Document Detail


Sialic acid on herpes simplex virus type 1 envelope glycoproteins is required for efficient infection of cells.
MedLine Citation:
PMID:  17229687     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Herpes simplex virus type 1 (HSV-1) envelope proteins are posttranslationally modified by the addition of sialic acids to the termini of the glycan side chains. Although gC, gD, and gH are sialylated, it is not known whether sialic acids on these envelope proteins are functionally important. Digestion of sucrose gradient purified virions for 4 h with neuraminidases that remove both alpha2,3 and alpha2,6 linked sialic acids reduced titers by 1,000-fold. Digestion with a alpha2,3-specific neuraminidase had no effect, suggesting that alpha2,6-linked sialic acids are required for infection. Lectins specific for either alpha2,3 or alpha2,6 linkages blocked attachment and infection to the same extent. In addition, the mobility of gH, gB, and gD in sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels was altered by digestion with either alpha2,3 specific neuraminidase or nonspecific neuraminidases, indicating the presence of both linkages on these proteins. The infectivity of a gC-1-null virus, DeltagC2-3, was reduced to the same extent as wild-type virus after neuraminidase digestion, and attachment was not altered. Neuraminidase digestion of virions resulted in reduced VP16 translocation to the nucleus, suggesting that the block occurred between attachment and entry. These results show for the first time that sialic acids on HSV-1 virions play an important role in infection and suggest that targeting virion sialic acids may be a valid antiviral drug development strategy.
Authors:
Jeremy R Teuton; Curtis R Brandt
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2007-01-17
Journal Detail:
Title:  Journal of virology     Volume:  81     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  2007 Apr 
Date Detail:
Created Date:  2007-03-29     Completed Date:  2007-05-18     Revised Date:  2014-09-15    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3731-9     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Antiviral Agents / metabolism,  pharmacology
Cell Nucleus / chemistry
Cercopithecus aethiops
Cytoplasm / chemistry
Electrophoresis, Polyacrylamide Gel
Electrophoretic Mobility Shift Assay
Gene Deletion
Glycoproteins / metabolism,  physiology*
Herpes Simplex Virus Protein Vmw65 / metabolism
Herpesvirus 1, Human / physiology*
Lectins / metabolism,  pharmacology
N-Acetylneuraminic Acid / metabolism,  physiology*
Neuraminidase / metabolism
Protein Transport
Vero Cells
Viral Envelope Proteins / genetics,  metabolism,  physiology*
Viral Proteins
Virus Attachment / drug effects
Virus Internalization
Grant Support
ID/Acronym/Agency:
GM-62116/GM/NIGMS NIH HHS; P01 AI052049/AI/NIAID NIH HHS; P01-AI52089/AI/NIAID NIH HHS; P30 EY016665/EY/NEI NIH HHS; P30 EY016665/EY/NEI NIH HHS; R01 EY007336/EY/NEI NIH HHS; R01-EY07336/EY/NEI NIH HHS
Chemical
Reg. No./Substance:
0/Antiviral Agents; 0/Glycoproteins; 0/Herpes Simplex Virus Protein Vmw65; 0/Lectins; 0/Viral Envelope Proteins; 0/Viral Proteins; 0/bovine herpesvirus type-1 glycoproteins; 0/glycoprotein D, Human herpesvirus 1; 0/glycoprotein H, herpes simplex virus type 1; 0/glycoprotein gC, herpes simplex virus type 1; EC 3.2.1.18/Neuraminidase; GZP2782OP0/N-Acetylneuraminic Acid
Comments/Corrections

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