Interferon-induced transmembrane protein 2

Last updated
IFITM2
Identifiers
Aliases IFITM2 , 1-8D, DSPA2c, interferon induced transmembrane protein 2
External IDs OMIM: 605578 MGI: 1933382 HomoloGene: 74574 GeneCards: IFITM2
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006435

NM_030694

RefSeq (protein)

NP_006426

NP_109619

Location (UCSC) Chr 11: 0.3 – 0.31 Mb Chr 7: 140.53 – 140.54 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Interferon-induced transmembrane protein 2 is a protein that in humans is encoded by the IFITM2 gene. [5] IFITM1 is a member of the IFITM family (Interferon-induced transmembrane protein) which is encoded by IFITM genes.

Contents

As the name implies, these genes are induced by interferon and form part of its signaling pathway. In the absence of interferon stimulation, IFITM proteins can express broadly in tissues and cell lines. In humans, IFITM1, IFITM2 and IFITM3 are able to express in different tissues and cells while the expression of IFITM5 is limited to osteoblasts. [6]

Antiviral function

IFITM proteins have been identified as antiviral restriction factors that block the early stages of viral replication. [7] They inhibit influenza A virus replication, [8] and infection with a wide range of other enveloped viruses [9]

Related Research Articles

<span class="mw-page-title-main">Defective interfering particle</span>

Defective interfering particles (DIPs), also known as defective interfering viruses, are spontaneously generated virus mutants in which a critical portion of the particle's genome has been lost due to defective replication or non-homologous recombination. The mechanism of their formation is presumed to be as a result of template-switching during replication of the viral genome, although non-replicative mechanisms involving direct ligation of genomic RNA fragments have also been proposed. DIPs are derived from and associated with their parent virus, and particles are classed as DIPs if they are rendered non-infectious due to at least one essential gene of the virus being lost or severely damaged as a result of the defection. A DIP can usually still penetrate host cells, but requires another fully functional virus particle to co-infect a cell with it, in order to provide the lost factors.

<span class="mw-page-title-main">TRIM5alpha</span>

Tripartite motif-containing protein 5 also known as RING finger protein 88 is a protein that in humans is encoded by the TRIM5 gene. The alpha isoform of this protein, TRIM5α, is a retrovirus restriction factor, which mediates a species-specific early block to retrovirus infection.

<span class="mw-page-title-main">CCL5</span> Mammalian protein found in Homo sapiens

Chemokine ligand 5 is a protein which in humans is encoded by the CCL5 gene. The gene has been discovered in 1990 by in situ hybridisation and it is localised on 17q11.2-q12 chromosome. It is also known as RANTES. RANTES was first described by Dr. Tom Schall who named the protein, the original source of the name Rantes was from the Argentine movie Man Facing Southeast about an alien who shows up in a mental ward who was named Rantés, the rather clunky acronym was only made to fit the name.

<span class="mw-page-title-main">STAT2</span> Protein-coding gene in Homo sapiens

Signal transducer and activator of transcription 2 is a protein that in humans is encoded by the STAT2 gene. It is a member of the STAT protein family. This protein is critical to the biological response of type I interferons (IFNs). STAT2 sequence identity between mouse and human is only 68%.

NSP1 (NS53), the product of rotavirus gene 5, is a nonstructural RNA-binding protein that contains a cysteine-rich region and is a component of early replication intermediates. RNA-folding predictions suggest that this region of the NSP1 mRNA can interact with itself, producing a stem-loop structure similar to that found near the 5'-terminus of the NSP1 mRNA.

<span class="mw-page-title-main">CD81</span>

CD81 molecule, also known as CD81, is a protein which in humans is encoded by the CD81 gene. It is also known as 26 kDa cell surface protein, TAPA-1, and Tetraspanin-28 (Tspan-28).

<span class="mw-page-title-main">IFI16</span> Protein-coding gene in the species Homo sapiens

Gamma-interferon-inducible protein Ifi-16 (Ifi-16) also known as interferon-inducible myeloid differentiation transcriptional activator is a protein that in humans is encoded by the IFI16 gene.

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

Mitochondrial antiviral-signaling protein (MAVS) is a protein that is essential for antiviral innate immunity. MAVS is located in the outer membrane of the mitochondria, peroxisomes, and mitochondrial-associated endoplasmic reticulum membrane (MAM). Upon viral infection, a group of cytosolic proteins will detect the presence of the virus and bind to MAVS, thereby activating MAVS. The activation of MAVS leads the virally infected cell to secrete cytokines. This induces an immune response which kills the host's virally infected cells, resulting in clearance of the virus.

<span class="mw-page-title-main">IFITM1</span> Protein-coding gene in the species Homo sapiens

Interferon-induced transmembrane protein 1 is a protein that in humans is encoded by the IFITM1 gene. IFITM1 has also recently been designated CD225. This protein has several additional names: fragilis, IFI17 [interferon-induced protein 17], 9-27 [Interferon-inducible protein 9-27] and Leu13.

<span class="mw-page-title-main">TRIM22</span> Protein-coding gene in the species Homo sapiens

Tripartite motif-containing 22, also known as TRIM22, is a protein which in humans is encoded by the TRIM22 gene.

<span class="mw-page-title-main">IFITM3</span> Protein-coding gene in the species Homo sapiens

Interferon-induced transmembrane protein 3 (IFITM3) is a protein that in humans is encoded by the IFITM3 gene. It plays a critical role in the immune system's defense against Swine Flu, where heightened levels of IFITM3 keep viral levels low, and the removal of IFITM3 allows the virus to multiply unchecked. This observation has been further advanced by a recent study from Paul Kellam's lab that shows that a single nucleotide polymorphism in the human IFITM3 gene purported to increase influenza susceptibility is overrepresented in people hospitalised with pandemic H1N1. The prevalence of this mutation is thought to be approximately 1/400 in European populations.

