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PMID: 10698932 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A new class of fusion-associated small transmembrane (FAST) proteins encoded by the non-enveloped fusogenic reoviruses.

The EMBO journal ·Vol. 19 ·No. 5 ·2000-03-01 ·Pages 902-12

Shmulevitz M, Duncan R

Abstract

The non-enveloped fusogenic avian and Nelson Bay reoviruses encode homologous 10 kDa non-structural transmembrane proteins. The p10 proteins localize to the cell surface of transfected cells in a type I orientation and induce efficient cell-cell fusion. Mutagenic studies revealed the importance of conserved sequence-predicted structural motifs in the membrane association and fusogenic properties of p10. These motifs included a centrally located transmembrane domain, a conserved cytoplasmic basic region, a small hydrophobic motif in the N-terminal domain and four conserved cysteine residues. Functional analysis indicated that the extreme C-terminus of p10 functions in a sequence-independent manner to effect p10 membrane localization, while the N-terminal domain displays a sequence-dependent effect on the fusogenic property of p10. The small size, unusual arrangement of structural motifs and lack of any homologues in previously described membrane fusion proteins suggest that the fusion-associated small transmembrane (FAST) proteins of reovirus represent a new class of membrane fusion proteins.

MeSH Terms
Amino Acid Sequence Animals Membrane Proteins/genetics,metabolism Molecular Sequence Data Reoviridae/physiology Viral Fusion Proteins/genetics,metabolism Viral Proteins/genetics,metabolism Virus Replication
Chemicals
Membrane Proteins Viral Fusion Proteins Viral Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Shmulevitz M
Department of Microbiology, Faculty of Medicine, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7.
Duncan R
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/19.5.902
Published
2000-03-01
Pages
902-12
Language
English
Region
England
NLM ID
8208664
PMCID
PMC305630
Subset
IM
External Links
PubMed source DOI: 10.1093/emboj/19.5.902 PMC Full Text View journal details
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