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Go go gadget glycoprotein!: HSV-1 draws on its sizeable glycoprotein tool kit to customize its diverse entry routes
Yet, entry of herpesviruses—large enveloped viruses that infect a wide variety of cells—is more complex, as it requires multiple viral glycoproteins (typically, at least three) and diverse host receptors [16]. [...]the coordinated activity of these multiple viral glycoproteins permits entry into dif...
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Published in: | PLoS pathogens 2019-05, Vol.15 (5), p.e1007660-e1007660 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Yet, entry of herpesviruses—large enveloped viruses that infect a wide variety of cells—is more complex, as it requires multiple viral glycoproteins (typically, at least three) and diverse host receptors [16]. [...]the coordinated activity of these multiple viral glycoproteins permits entry into different cell types by different routes. Other envelope proteins (gE, gI, gM, gN, and UL45) have roles in cell-to-cell spread and membrane fusion but have not yet been assigned any roles in entry. 3-OS-HS, 3-O-sulfated-heparan sulfate; HSV-1, herpes simplex virus type 1; HVEM, herpes virus entry mediator; PDB, Protein Data Bank; PILRα, paired immunoglobulin-like type 2 receptor alpha; RCSB, Research Collaboratory for Structural Bioinformatics. https://doi.org/10.1371/journal.ppat.1007660.g001 HSV-1 entry into any cell requires the coordinated efforts of gD, gH, gL, and gB. [...]gD, gH, gL, and gB can also mediate cell–cell fusion of uninfected, receptor-bearing cells expressing these four glycoproteins [23]. 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. |
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ISSN: | 1553-7374 1553-7366 1553-7374 |
DOI: | 10.1371/journal.ppat.1007660 |