Site-specific proteolytic cleavage of the amino terminus of herpes simplex virus glycoprotein K on virion particles inhibits virus entry.
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Inhibitors of signal peptide peptidase (SPP) affect HSV-1 infectivity in vitro and in vivo.Herpes simplex virus 1 protein UL37 interacts with viral glycoprotein gK and membrane protein UL20 and functions in cytoplasmic virion envelopment.Amino acid differences in glycoproteins B (gB), C (gC), H (gH) and L (gL) are associated with enhanced herpes simplex virus type-1 (McKrae) entry via the paired immunoglobulin-like type-2 receptor α.The amino terminus of herpes simplex virus 1 glycoprotein K is required for virion entry via the paired immunoglobulin-like type-2 receptor alphaBovine herpesvirus glycoprotein D: a review of its structural characteristics and applications in vaccinologyA herpes simplex virus 1 (McKrae) mutant lacking the glycoprotein K gene is unable to infect via neuronal axons and egress from neuronal cell bodies.Herpes Simplex Vaccines: Prospects of Live-attenuated HSV Vaccines to Combat Genital and Ocular infections.Deletion of a Predicted β-Sheet Domain within the Amino Terminus of Herpes Simplex Virus Glycoprotein K Conserved among Alphaherpesviruses Prevents Virus Entry into Neuronal Axons.Cysteines and N-glycosylation Sites Conserved Among all Alphaherpesviruses Regulate Membrane Fusion in Herpes Simplex Virus Type 1 Infection.Binding of Herpes Simplex Virus 1 UL20 to GODZ (DHHC3) Affects Its Palmitoylation and Is Essential for Infectivity and Proper Targeting and Localization of UL20 and Glycoprotein K.Herpes Simplex Virus 1 UL37 Protein Tyrosine Residues Conserved among All Alphaherpesviruses Are Required for Interactions with Glycoprotein K, Cytoplasmic Virion Envelopment, and Infectious Virus Production.Phenylalanine residues at the carboxyl terminus of the herpes simplex virus 1 UL20 membrane protein regulate cytoplasmic virion envelopment and infectious virus productionBinding of HSV-1 glycoprotein K (gK) to signal peptide peptidase (SPP) is required for virus infectivityHerpes simplex virus 1 glycoprotein M and the membrane-associated protein UL11 are required for virus-induced cell fusion and efficient virus entryA replication competent HSV-1(McKrae) with a mutation in the amino-terminus of glycoprotein K (gK) is unable to infect mouse trigeminal ganglia after cornea infection.The absence of DHHC3 affects primary and latent HSV-1 infection.The Amino-terminus of HSV-1 Glycoprotein K (gK) is Required for gB Binding to Akt, Release of Intracellular Calcium and Fusion of the Viral Envelope with Plasma Membranes.
P2860
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P2860
Site-specific proteolytic cleavage of the amino terminus of herpes simplex virus glycoprotein K on virion particles inhibits virus entry.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
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2011年论文
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2011年论文
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name
Site-specific proteolytic clea ...... articles inhibits virus entry.
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Site-specific proteolytic clea ...... articles inhibits virus entry.
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type
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Site-specific proteolytic clea ...... articles inhibits virus entry.
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Site-specific proteolytic clea ...... articles inhibits virus entry.
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Site-specific proteolytic clea ...... articles inhibits virus entry.
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Site-specific proteolytic clea ...... articles inhibits virus entry.
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P2093
P2860
P356
P1433
P1476
Site-specific proteolytic clea ...... articles inhibits virus entry.
@en
P2093
Jason D Walker
Konstantin G Kousoulas
Nithya Jambunathan
Ramesh Subramanian
Sona Chowdhury
Vladimir N Chouljenko
P2860
P304
12910-12918
P356
10.1128/JVI.06268-11
P407
P577
2011-10-12T00:00:00Z