<span class="mw-page-title-main">Tetherin</span> Mammalian protein found in Homo sapiens

Tetherin, also known as bone marrow stromal antigen 2, is a lipid raft associated protein that in humans is encoded by the BST2 gene. In addition, tetherin has been designated as CD317. This protein is constitutively expressed in mature B cells, plasma cells and plasmacytoid dendritic cells, and in many other cells, it is only expressed as a response to stimuli from IFN pathway.

<span class="mw-page-title-main">IFIT3</span> Protein-coding gene in the species Homo sapiens

Interferon-induced protein with tetratricopeptide repeats 3, also known as interferon-stimulated gene 49 (ISG49), is a protein that in humans is encoded by the IFIT3 gene. It plays a part in the innate immune response to viruses in response to type I interferon signaling.

<span class="mw-page-title-main">Vpu protein</span>

Vpu is an accessory protein that in HIV is encoded by the vpu gene. Vpu stands for "Viral Protein U". The Vpu protein acts in the degradation of CD4 in the endoplasmic reticulum and in the enhancement of virion release from the plasma membrane of infected cells. Vpu induces the degradation of the CD4 viral receptor and therefore participates in the general downregulation of CD4 expression during the course of HIV infection. Vpu-mediated CD4 degradation is thought to prevent CD4-Env binding in the endoplasmic reticulum to facilitate proper Env assembly into virions. It is found in the membranes of infected cells, but not the virus particles themselves.

<span class="mw-page-title-main">Hepatitis C virus nonstructural protein 2</span>

Nonstructural protein 2 (NS2) is a viral protein found in the hepatitis C virus. It is also produced by influenza viruses, and is alternatively known as the nuclear export protein (NEP).

<span class="mw-page-title-main">Antiviral protein</span>

Antiviral proteins are proteins that are induced by human or animal cells to interfere with viral replication. These proteins are isolated to inhibit the virus from replicating in a host's cells and stop it from spreading to other cells. The Pokeweed antiviral protein and the Zinc-Finger antiviral protein are two major antiviral proteins that have undergone several tests for viruses, including HIV and influenza.

RIG-I-like receptors are a type of intracellular pattern recognition receptor involved in the recognition of viruses by the innate immune system. RIG-I is the best characterized receptor within the RIG-I like receptor (RLR) family. Together with MDA5 and LGP2, this family of cytoplasmic pattern recognition receptors (PRRs) are sentinels for intracellular viral RNA that is a product of viral infection. The RLR receptors provide frontline defence against viral infections in most tissues.

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

Radical S-adenosyl methionine domain-containing protein 2 is a protein that in humans is encoded by the RSAD2 gene. RSAD2 is a multifunctional protein in viral processes that is an interferon stimulated gene. It has been reported that viperin could be induced by either IFN-dependent or IFN-independent pathways and certain viruses may use viperin to increase their infectivity.

In molecular biology, the protein family Dispanin is another name for Interferon-induced transmembrane protein (IFITM). This refers to a family of protein domains which have a specific formation, or in other words, topology containing two alpha helices in within the cell membrane which are called two transmembrane proteins. This includes proteins such as CD225. The function of this protein family is to inhibit cell invasion of many harmful, pathogenic viruses, such as HIV. Henceforth, they are being intensively studied in the hope of drug discovery. They mediate the immune response by interferons.

Paul Darren Bieniasz is a British-American virologist whose main area of research is HIV/AIDS. He is currently a professor of retrovirology at the Rockefeller University. He received the 2015 KT Jeang Retrovirology Prize and the 2010 Eli Lilly and Company Research Award. Bieniasz has been a Howard Hughes Medical Institute investigator since 2008.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000185201 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000060591 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: Interferon induced transmembrane protein 2" . Retrieved 2016-02-21.
  6. Tanaka SS, Yamaguchi YL, Tsoi B, Lickert H, Tam PP (December 2005). "IFITM/Mil/fragilis family proteins IFITM1 and IFITM3 play distinct roles in mouse primordial germ cell homing and repulsion". Dev. Cell. 9 (6): 745–56. doi: 10.1016/j.devcel.2005.10.010 . PMID   16326387.
  7. Li K, Markosyan RM, Zheng YM, Golfetto O, Bungart B, Li M, Ding S, He Y, Liang C, Lee JC, Gratton E, Cohen FS, Liu SL (January 2013). "IFITM proteins restrict viral membrane hemifusion". PLOS Pathog. 9 (1): e1003124. doi: 10.1371/journal.ppat.1003124 . PMC   3554583 . PMID   23358889.
  8. Feeley EM, Sims JS, John SP, Chin CR, Pertel T, Chen LM, Gaiha GD, Ryan BJ, Donis RO, Elledge SJ, Brass AL (October 2011). "IFITM3 inhibits influenza A virus infection by preventing cytosolic entry". PLOS Pathog. 7 (10): e1002337. doi: 10.1371/journal.ppat.1002337 . PMC   3203188 . PMID   22046135.
  9. Brass AL, Huang IC, Benita Y, John SP, Krishnan MN, Feeley EM, Ryan BJ, Weyer JL, van der Weyden L, Fikrig E, Adams DJ, Xavier RJ, Farzan M, Elledge SJ (December 2009). "The IFITM proteins mediate cellular resistance to influenza A H1N1 virus, West Nile virus, and dengue virus". Cell. 139 (7): 1243–54. doi:10.1016/j.cell.2009.12.017. PMC   2824905 . PMID   20064371.

Further reading