the pathogen's dominant antigen can be altered, the pathogen can then evade the host's acquired immune system. Antigenic variation can occur by altering a variety of surface molecules including proteins and carbohydrates. Antigenic variation can result from gene conversion, site-specific DNA inversions, hypermutation, or recombination of sequence cassettes. The result is that even a clonal population of pathogens expresses a heterogeneous phenotype. Many of the proteins known to show antigenic or phase variation are related to virulence.

CD4 immunoadhesin is a recombinant fusion protein consisting of a combination of CD4 and the fragment crystallizable region, similarly known as immunoglobulin. It belongs to the antibody (Ig) gene family. CD4 is a surface receptor for human immunodeficiency virus (HIV). The CD4 immunoadhesin molecular fusion allow the protein to possess key functions from each independent subunit. The CD4 specific properties include the gp120-binding and HIV-blocking capabilities. Properties specific to immunoglobulin are the long plasma half-life and Fc receptor binding. The properties of the protein means that it has potential to be used in AIDS therapy as of 2017. Specifically, CD4 immunoadhesin plays a role in antibody-dependent cell-mediated cytotoxicity (ADCC) towards HIV-infected cells. While natural anti-gp120 antibodies exhibit a response towards uninfected CD4-expressing cells that have a soluble gp120 bound to the CD4 on the cell surface, CD4 immunoadhesin, however, will not exhibit a response. One of the most relevant of these possibilities is its ability to cross the placenta.

<span class="mw-page-title-main">HAVCR1</span> Protein-coding gene in the species Homo sapiens

Hepatitis A virus cellular receptor 1 (HAVcr-1) also known as T-cell immunoglobulin and mucin domain 1 (TIM-1) is a protein that in humans is encoded by the HAVCR1 gene.

2F5 is a broadly neutralizing human monoclonal antibody (mAb) that has been shown to bind to and neutralize HIV-1 in vitro, making it a potential candidate for use in vaccine synthesis. 2F5 recognizes an epitope in the membrane-proximal external region (MPER) of HIV-1 gp41. 2F5 then binds to this epitope and its constant region interacts with the viral lipid membrane, which neutralizes the virus.

A neutralizing antibody (NAb) is an antibody that defends a cell from a pathogen or infectious particle by neutralizing any effect it has biologically. Neutralization renders the particle no longer infectious or pathogenic. Neutralizing antibodies are part of the humoral response of the adaptive immune system against viruses, bacteria and microbial toxin. By binding specifically to surface structures (antigen) on an infectious particle, neutralizing antibodies prevent the particle from interacting with its host cells it might infect and destroy.

Pseudotyping is the process of producing viruses or viral vectors in combination with foreign viral envelope proteins. The result is a pseudotyped virus particle, also called a pseudovirus. With this method, the foreign viral envelope proteins can be used to alter host tropism or increase or decrease the stability of the virus particles. Pseudotyped particles do not carry the genetic material to produce additional viral envelope proteins, so the phenotypic changes cannot be passed on to progeny viral particles. In some cases, the inability to produce viral envelope proteins renders the pseudovirus replication incompetent. In this way, the properties of dangerous viruses can be studied in a lower risk setting.

Intrastructural help (ISH) is where T and B cells cooperate to help or suppress an immune response gene. ISH has proven effective for the treatment of influenza, rabies related lyssavirus, hepatitis B, and the HIV virus. This process was used in 1979 to observe that T cells specific to the influenza virus could promote the stimulation of hemagglutinin specific B cells and elicit an effective humoral immune response. It was later applied to the lyssavirus and was shown to protect raccoons from lethal challenge. The ISH principle is especially beneficial because relatively invariable structural antigens can be used for the priming of T-cells to induce humoral immune response against variable surface antigens. Thus, the approach has also transferred well for the treatment of hepatitis B and HIV.

Catherine Blish is a translational immunologist and professor at Stanford University. Her lab works on clinical immunology and focuses primarily on the role of the innate immune system in fighting infectious diseases like HIV, dengue fever, and influenza. Her immune cell biology work characterizes the biology and action of Natural Killer (NK) cells and macrophages.

<span class="mw-page-title-main">Viral vector vaccine</span> Type of vaccine

A viral vector vaccine is a vaccine that uses a viral vector to deliver genetic material (DNA) that can be transcribed by the recipient's host cells as mRNA coding for a desired protein, or antigen, to elicit an immune response. As of April 2021, six viral vector vaccines, four COVID-19 vaccines and two Ebola vaccines, have been authorized for use in humans.

Passive antibody therapy, also called serum therapy, is a subtype of passive immunotherapy that administers antibodies to target and kill pathogens or cancer cells. It is designed to draw support from foreign antibodies that are donated from a person, extracted from animals, or made in the laboratory to elicit an immune response instead of relying on the innate immune system to fight disease. It has a long history from the 18th century for treating infectious diseases and is now a common cancer treatment. The mechanism of actions include: antagonistic and agonistic reaction, complement-dependent cytotoxicity (CDC), and antibody-dependent cellular cytotoxicity (ADCC).

References

  1. 1 2 3 4 5 Tirado SM, Yoon KJ (2003). "Antibody-dependent enhancement of virus infection and disease". Viral Immunology. 16 (1): 69–86. doi:10.1089/088282403763635465. PMID   12725690.
  2. ↑ Wilder-Smith A, Hombach J, Ferguson N, Selgelid M, O'Brien K, Vannice K, et al. (January 2019). "Antibody-Dependent Enhancement of Viral Infections". Dynamics of Immune Activation in Viral Diseases. Vol. 19. Springer. pp. e31–e38. doi:10.1007/978-981-15-1045-8_2. ISBN   978-981-15-1044-1. PMC   7119964 . PMID   30195995.{{cite book}}: |journal= ignored (help)
  3. ↑ Su S, Du L, Jiang S (March 2021). "Learning from the past: development of safe and effective COVID-19 vaccines". Nature Reviews. Microbiology. 19 (3): 211–219. doi:10.1038/s41579-020-00462-y. ISSN   1740-1526. PMC   7566580 . PMID   33067570.
  4. ↑ "Why ADE Hasn't Been a Problem With COVID Vaccines". www.medpagetoday.com. 2021-03-16. Retrieved 2022-04-05.
  5. 1 2 3 4 Bournazos S, Gupta A, Ravetch JV (October 2020). "The role of IgG Fc receptors in antibody-dependent enhancement". Nature Reviews. Immunology. 20 (10): 633–643. doi: 10.1038/s41577-020-00410-0 . PMC   7418887 . PMID   32782358. S2CID   221108413.
  6. 1 2 Wilder-Smith A, Hombach J, Ferguson N, Selgelid M, O'Brien K, Vannice K, et al. (January 2019). "Antibody-Dependent Enhancement of Viral Infections". Dynamics of Immune Activation in Viral Diseases. Vol. 19. Springer. pp. e31–e38. doi:10.1007/978-981-15-1045-8_2. ISBN   978-981-15-1044-1. PMC   7119964 . PMID   30195995.{{cite book}}: |journal= ignored (help)
  7. ↑ Klasse PJ (2014-09-09). "Neutralization of Virus Infectivity by Antibodies: Old Problems in New Perspectives". Advances in Biology. 2014: 1–24. doi: 10.1155/2014/157895 . PMC   4835181 . PMID   27099867.
