ArticleJournal of virology2006
Hydrophobic alpha-helices 1 and 2 of herpes simplex virus gH interact with lipids, and their mimetic peptides enhance virus infection and fusion.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 40 citations in OpenAlex.
- Structure-Function Dissection of Pseudorabies Virus Glycoprotein B Fusion Loops.Journal of virology · 2018Article
- Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1.Journal of peptide science : an official publication of the European Peptide Society · 2017Article
- Cell entry mechanisms of HSV: what we have learned in recent years.Future virology · 2015Article
- Interaction domain of glycoproteins gB and gH of Marek's disease virus and identification of an antiviral peptide with dual functions.PloS one · 2013Article
- Structure-based mutational analysis of the highly conserved domain IV of glycoprotein H of pseudorabies virus.Journal of virology · 2012Article
- Review
- Structure-function analysis of varicella-zoster virus glycoprotein H identifies domain-specific roles for fusion and skin tropism.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.Journal of virology · 2011Article
- Fusing structure and function: a structural view of the herpesvirus entry machinery.Nature reviews. Microbiology · 2011Review
- Reevaluating herpes simplex virus hemifusion.Journal of virology · 2010Article
- Herpes simplex virus glycoproteins H/L bind to cells independently of {alpha}V{beta}3 integrin and inhibit virus entry, and their constitutive expression restricts infection.Journal of virology · 2010Article
- Insertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion, or abrogate functions in cell fusion and viral entry.Journal of virology · 2010Article
- Anti-glycoprotein H antibody impairs the pathogenicity of varicella-zoster virus in skin xenografts in the SCID mouse model.Journal of virology · 2010Article
- Insertional mutations in herpes simplex virus type 1 gL identify functional domains for association with gH and for membrane fusion.Journal of virology · 2009Article
- Cross talk among the glycoproteins involved in herpes simplex virus entry and fusion: the interaction between gB and gH/gL does not necessarily require gD.Journal of virology · 2009Article
- Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops.Journal of virology · 2009Article
- Herpes simplex virus gD forms distinct complexes with fusion executors gB and gH/gL in part through the C-terminal profusion domain.The Journal of biological chemistry · 2009Article
- Peptides containing membrane-interacting motifs inhibit herpes simplex virus type 1 infectivity.Peptides · 2008Article
- Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Intracellular trafficking and maturation of herpes simplex virus type 1 gB and virus egress require functional biogenesis of multivesicular bodies.Journal of virology · 2007Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Entry of herpes simplex virus into cells occurs by fusion and requires four glycoproteins. gD serves as the receptor binding glycoprotein. Of the remaining glycoproteins, gH carries structural and functional elements typical of class 1 fusion glycoproteins, in particular alpha-helix 1 (alpha-H1), with properties of a candidate fusion peptide, and two heptad repeats. Here, we characterized alpha-H2 and compared it to alpha-H1. alpha-H2 (amino acids 513 to 531) is of lower hydrophobicity than alpha-H1. Its deletion or mutation decreased virus infection and cell fusion. Its replacement with heterologous fusion peptides did not rescue infection and cell fusion beyond the levels exhibited by the alpha-H2-deleted gH. This contrasts with alpha-H1, which cannot be deleted and can be functionally replaced with heterologous fusion peptides (T. Gianni et al., J. Virol. 79:2931-2940, 2005). Synthetic peptides mimicking alpha-H1 and alpha-H2 induced fusion of nude lipid vesicles. Importantly, they increased infection of herpes simplex virus, pseudorabies virus, bovine herpesvirus 1, and vesicular stomatitis virus. The alpha-H1 mimetic peptide was more effective than the alpha-H2 peptide. Consistent with the findings that gH carries membrane-interacting segments, a soluble form of gH, but not of gD or gB, partitioned with lipid vesicles. Current findings highlight that alpha-H2 is an important albeit nonessential region for virus entry and fusion. alpha-H1 and alpha-H2 share the ability to target the membrane lipids; they contribute to virus entry and fusion, possibly by destabilizing the membranes. However, alpha-H2 differs from alpha-H1 in that it is of lower hydrophobicity and cannot be replaced with heterologous fusion peptides.
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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.