Mutational mapping of pUL131A of human cytomegalovirus emphasizes its central role for endothelial cell tropism

Schuessler, Andrea, Sampaio, Kerstin L., Straschewski, Sarah and Sinzger, Christian (2012) Mutational mapping of pUL131A of human cytomegalovirus emphasizes its central role for endothelial cell tropism. Journal of Virology, 86 1: 504-512. doi:10.1128/JVI.05354-11


Author Schuessler, Andrea
Sampaio, Kerstin L.
Straschewski, Sarah
Sinzger, Christian
Title Mutational mapping of pUL131A of human cytomegalovirus emphasizes its central role for endothelial cell tropism
Journal name Journal of Virology   Check publisher's open access policy
ISSN 0022-538X
1098-5514
Publication date 2012-01-01
Year available 2012
Sub-type Article (original research)
DOI 10.1128/JVI.05354-11
Open Access Status DOI
Volume 86
Issue 1
Start page 504
End page 512
Total pages 9
Place of publication Washington, DC United States
Publisher American Society for Microbiology
Collection year 2013
Language eng
Subject 2403 Immunology
2406 Virology
Abstract 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.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Medicine Publications
 
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