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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. A new class of receptor for herpes simplex virus has heptad repeat motifs that are common to membrane fusion proteins. Perez, A., Li, Q.X., Perez-Romero, P., Delassus, G., Lopez, S.R., Sutter, S., McLaren, N., Fuller, A.O. J. Virol. (2005) [Pubmed]
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