  8. ↑ Iwasaki A, Yang Y (June 2020). "The potential danger of suboptimal antibody responses in COVID-19". Nature Reviews. Immunology. 20 (6): 339–341. doi: 10.1038/s41577-020-0321-6 . PMC   7187142 . PMID   32317716.
  9. ↑ Ricke D, Malone RW (2020). "Medical Countermeasures Analysis of 2019-nCoV and Vaccine Risks for Antibody-Dependent Enhancement (ADE)". SSRN Working Paper Series. doi:10.2139/ssrn.3546070. ISSN   1556-5068. S2CID   216395996.
  10. ↑ Tay MZ, Wiehe K, Pollara J (2019). "Antibody-Dependent Cellular Phagocytosis in Antiviral Immune Responses". Frontiers in Immunology. 10: 332. doi: 10.3389/fimmu.2019.00332 . PMC   6404786 . PMID   30873178.
  11. ↑ Smatti MK, Al Thani AA, Yassine HM (2018-12-05). "Viral-Induced Enhanced Disease Illness". Frontiers in Microbiology. 9: 2991. doi: 10.3389/fmicb.2018.02991 . PMC   6290032 . PMID   30568643.
  12. ↑ de Alwis R, Williams KL, Schmid MA, Lai CY, Patel B, Smith SA, et al. (October 2014). "Dengue viruses are enhanced by distinct populations of serotype cross-reactive antibodies in human immune sera". PLOS Pathogens. 10 (10): e1004386. doi: 10.1371/journal.ppat.1004386 . PMC   4183589 . PMID   25275316.
  13. ↑ Khandia R, Munjal A, Dhama K, Karthik K, Tiwari R, Malik YS, et al. (2018). "Modulation of Dengue/Zika Virus Pathogenicity by Antibody-Dependent Enhancement and Strategies to Protect Against Enhancement in Zika Virus Infection". Frontiers in Immunology. 9: 597. doi: 10.3389/fimmu.2018.00597 . PMC   5925603 . PMID   29740424.
  14. ↑ Plotkin S, Orenstein W (2012). "Yellow fever vaccine". Vaccines (6 ed.). Amsterdam: Elsevier. pp. 870–968. ISBN   9781455700905.
  15. ↑ Yip MS, Leung NH, Cheung CY, Li PH, Lee HH, Daëron M, et al. (May 2014). "Antibody-dependent infection of human macrophages by severe acute respiratory syndrome coronavirus". Virology Journal. 11 (1): 82. doi: 10.1186/1743-422X-11-82 . PMC   4018502 . PMID   24885320.
  16. ↑ Winarski KL, Tang J, Klenow L, Lee J, Coyle EM, Manischewitz J, et al. (July 2019). "Antibody-dependent enhancement of influenza disease promoted by increase in hemagglutinin stem flexibility and virus fusion kinetics". Proceedings of the National Academy of Sciences of the United States of America. 116 (30): 15194–15199. Bibcode:2019PNAS..11615194W. doi: 10.1073/pnas.1821317116 . PMC   6660725 . PMID   31296560.
  17. ↑ Füst G (1997). "Enhancing antibodies in HIV infection". Parasitology. 115 (7): S127-40. doi:10.1017/s0031182097001819. PMID   9571698. S2CID   27083994.
  18. 1 2 Janoff EN, Wahl SM, Thomas K, Smith PD (September 1995). "Modulation of human immunodeficiency virus type 1 infection of human monocytes by IgA". The Journal of Infectious Diseases. 172 (3): 855–8. doi:10.1093/infdis/172.3.855. PMID   7658082.
  19. 1 2 Kozlowski PA, Black KP, Shen L, Jackson S (June 1995). "High prevalence of serum IgA HIV-1 infection-enhancing antibodies in HIV-infected persons. Masking by IgG". Journal of Immunology. 154 (11): 6163–73. doi: 10.4049/jimmunol.154.11.6163 . PMID   7751656. S2CID   32129993.
