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InterPro: IPR000936 Alphavirus E2 glycoprotein

Protein matchesHelp
UniProtKB
Matches:
1624 proteins
AccessionHelp IPR000936 Alpha_E2_glycop
TypeHelp Family
SignaturesHelp
GO Term annotationHelp
Function GO:0005198 structural molecule activity
Component GO:0019028 viral capsid
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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.

Database linksHelp
Enzyme: EC:3.4.21
PANDIT: PF00943
Blocks: IPB000936

Taxonomic coverageHelp

Example proteinsHelp
P03315 Structural polyprotein

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000930 Peptidase S3, togavirin
IPR002533 Alphavirus E3 spike glycoprotein
IPR009003 Serine/cysteine peptidase, trypsin-like
IPR000936 Alphavirus E2 glycoprotein
IPR002548 Alphavirus E1 glycoprotein
IPR014756 Immunoglobulin E-set
IPR011998 Glycoprotein E, central and dimerisation domain, viral
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. 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
2. 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
3. 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
4. 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

Additional ReadingHelp
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
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
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
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