Mutational mapping of UL130 of human cytomegalovirus defines peptide motifs within the C-terminal third as essential for endothelial cell infection

Schuessler, Andrea, Sampaio, Kerstin L., Scrivano, Laura and Sinzger, Christian (2010) Mutational mapping of UL130 of human cytomegalovirus defines peptide motifs within the C-terminal third as essential for endothelial cell infection. Journal of Virology, 84 18: 9019-9026. doi:10.1128/JVI.00572-10


Author Schuessler, Andrea
Sampaio, Kerstin L.
Scrivano, Laura
Sinzger, Christian
Title Mutational mapping of UL130 of human cytomegalovirus defines peptide motifs within the C-terminal third as essential for endothelial cell infection
Journal name Journal of Virology   Check publisher's open access policy
ISSN 0022-538X
1098-5514
Publication date 2010-09-01
Year available 2010
Sub-type Article (original research)
DOI 10.1128/JVI.00572-10
Open Access Status DOI
Volume 84
Issue 18
Start page 9019
End page 9026
Total pages 8
Place of publication Washington, DC United States
Publisher American Society for Microbiology
Language eng
Subject 2403 Immunology
2406 Virology
Abstract The UL130 gene is one of the major determinants of endothelial cell (EC) tropism of human cytomegalovirus (HCMV). In order to define functionally important peptides within this protein, we have performed a charge-cluster-to- alanine (CCTA) mutational scanning of UL130 in the genetic background of a bacterial artificial chromosome-cloned endotheliotropic HCMV strain. A total of 10 charge clusters were defined, and in each of them two or three charged amino acids were replaced with alanines. While the six N-terminal clusters were phenotypically irrelevant, mutation of the four C-terminal clusters each caused a reduction of EC tropism. The importance of this protein domain was further emphasized by the fact that the C-terminal pentapeptide PNLIV was essential for infection of ECs, and the cell tropism could not be rescued by a scrambled version of this sequence. We conclude that the C terminus of the UL130 protein serves an important function for infection of ECs by HCMV. This makes UL130 a promising molecular target for antiviral strategies, e.g., the development of antiviral peptides. Copyright
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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