  20. ↑ van Erp EA, van Kasteren PB, Guichelaar T, Ahout IM, de Haan CA, Luytjes W, et al. (November 2017). "In Vitro Enhancement of Respiratory Syncytial Virus Infection by Maternal Antibodies Does Not Explain Disease Severity in Infants". Journal of Virology. 91 (21). doi:10.1128/JVI.00851-17. PMC   5640862 . PMID   28794038.
  21. ↑ Osiowy C, Horne D, Anderson R (November 1994). "Antibody-dependent enhancement of respiratory syncytial virus infection by sera from young infants". Clinical and Diagnostic Laboratory Immunology. 1 (6): 670–7. doi:10.1128/CDLI.1.6.670-677.1994. PMC   368388 . PMID   8556519.
  22. ↑ Gimenez HB, Chisholm S, Dornan J, Cash P (May 1996). "Neutralizing and enhancing activities of human respiratory syncytial virus-specific antibodies". Clinical and Diagnostic Laboratory Immunology. 3 (3): 280–6. doi:10.1128/CDLI.3.3.280-286.1996. PMC   170331 . PMID   8705669.
  23. ↑ Porterfield JS, Cardosa MJ (1984). "Host Range and Tissue Tropisms: Antibody-Dependent Mechanisms". In Notkins AL, Oldstone MB (eds.). Concepts in Viral Pathogenesis. New York, NY: Springer. pp. 117–122. doi: 10.1007/978-1-4612-5250-4_17 . ISBN   978-1-4612-5250-4.
  24. 1 2 Bournazos S, Gupta A, Ravetch JV (October 2020). "The role of IgG Fc receptors in antibody-dependent enhancement". Nature Reviews. Immunology. 20 (10): 633–643. doi:10.1038/s41577-020-00410-0. PMC   7418887 . PMID   32782358.
  25. ↑ Takada A, Kawaoka Y (2003). "Antibody-dependent enhancement of viral infection: molecular mechanisms and in vivo implications". Reviews in Medical Virology. 13 (6): 387–98. doi:10.1002/rmv.405. PMID   14625886. S2CID   9755341.
  26. 1 2 3 4 Cardosa MJ, Porterfield JS, Gordon S (July 1983). "Complement receptor mediates enhanced flavivirus replication in macrophages". The Journal of Experimental Medicine. 158 (1): 258–63. doi:10.1084/jem.158.1.258. PMC   2187083 . PMID   6864163.
  27. ↑ Hotez PJ, Bottazzi ME (27 January 2022). "Whole Inactivated Virus and Protein-Based COVID-19 Vaccines". Annual Review of Medicine. 73 (1): 55–64. doi: 10.1146/annurev-med-042420-113212 . ISSN   0066-4219. PMID   34637324. S2CID   238747462.
  28. ↑ Hackethal V (16 March 2021). "Why ADE Hasn't Been a Problem With COVID Vaccines". www.medpagetoday.com. Archived from the original on 25 June 2021. Retrieved 1 July 2021.
  29. ↑ Haynes BF, Corey L, Fernandes P, Gilbert PB, Hotez PJ, Rao S, Santos MR, Schuitemaker H, Watson M, Arvin A (4 November 2020). "Prospects for a safe COVID-19 vaccine". Science Translational Medicine. 12 (568): eabe0948. doi: 10.1126/scitranslmed.abe0948 . ISSN   1946-6242. PMID   33077678. S2CID   224809822.
  30. ↑ Lambert PH, Ambrosino DM, Andersen SR, Baric RS, Black SB, Chen RT, et al. (June 2020). "Consensus summary report for CEPI/BC March 12-13, 2020 meeting: Assessment of risk of disease enhancement with COVID-19 vaccines". Vaccine. 38 (31): 4783–4791. doi:10.1016/j.vaccine.2020.05.064. PMC   7247514 . PMID   32507409.
  31. ↑ Haynes BF, Corey L, Fernandes P, Gilbert PB, Hotez PJ, Rao S, Santos MR, Schuitemaker H, Watson M, Arvin A (2020-10-19). "Prospects for a safe COVID-19 vaccine". Science Translational Medicine. 12 (568): eabe0948. doi: 10.1126/scitranslmed.abe0948 . PMID   33077678. S2CID   224809822.
  32. ↑ Skowronski DM, De Serres G, Crowcroft NS, Janjua NZ, Boulianne N, Hottes TS, et al. (April 2010). "Association between the 2008-09 seasonal influenza vaccine and pandemic H1N1 illness during Spring-Summer 2009: four observational studies from Canada". PLOS Medicine. 7 (4): e1000258. doi: 10.1371/journal.pmed.1000258 . PMC   2850386 . PMID   20386731.
  33. ↑ Gotoff R, Tamura M, Janus J, Thompson J, Wright P, Ennis FA (January 1994). "Primary influenza A virus infection induces cross-reactive antibodies that enhance uptake of virus into Fc receptor-bearing cells". The Journal of Infectious Diseases. 169 (1): 200–3. doi:10.1093/infdis/169.1.200. PMID   8277183.
  34. ↑ "Model of antibody-dependent enhancement of dengue infection | Learn Science at Scitable". www.nature.com. Archived from the original on 2021-03-16. Retrieved 2021-05-20.
  35. ↑ Boonnak K, Slike BM, Burgess TH, Mason RM, Wu SJ, Sun P, et al. (April 2008). "Role of dendritic cells in antibody-dependent enhancement of dengue virus infection". Journal of Virology. 82 (8): 3939–51. doi:10.1128/JVI.02484-07. PMC   2292981 . PMID   18272578.
  36. ↑ Ambuel Y, Young G, Brewoo JN, Paykel J, Weisgrau KL, Rakasz EG, et al. (15 September 2014). "A rapid immunization strategy with a live-attenuated tetravalent dengue vaccine elicits protective neutralizing antibody responses in non-human primates". Frontiers in Immunology. 5 (2014): 263. doi: 10.3389/fimmu.2014.00263 . PMC   4046319 . PMID   24926294.
  37. ↑ Guzman MG, Vazquez S (December 2010). "The complexity of antibody-dependent enhancement of dengue virus infection". Viruses. 2 (12): 2649–62. doi: 10.3390/v2122649 . PMC   3185591 . PMID   21994635.
  38. ↑ King CA, Anderson R, Marshall JS (August 2002). "Dengue virus selectively induces human mast cell chemokine production". Journal of Virology. 76 (16): 8408–19. doi:10.1128/JVI.76.16.8408-8419.2002. PMC   155122 . PMID   12134044.
  39. ↑ Normile D (October 2013). "Tropical medicine. Surprising new dengue virus throws a spanner in disease control efforts". Science. 342 (6157): 415. Bibcode:2013Sci...342..415N. doi:10.1126/science.342.6157.415. PMID   24159024.
  40. ↑ Alvarez G, Piñeros JG, Tobón A, Ríos A, Maestre A, Blair S, Carmona-Fonseca J (October 2006). "Efficacy of three chloroquine-primaquine regimens for treatment of Plasmodium vivax malaria in Colombia". The American Journal of Tropical Medicine and Hygiene. 75 (4): 605–9. doi: 10.4269/ajtmh.2006.75.605 . PMID   17038680.
  41. 1 2 3 Guzman MG, Alvarez M, Rodriguez-Roche R, Bernardo L, Montes T, Vazquez S, et al. (February 2007). "Neutralizing antibodies after infection with dengue 1 virus". Emerging Infectious Diseases. 13 (2): 282–6. doi:10.3201/eid1302.060539. PMC   2725871 . PMID   17479892.
  42. ↑ Goncalvez AP, Engle RE, St Claire M, Purcell RH, Lai CJ (May 2007). "Monoclonal antibody-mediated enhancement of dengue virus infection in vitro and in vivo and strategies for prevention". Proceedings of the National Academy of Sciences of the United States of America. 104 (22): 9422–7. Bibcode:2007PNAS..104.9422G. doi: 10.1073/pnas.0703498104 . PMC   1868655 . PMID   17517625.
  43. ↑ Peluso R, Haase A, Stowring L, Edwards M, Ventura P (November 1985). "A Trojan Horse mechanism for the spread of visna virus in monocytes". Virology. 147 (1): 231–6. doi:10.1016/0042-6822(85)90246-6. PMID   2998068.
  44. ↑ Chen YC, Wang SY (October 2002). "Activation of terminally differentiated human monocytes/macrophages by dengue virus: productive infection, hierarchical production of innate cytokines and chemokines, and the synergistic effect of lipopolysaccharide". Journal of Virology. 76 (19): 9877–87. doi:10.1128/JVI.76.19.9877-9887.2002. PMC   136495 . PMID   12208965.
  45. ↑ Witayathawornwong P (January 2005). "Fatal dengue encephalitis" (PDF). The Southeast Asian Journal of Tropical Medicine and Public Health. 36 (1): 200–2. PMID   15906668. Archived from the original (PDF) on 24 July 2011.
  46. ↑ Rodenhuis-Zybert IA, Wilschut J, Smit JM (August 2010). "Dengue virus life cycle: viral and host factors modulating infectivity". Cellular and Molecular Life Sciences. 67 (16): 2773–86. doi:10.1007/s00018-010-0357-z. PMC   11115823 . PMID   20372965. S2CID   4232236.
  47. ↑ Guzman MG, Halstead SB, Artsob H, Buchy P, Farrar J, Gubler DJ, et al. (December 2010). "Dengue: a continuing global threat". Nature Reviews. Microbiology. 8 (12 Suppl): S7-16. doi:10.1038/nrmicro2460. PMC   4333201 . PMID   21079655.
  48. ↑ Dejnirattisai W, Jumnainsong A, Onsirisakul N, Fitton P, Vasanawathana S, Limpitikul W, et al. (May 2010). "Cross-reacting antibodies enhance dengue virus infection in humans". Science. 328 (5979): 745–8. Bibcode:2010Sci...328..745D. doi:10.1126/science.1185181. PMC   3837288 . PMID   20448183.
  49. ↑ Modhiran N, Kalayanarooj S, Ubol S (December 2010). "Subversion of innate defenses by the interplay between DENV and pre-existing enhancing antibodies: TLRs signaling collapse". PLOS Neglected Tropical Diseases. 4 (12). PLOS ONE: e924. doi: 10.1371/journal.pntd.0000924 . PMC   3006139 . PMID   21200427.
  50. ↑ Guzman MG (2000). "Dr. Guzman et al. Respond to Dr. Vaughn". American Journal of Epidemiology. 152 (9): 804. doi: 10.1093/aje/152.9.804 .
  51. 1 2 3 Willey S, Aasa-Chapman MM, O'Farrell S, Pellegrino P, Williams I, Weiss RA, Neil SJ (March 2011). "Extensive complement-dependent enhancement of HIV-1 by autologous non-neutralising antibodies at early stages of infection". Retrovirology. 8: 16. doi: 10.1186/1742-4690-8-16 . PMC   3065417 . PMID   21401915.
  52. ↑ Levy JA (2007). HIV and the pathogenesis of AIDS. Wiley-Blackwell. p. 247. ISBN   978-1-55581-393-2.
  53. 1 2 Yu Q, Yu R, Qin X (September 2010). "The good and evil of complement activation in HIV-1 infection". Cellular & Molecular Immunology. 7 (5): 334–40. doi:10.1038/cmi.2010.8. PMC   4002684 . PMID   20228834.
  54. 1 2 Gras GS, Dormont D (January 1991). "Antibody-dependent and antibody-independent complement-mediated enhancement of human immunodeficiency virus type 1 infection in a human, Epstein-Barr virus-transformed B-lymphocytic cell line". Journal of Virology. 65 (1): 541–5. doi:10.1128/JVI.65.1.541-545.1991. PMC   240554 . PMID   1845908.
