Erica Ollmann Saphire is an American structural biologist and immunologist and a professor at the La Jolla Institute for Immunology. She investigates the structural biology of viruses that cause hemorrhagic fever such as Ebola, Sudan, Marburg, Bundibugyo, and Lassa.
Saphire has served as president and CEO of La Jolla Institute for Immunology since 2021. [1]
Saphire earned a Bachelor of Arts in biochemistry and cell biology from Rice University in 1993. She then moved to Scripps Research, where she earned a PhD in molecular biology in 2000. [2] Her doctoral research focused on the crystal structure of a neutralizing antibody against HIV-1. [3] She was an avid rugby player throughout college and graduate school, and toured twice with the United States women's national rugby union team. [4]
After an immunology postdoctoral fellowship at Scripps Research, Saphire joined the faculty in the department of immunology as an assistant professor in 2003. She was promoted to associate professor in 2008 and full professor in 2012. [2] In 2019, joined the faculty at the La Jolla Institute for Immunology. [5]
Saphire solved the first structure of the entire human IgG [6] . The hexameric array predicted the assembly by which IgG could recruit C1q and launch the complement cascade [7] , which Saphire confirmed by obtaining the cryoEM structure of the C1q-IgG complex and hexameric IgG preparations.
Saphire is best known for her research on Ebola virus and other causes of viral hemorrhagic fever. [5] She was the first to discover the structure of the Ebola virus surface glycoprotein [8] and predicted that the Ebola virus receptor was located in the endosome rather than on the cell surface. Later, she showed that the Ebola virus VP40 matrix protein can fold into multiple distinct structures. [3] In 2024, Saphire used in situ cryo-electron tomography to illuminate Ebola virus replication factories inside living cells revealing a hitherto unresolved third and outer layer of the nucleoprotein. [9] Her laboratory has also discovered the structure of the glycoproteins of Sudan virus, Marburg virus, Bundibugyo virus, Lassa virus and LCMV. [10] On field work in West Africa, she followed rodents to study how they spread viruses such as Ebola and Lassa. [5] Saphire attracted national media attention in 2014 when she launched a crowdfunding appeal to raise funds for equipment to assist in research to fight Ebola virus. [5] [11]
In recent work, Saphire determined the cryo-electron microscopy structure of the measles virus fusion protein in complex with an antibody and determined that the antibody can trap the fusion protein in an intermediate state, thus halting fusion [12] .
Saphire directs the Viral Hemorrhagic Fever Immunotherapeutic Consortium (VIC) [10] and is a strong advocate for strategic collaborations to rapidly develop treatments for Ebola and other severe threats. [13] In 2020, Saphire was named director of the Coronavirus Immunotherapy Consortium (CoVIC), an international effort to evaluate human antibodies against the novel coronavirus, SARS-CoV-2. [14] [15] Her lab also co-led research into COVID-19 mutations with scientists at the Los Alamos National Laboratory. [16] Saphire is also spearheading "America's SHIELD:Strategic Herpesvirus Immune Evasion and Latency Defense" [17] as part of ARPA-H's Antigens Predicted for Broad Viral Efficacy through Computational Experimentation (APECx) program.
In 2021, Saphire was appointed president and CEO of La Jolla Institute for Immunology. She succeeded Dr. Mitchell Kronenberg, who had served as institute president since 2003. Saphire is the institute's fifth president and is the first woman to serve in that role. [1]
Saphire received the Presidential Early Career Award for Scientists and Engineers and the Global Virus Network's Gallo Award for Scientific Excellence and Leadership. [10] She received the American Society for Biochemistry and Molecular Biology's Young Investigator Award in 2015, [3] the Pantheon Award for Academia, Non-Profit, & Research in 2023, [18] the Marion Spencer Fay Award in 2023 [19] and the Bert & Natalie Vallee Award in Biomedical Science (2023). [20]
An antibody (Ab) or immunoglobulin (Ig) is a large, Y-shaped protein belonging to the immunoglobulin superfamily which is used by the immune system to identify and neutralize antigens such as bacteria and viruses, including those that cause disease. Antibodies can recognize virtually any size antigen with diverse chemical compositions from molecules. Each antibody recognizes one or more specific antigens. Antigen literally means "antibody generator", as it is the presence of an antigen that drives the formation of an antigen-specific antibody. Each tip of the "Y" of an antibody contains a paratope that specifically binds to one particular epitope on an antigen, allowing the two molecules to bind together with precision. Using this mechanism, antibodies can effectively "tag" a microbe or an infected cell for attack by other parts of the immune system, or can neutralize it directly.
The genus Ebolavirus is a virological taxon included in the family Filoviridae, order Mononegavirales. The members of this genus are called ebolaviruses, and encode their genome in the form of single-stranded negative-sense RNA. The six known virus species are named for the region where each was originally identified: Bundibugyo ebolavirus, Reston ebolavirus, Sudan ebolavirus, Taï Forest ebolavirus, Zaire ebolavirus, and Bombali ebolavirus. The last is the most recent species to be named and was isolated from Angolan free-tailed bats in Sierra Leone. Each species of the genus Ebolavirus has one member virus, and four of these cause Ebola virus disease (EVD) in humans, a type of hemorrhagic fever having a very high case fatality rate. The Reston virus has caused EVD in other primates. Zaire ebolavirus has the highest mortality rate of the ebolaviruses and is responsible for the largest number of outbreaks of the six known species of the genus, including the 1976 Zaire outbreak and the outbreak with the most deaths (2014).
