UL74 of human cytomegalovirus contributes to virus release by promoting secondary envelopment of virions

Journal of Virology
Xiao Jing JiangChristian Sinzger

Abstract

The glycoprotein (g) complex gH/gL represents an essential part of the herpesvirus fusion machinery mediating entry of cell-free virions and cell-associated viral spread. In some herpesviruses additional proteins are associated with gH/gL contributing to the cell tropism of the respective virus. Human cytomegalovirus (HCMV) gH/gL forms complexes with either gO (UL74) or proteins of the UL128-131A gene locus. While a contribution of UL128-131A to endothelial cell tropism is known, the role of gO is less clear. We studied the role of gH/gL-associated proteins in HCMV replication in human foreskin fibroblasts (HFF) and human umbilical vein endothelial cells (HUVEC). Deletions of UL74 alone or in combination with mutations of the UL128-131A gene region were introduced into bacterial artificial chromosome vectors derived from the endotheliotropic strain TB40/E. Deletion of UL74 caused a profound defect regarding virus release from infected HFF and HUVEC. Large numbers of capsids accumulated in the cytoplasm of infected HFF but failed to acquire an envelope. Clear cell type differences were observed in the cell-associated spread of the UL74-defective virus. In HFF, focal growth was severely impaired, whereas it was normal in HUVEC. D...Continue Reading

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Citations

Sep 23, 2011·Archives of Virology·Xiao Jing JiangChristian Sinzger
Sep 5, 2008·Proceedings of the National Academy of Sciences of the United States of America·Brent J RyckmanDavid C Johnson
Oct 5, 2011·Antimicrobial Agents and Chemotherapy·Gilles A SpodenLuise Florin
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