  55. ↑ Bouhlal H, Chomont N, Réquena M, Nasreddine N, Saidi H, Legoff J, et al. (January 2007). "Opsonization of HIV with complement enhances infection of dendritic cells and viral transfer to CD4 T cells in a CR3 and DC-SIGN-dependent manner". Journal of Immunology. 178 (2): 1086–95. doi: 10.4049/jimmunol.178.2.1086 . PMID   17202372.
  56. ↑ Bouhlal H, Chomont N, Haeffner-Cavaillon N, Kazatchkine MD, Belec L, Hocini H (September 2002). "Opsonization of HIV-1 by semen complement enhances infection of human epithelial cells". Journal of Immunology. 169 (6): 3301–6. doi: 10.4049/jimmunol.169.6.3301 . PMID   12218150.
  57. ↑ Subbramanian RA, Xu J, Toma E, Morisset R, Cohen EA, Menezes J, Ahmad A (June 2002). "Comparison of human immunodeficiency virus (HIV)-specific infection-enhancing and -inhibiting antibodies in AIDS patients". Journal of Clinical Microbiology. 40 (6): 2141–6. doi:10.1128/JCM.40.6.2141-2146.2002. PMC   130693 . PMID   12037078.
  58. ↑ Beck Z, Prohászka Z, Füst G (June 2008). "Traitors of the immune system-enhancing antibodies in HIV infection: their possible implication in HIV vaccine development". Vaccine. 26 (24): 3078–85. doi:10.1016/j.vaccine.2007.12.028. PMC   7115406 . PMID   18241961.
  59. ↑ Robinson WE, Montefiori DC, Mitchell WM (April 1990). "Complement-mediated antibody-dependent enhancement of HIV-1 infection requires CD4 and complement receptors". Virology. 175 (2): 600–4. doi:10.1016/0042-6822(90)90449-2. PMID   2327077.
  60. ↑ Gilbert PB, Peterson ML, Follmann D, Hudgens MG, Francis DP, Gurwith M, et al. (March 2005). "Correlation between immunologic responses to a recombinant glycoprotein 120 vaccine and incidence of HIV-1 infection in a phase 3 HIV-1 preventive vaccine trial". The Journal of Infectious Diseases. 191 (5): 666–77. doi: 10.1086/428405 . PMID   15688279.
  61. ↑ Takada A, Kawaoka Y (2003). "Antibody-dependent enhancement of viral infection: molecular mechanisms and in vivo implications". Reviews in Medical Virology. 13 (6): 387–98. doi:10.1002/rmv.405. PMID   14625886. S2CID   9755341.
  62. ↑ Takada A, Feldmann H, Ksiazek TG, Kawaoka Y (July 2003). "Antibody-dependent enhancement of Ebola virus infection". Journal of Virology. 77 (13): 7539–44. doi:10.1128/JVI.77.13.7539-7544.2003. PMC   164833 . PMID   12805454.
  63. ↑ Kinchen JM, Ravichandran KS (October 2008). "Phagosome maturation: going through the acid test". Nature Reviews. Molecular Cell Biology. 9 (10): 781–95. doi:10.1038/nrm2515. PMC   2908392 . PMID   18813294.
  64. ↑ Yates RM, Hermetter A, Russell DG (May 2005). "The kinetics of phagosome maturation as a function of phagosome/lysosome fusion and acquisition of hydrolytic activity". Traffic. 6 (5): 413–20. doi: 10.1111/j.1600-0854.2005.00284.x . PMID   15813751. S2CID   24021382.
  65. ↑ Ong EZ, Zhang SL, Tan HC, Gan ES, Chan KR, Ooi EE (January 2017). "Dengue virus compartmentalization during antibody-enhanced infection". Scientific Reports. 7 (1): 40923. Bibcode:2017NatSR...740923O. doi:10.1038/srep40923. PMC   5234037 . PMID   28084461.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.