ArticleJournal of virology2005
A new class of receptor for herpes simplex virus has heptad repeat motifs that are common to membrane fusion proteins.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed, 31 citations in OpenAlex.
- Distribution of cellular HSV-1 receptor expression in human brain.Journal of neurovirology · 2017Article
- Biologically active and antimicrobial peptides from plants.BioMed research international · 2015Review
- Early events in herpes simplex virus lifecycle with implications for an infection of lifetime.The open virology journal · 2012Article
- Herpes simplex virus infects most cell types in vitro: clues to its success.Virology journal · 2011Review
- HSV usurps eukaryotic initiation factor 3 subunit M for viral protein translation: novel prevention target.PloS one · 2010Article
- Viral entry mechanisms: cellular and viral mediators of herpes simplex virus entry.The FEBS journal · 2009Review
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- Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection.Antimicrobial agents and chemotherapy · 2009Article
- Formation and reversible dissociation of coiled coil of peptide to the C-terminus of the HSV B5 protein: a time-resolved spectroscopic analysis.Biophysical journal · 2007Article
- Reconstitution reveals the functional core of mammalian eIF3.The EMBO journal · 2007Article
- Nectin-2-mediated entry of a syncytial strain of herpes simplex virus via pH-independent fusion with the plasma membrane of Chinese hamster ovary cells.Virology journal · 2006Article
- Peptide antimicrobial agents.Clinical microbiology reviews · 2006Review
- Triggering and visualizing the aggregation and fusion of lipid membranes in microfluidic chambers.Biophysical journal · 2006Article
- The C terminus of the B5 receptor for herpes simplex virus contains a functional region important for infection.Journal of virology · 2005Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.