Lassa mammarenavirus (LASV) is an arenavirus that causes Lassa hemorrhagic fever, a type of viral hemorrhagic fever (VHF), in humans and other primates. Lassa mammarenavirus is an emerging virus and a select agent, requiring Biosafety Level 4-equivalent containment. It is endemic in West African countries, especially Sierra Leone, the Republic of Guinea, Nigeria, and Liberia, where the annual incidence of infection is between 300,000 and 500,000 cases, resulting in 5,000 deaths per year.
In immunology, epitope mapping is the process of experimentally identifying the binding site, or epitope, of an antibody on its target antigen. Identification and characterization of antibody binding sites aid in the discovery and development of new therapeutics, vaccines, and diagnostics. Epitope characterization can also help elucidate the binding mechanism of an antibody and can strengthen intellectual property (patent) protection. Experimental epitope mapping data can be incorporated into robust algorithms to facilitate in silico prediction of B-cell epitopes based on sequence and/or structural data.
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.
Ian Andrew Wilson is the Hansen Professor of Structural Biology and chair of the Department of Integrative Structural and Computational Biology at the Scripps Research Institute in San Diego, California, United States.
Kimishige "Kimi" Ishizaka was a Japanese immunologist who, with his wife Teruko Ishizaka, discovered the antibody class Immunoglobulin E (IgE) in 1966–1967. Their work was regarded as a major breakthrough in the understanding of allergy. He was awarded the 1973 Gairdner Foundation International Award and the 2000 Japan Prize for his work in immunology.
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.
La Jolla Institute for Immunology (LJI) is a non-profit research organization in La Jolla, a community of San Diego, California. The institute was founded in 1988. It is located in UC San Diego’s Research Park. The institute researches immunology and immune system diseases. The institute employs 220 M.D.s and Ph.D.s, including 23 faculty members and more than 450 employees. Dr. Erica Ollmann Saphire has served as its president and CEO since 2021.
In molecular biology, hemagglutinins are receptor-binding membrane fusion glycoproteins produced by viruses in the Paramyxoviridae and Orthomyxoviridae families. Hemagglutinins are responsible for binding to receptors on host cells to initiate viral attachment and infection.
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.
Zaire ebolavirus, more commonly known as Ebola virus, is one of six known species within the genus Ebolavirus. Four of the six known ebolaviruses, including EBOV, cause a severe and often fatal hemorrhagic fever in humans and other mammals, known as Ebola virus disease (EVD). Ebola virus has caused the majority of human deaths from EVD, and was the cause of the 2013–2016 epidemic in western Africa, which resulted in at least 28,646 suspected cases and 11,323 confirmed deaths.
Almyra Oveta Fuller was an associate professor of microbiology and immunology at University of Michigan Medical School. She served as the director of the African Studies Center (ASC), faculty in the ASC STEM Initiative at the University of Michigan (U-M) and an adjunct professor at Payne Theological Seminary. Fuller was a virologist and specialized in research of Herpes simplex virus, as well as HIV/AIDS. Fuller and her research team discovered a B5 receptor, advancing the understanding of Herpes simplex virus and the cells it attacks.
Robert A. Lamb was a British-American virologist. He was the Kenneth F. Burgess Professor at Northwestern University and since 1991, an investigator of the Howard Hughes Medical Institute. From 1990 to 2016, he was the John Evans Professor of Molecular and Cellular Biology at Northwestern University.
Yorgo E. Modis is Professor in Virology and Immunology, and a Wellcome Trust Senior Research Fellow at the Department of Medicine, University of Cambridge. He is head of The Modis Lab in the Molecular Immunity Unit at the MRC Laboratory of Molecular Biology. He studies cellular mechanisms of viral gene sensing and silencing. His group employs a diverse set of complementary biophysical approaches including cryo-electron microscopy (cryoEM), X-ray crystallography, solution biophysics, fluorescence microscopy and cell biological approaches to understand the cellular mechanisms of viral gene sensing and silencing in molecular-level detail.
Nancy Jean Sullivan is an American cell biologist researching filovirus immunology and vaccine development. She is a senior investigator and chief of the biodefense research section at the Vaccine Research Center. Her team discovered the monoclonal antibody, mAb114.
David Veesler is a French biochemist and an assistant professor in the Department of Biochemistry at the University of Washington, where his group focuses on the study the structural biology of infectious diseases. His team recently helped determine the structure of the SARS-CoV-2 spike glycoprotein using Cryo-EM techniques, and it is currently trying to identify neutralizing antibodies for SARS-CoV-2 that could be used as a preventative treatment against COVID-19 or as a post-exposure therapy using X-ray crystallography. Veesler is Howard Hughes Medical Investigators.
Katherine Jane Doores is a British biochemist who is a senior lecturer in the School of Immunology & Microbial Sciences at King's College London. During the COVID-19 pandemic Doores studied the levels of antibodies in patients who had suffered from COVID-19.
Elina Zúñiga is an Argentinian Immunologist and Professor of Molecular Biology in the Division of Biological Sciences at the University of California, San Diego. Zúñiga has made critical discoveries regarding host-virus interactions in both acute and chronic infections. Using lymphocytic choriomeningitis models (LCMV) and murine cytomegalovirus models, her laboratory at UCSD studies host immune adaptations in chronic viral disease and methods of viral suppression of the immune system in order to develop novel methods and identify novel targets of anti-viral defence. In 2018, Zúñiga was chosen by the American Association of Immunologists to give the international Vanguard Lecture. Zúñiga is also co-founder of the Global Immunotalks series which she and Carla Rothlin started in 2020 as a means to make cutting-edge immunology research freely available and easily accessible to a global audience.
Spike (S) glycoprotein is the largest of the four major structural proteins found in coronaviruses. The spike protein assembles into trimers that form large structures, called spikes or peplomers, that project from the surface of the virion. The distinctive appearance of these spikes when visualized using negative stain transmission electron microscopy, "recalling the solar corona", gives the virus family its main name.
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