Format

Send to

Choose Destination
Trends Microbiol. 2011 Aug;19(8):389-99. doi: 10.1016/j.tim.2011.03.005. Epub 2011 Apr 20.

Modes of paramyxovirus fusion: a Henipavirus perspective.

Author information

1
Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, USA. bleebhl@ucla.edu

Abstract

Henipavirus is a new genus of Paramyxoviridae that uses protein-based receptors (ephrinB2 and ephrinB3) for virus entry. Paramyxovirus entry requires the coordinated action of the fusion (F) and attachment viral envelope glycoproteins. Receptor binding to the attachment protein triggers F to undergo a conformational cascade that results in membrane fusion. The accumulation of structural and functional studies on many paramyxoviral fusion and attachment proteins, including the recent elucidation of structures of Nipah virus (NiV) and Hendra virus (HeV) G glycoproteins bound and unbound to cognate ephrinB receptors, indicate that henipavirus entry and fusion could differ mechanistically from paramyxoviruses that use glycan-based receptors.

PMID:
21511478
PMCID:
PMC3264399
DOI:
10.1016/j.tim.2011.03.005
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center