Document Detail


Mutational mapping of pUL131A of human cytomegalovirus emphasizes its central role for endothelial cell tropism.
MedLine Citation:
PMID:  22031943     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The UL131A protein is part of a pentameric variant of the gcIII complex in the virion envelope of human cytomegalovirus (HCMV), which has been found essential for efficient entry into endothelial cells (ECs). Using a systematic mutational scanning approach, we aimed to define peptide motifs within the UL131A protein that contribute to EC infection. Mutant viruses were generated in which charged amino acids within frames of 2 to 6 amino acids were replaced with alanines. The resulting viruses were evaluated with regard to their potential to infect EC cultures. Four clusters of charged amino acids essential for EC infection were identified (amino acids 22 to 27, 32 to 35, 64 to 69, and 116 to 121). Mutations of individual charge clusters within amino acids 72 to 104 caused minor reductions of EC tropism, but these effects were additive in a combined mutation, showing that this region also contributes to EC tropism. Only charge clusters within amino acids 46 to 58 were found irrelevant for EC infection. In conclusion, the unusual sensitivity to mutations, together with the remarkable conservation of the UL131A protein, emphasizes its particular role for EC tropism of HCMV.
Authors:
Andrea Schuessler; Kerstin Laib Sampaio; Sarah Straschewski; Christian Sinzger
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-10-26
Journal Detail:
Title:  Journal of virology     Volume:  86     ISSN:  1098-5514     ISO Abbreviation:  J. Virol.     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2011-12-14     Completed Date:  2012-02-14     Revised Date:  2013-06-27    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  504-12     Citation Subset:  IM    
Affiliation:
Institute of Medical Virology and Epidemiology of Virus Diseases, University of Tuebingen, Tuebingen, Germany.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Motifs
Amino Acid Sequence
Cell Line
Cytomegalovirus / chemistry,  genetics,  physiology*
Cytomegalovirus Infections / virology*
Endothelial Cells / virology*
Humans
Molecular Sequence Data
Mutation*
Viral Envelope Proteins / chemistry,  genetics*,  metabolism
Viral Tropism*
Virus Internalization
Chemical
Reg. No./Substance:
0/Viral Envelope Proteins
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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