Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Virol. 2005 Jun;79(12):7419-30.

A new class of receptor for herpes simplex virus has heptad repeat motifs that are common to membrane fusion proteins.

Author information

  • 1Department of Microbiology and Immunology, University of Michigan School of Medicine, 6736 Medical Sciences II, 0620, Ann Arbor, MI 48109-0620, USA.

Abstract

We isolated a human cDNA by expression cloning and characterized its gene product as a new human protein that enables entry and infection of herpes simplex virus (HSV). The gene, designated hfl-B5, encodes a type II cell surface membrane protein, B5, that is broadly expressed in human primary tissue and cell lines. It contains a high-scoring heptad repeat at the extracellular C terminus that is predicted to form an alpha-helix for coiled coils like those in cellular SNAREs or in some viral fusion proteins. A synthetic 30-mer peptide that has the same sequence as the heptad repeat alpha-helix blocks HSV infection of B5-expressing porcine cells and human HEp-2 cells. Transient expression of human B5 in HEp-2 cells results in increased polykarocyte formation even in the absence of viral proteins. The B5 protein fulfills all criteria as a receptor or coreceptor for HSV entry. Use by HSV of a human cellular receptor, such as B5, that contains putative membrane fusion domains provides an example where a pathogenic virus with broad tropism has usurped a widely expressed cellular protein to function in infection at events that lead to membrane fusion.

PMID:
15919898
[PubMed - indexed for MEDLINE]
PMCID:
PMC1143644
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk