| Mutational mapping of pUL131A of human cytomegalovirus emphasizes its central role for endothelial cell tropism. | |
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MedLine Citation:
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PMID: 22031943 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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 2-6 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 22-27, 32-35, 64-69 and 116-121). Mutations of individual charge clusters within amino acids 72-104 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 46-58 were found irrelevant for EC infection. In conclusion, the unusual sensitivity to mutations together with the remarkable conservation of the UL131A protein emphasize its particular role for EC tropism of HCMV. |
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Authors:
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Andrea Schuessler; Kerstin Laib Sampaio; Sarah Straschewski; Christian Sinzger |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-10-26 |
Journal Detail:
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Title: Journal of virology Volume: - ISSN: 1098-5514 ISO Abbreviation: - Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-10-27 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0113724 Medline TA: J Virol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Institute of Medical Virology and Epidemiology of Virus Diseases, University of Tuebingen, D-72076 Tuebingen, Germany. |
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