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InterPro: IPR000936 Alphavirus E2 glycoprotein
Protein matches
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UniProtKB Matches: 1624 proteins |
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Accession
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IPR000936 Alpha_E2_glycop |
Type
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Family |
Signatures
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GO Term annotation
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Function
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GO:0005198 structural molecule activity
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Component
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GO:0019028 viral capsid
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Alphaviruses are enveloped RNA viruses that use arthropods such as mosquitoes for transmission to their vertebrate hosts, and include Semliki Forest and Sindbis viruses [1]. Alphaviruses consist of three structural proteins: the core nucleocapsid protein C, and the envelope proteins P62 and E1 ( IPR002548) that associate as a heterodimer. The viral membrane-anchored surface glycoproteins are responsible for receptor recognition and entry into target cells through membrane fusion. The proteolytic maturation of P62 into E2 and E3 ( IPR002533) causes a change in the viral surface. Together the E1, E2, and sometimes E3 glycoprotein "spikes" form an E1/E2 dimer or an E1/E2/E3 trimer, where E2 extends from the centre to the vertices, E1 fills the space between the vertices, and E3, if present, is at the distal end of the spike [2, 3]. Upon exposure of the virus to the acidity of the endosome, E1 dissociates from E2 to form an E1 homotrimer, which is necessary for the fusion step to drive the cellular and viral membranes together [4]. This entry represents the alphaviral E2 glycoprotein. The E2 glycoprotein functions to interact with the nucleocapsid through its cytoplasmic domain, while its ectodomain is responsible for binding a cellular receptor.
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Database links
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Publications
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1.
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Weaver SC, Barrett AD.
Transmission cycles, host range, evolution and emergence of arboviral disease.
Nat. Rev. Microbiol. 2 789-801 2004
[PubMed: 15378043]
http://dx.doi.org/10.1038/nrmicro1006
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2.
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Venien-Bryan C, Fuller SD.
The organization of the spike complex of Semliki Forest virus.
J. Mol. Biol. 236 572-83 1994
[PubMed: 8107141]
http://dx.doi.org/10.1006/jmbi.1994.1166
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3.
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Paredes AM, Heidner H, Thuman-Commike P, Prasad BV, Johnston RE, Chiu W.
Structural localization of the E3 glycoprotein in attenuated Sindbis virus mutants.
J. Virol. 72 1534-41 1998
[PubMed: 9445057]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=9445057&action=stream&blobtype=pdf
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4.
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Lescar J, Roussel A, Wien MW, Navaza J, Fuller SD, Wengler G, Wengler G, Rey FA.
The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH.
Cell 105 137-48 2001
[PubMed: 11301009]
http://dx.doi.org/10.1016/S0092-8674(01)00303-8
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Additional Reading
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Carleton M, Lee H, Mulvey M, Brown DT.
Role of glycoprotein PE2 in formation and maturation of the Sindbis virus spike.
J. Virol. 71 1997 1558-66
[PubMed: 8995682]
http://jvi.asm.org/cgi/content/abstract/71/2/1558
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Cheng RH, Kuhn RJ, Olson NH, Rossmann MG, Choi HK, Smith TJ, Baker TS.
Nucleocapsid and glycoprotein organization in an enveloped virus.
Cell 80 1995 621-30
[PubMed: 7867069]
http://dx.doi.org/10.1016/0092-8674(95)90516-2
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Barth BU, Garoff H.
The nucleocapsid-binding spike subunit E2 of Semliki Forest virus requires complex formation with the E1 subunit for activity.
J. Virol. 71 1997 7857-65
[PubMed: 9311874]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=9311874&action=stream&blobtype=pdf
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Joe AK, Foo HH, Kleeman L, Levine B.
The transmembrane domains of Sindbis virus envelope glycoproteins induce cell death.
J. Virol. 72 1998 3935-43
[PubMed: 9557679]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=9557679&action=stream&blobtype=pdf
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InterPro 23.1
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