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Dissociation of HSV gL from gH by αvβ6- or αvβ8-integrin promotes gH activation and virus entry
- Source :
- Proceedings of the National Academy of Sciences. 112
- Publication Year :
- 2015
- Publisher :
- Proceedings of the National Academy of Sciences, 2015.
-
Abstract
- Significance Entry of enveloped viruses into the cell requires the activation of viral glycoproteins, often mediated by cellular receptors. Herpesviruses infect cells via a multipartite system, which includes species-specific glycoproteins plus conserved apparatus gH/gL and gB. HSV makes use of αvβ6- or αvβ8-integrins as gH/gL receptors. The interaction of HSV gH/gL with integrins resulted in the dissociation of gL. The dissociation took place if all the actors of the entry apparatus were present, i.e., under conditions that lead to glycoprotein activation and virus entry. We propose that ( i ) gL is a regulator of gH and prevents its activation until integrins promote gL dissociation from gH/gL. ( ii ) Dissociation from an inhibitory regulator represents a previously unidentified mechanism of activation of viral fusion glycoproteins.
- Subjects :
- glycoprotein
Integrins
viruses
Amino Acid Motifs
Nectins
Integrin
Herpesvirus 1, Human
gL
virus entry
Biology
medicine.disease_cause
Models, Biological
Herpesviridae
gH
Viral Envelope Proteins
Antigens, Neoplasm
Viral entry
Cell Line, Tumor
medicine
Humans
Receptor
chemistry.chemical_classification
Brefeldin A
Multidisciplinary
Cell adhesion molecule
Cell Membrane
Virion
Antibodies, Monoclonal
Epithelial Cells
Herpes Simplex
Virus Internalization
herpes simplex viru
Antibodies, Neutralizing
Virology
Molecular biology
Herpesvirus glycoprotein B
Endocytosis
Protein Structure, Tertiary
Herpes simplex virus
Microscopy, Fluorescence
Solubility
PNAS Plus
chemistry
Mutation
Proteolysis
biology.protein
Glycoprotein
Cell Adhesion Molecules
Subjects
Details
- ISSN :
- 10916490 and 00278424
- Volume :
- 112
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences
- Accession number :
- edsair.doi.dedup.....211b85b8bb5ace89688fbcd712111424