Vesiculovirus matrix proteins

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Vesiculo_matrix
PDB 1lg7 EBI.jpg
crystal structure of vesicular stomatitis virus matrix protein
Identifiers
SymbolVesiculo_matrix
Pfam PF06326
InterPro IPR009397
SCOP2 1lg7 / SCOPe / SUPFAM
OPM superfamily 381
OPM protein 1lg7

The family of vesiculovirus matrix proteins consists of several matrix proteins of the vesicular stomatitis virus, also known as VSIV or VSV. The matrix (M) protein of the virus causes many of the cytopathic effects of VSV, including an inhibition of host gene expression and the induction of cell rounding. It has been shown that M protein also induces apoptosis in the absence of other viral components. It is thought that the activation of apoptotic pathways causes the inhibition of host gene expression and cell rounding by M protein. [1]

Contents

Function

These proteins play a major role in assembly and budding of VSIV virions. [2] Their main role is to aid virus assembly. They starts by shutting off host cell transcription by inhibiting mRNA nuclear export through direct interaction with the host RAE1-NUP98 complex. This inhibits interferon signaling and thus establishment of antiviral state in virus infected cells. In turn, this induces cell-rounding, cytoskeleton disorganization and apoptosis in infected cell. Enveloped viruses acquire their membrane by budding at a membrane of their host cell. [3]

Structure

The structure of these matrix proteins has revealed a single-globular domain with a new fold. The N-terminal part consists of a large five-stranded anti-parallel beta-sheet packed against two alpha-helices; the C-terminal part comprises a small two stranded anti-parallel beta-sheet and an alpha-helix.

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Indiana vesiculovirus, formerly Vesicular stomatitis Indiana virus is a virus in the family Rhabdoviridae; the well-known Rabies lyssavirus belongs to the same family. VSIV can infect insects, cattle, horses and pigs. It has particular importance to farmers in certain regions of the world where it infects cattle. This is because its clinical presentation is identical to the very important foot and mouth disease virus.

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Rubella virus Species of virus

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<i>Baculoviridae</i> Family of viruses

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<i>Myxoma virus</i> Species of virus

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An alveolar macrophage, pulmonary macrophage, is a type of macrophage, a professional phagocyte, found in the airways and at the level of the alveoli in the lungs, but separated from their walls.

Mitochondrial antiviral-signaling protein Protein-coding gene in the species Homo sapiens

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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.

Herpesvirus glycoprotein B

Herpesvirus glycoprotein B is a viral glycoprotein that is involved in the viral cell entry of Herpes simplex virus (HSV). Herpesviruses have a lipid bilayer, called the envelope, which contains twelve surface glycoproteins. For infectivity to be attained, the double stranded DNA genome of HSV must enter the host cell through means of fusion of its envelope with the cellular membrane or via endocytosis. Other viral glycoproteins involved in the process of viral cell entry include gC, gB, gD, gH, and gL, but only gC, gB, gD, and gH are required for the fusion of the HSV's envelope with the cellular membrane. It can be noted that all herpesviruses have glycoproteins gB, gH, and gL.

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VP40

In molecular biology, VP40 is the name of a viral matrix protein. Most commonly it is found in the Ebola virus (EBOV), a type of non-segmented, negative-strand RNA virus. Ebola virus causes a severe and often fatal haemorrhagic fever in humans, known as Ebola virus disease. The virus matrix protein VP40 is a major structural protein that plays a central role in virus assembly and budding at the plasma membrane of infected cells. VP40 proteins work by associating with cellular membranes, interacting with the cytoplasmic tails of glycoproteins and binding to the ribonucleoprotein complex.

Picornain 3C

Picornain 3C is a protease found in picornaviruses, which cleaves peptide bonds of non-terminal sequences. Picornain 3C’s endopeptidase activity is primarily responsible for the catalytic process of selectively cleaving Gln-Gly bonds in the polyprotein of poliovirus and with substitution of Glu for Gln, and Ser or Thr for Gly in other picornaviruses. Picornain 3C are cysteine proteases related by amino acid sequence to trypsin-like serine proteases. Picornain 3C is encoded by enteroviruses, rhinoviruses, aphtoviruses and cardioviruses. These genera of picoviruses cause a wide range of infections in humans and mammals.

David M. Knipe is the Higgins Professor of Microbiology and Molecular Genetics in the Department of Microbiology at the Harvard Medical School in Boston, Massachusetts and co-chief editor of the reference book Fields Virology. He returned to the Chair of the Program in Virology at Harvard Medical School in 2019, having previously held the position from 2004 through 2016 and served as interim Co-Chair of the Microbiology and Immunobiology Department from 2016 through 2018.

Early 35 kDa protein Anti-apoptotic viral protein

The Early 35 kDa protein, or P35 in short, is a baculoviral protein that inhibits apoptosis in the cells infected by the virus. Although baculoviruses infect only invertebrates in nature, ectopic expression of P35 in vertebrate animals and cells also results in inhibition of apoptosis, thus indicating a universal mechanism. P35 has been shown to be a caspase inhibitor with a very wide spectrum of activity both in regard to inhibited caspase types and to species in which the mechanism is conserved.

References

  1. Kopecky SA, Lyles DS (May 2003). "The cell-rounding activity of the vesicular stomatitis virus matrix protein is due to the induction of cell death". J. Virol. 77 (9): 5524–8. doi:10.1128/jvi.77.9.5524-5528.2003. PMC   153969 . PMID   12692256.
  2. Gaudier, Martin; Gaudin, Yves; Knossow, Marcel (2002-06-17). "Crystal structure of vesicular stomatitis virus matrix protein". The EMBO Journal. 21 (12): 2886–2892. doi:10.1093/emboj/cdf284. ISSN   0261-4189. PMC   126044 . PMID   12065402.
  3. Solon J, Gareil O, Bassereau P, Gaudin Y (2005). "Membrane deformations induced by the matrix protein of vesicular stomatitis virus in a minimal system". J Gen Virol. 86 (Pt 12): 3357–63. doi: 10.1099/vir.0.81129-0 . PMID   16298982.
This article incorporates text from the public domain Pfam and InterPro: IPR009397