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- W2904685881 endingPage "704" @default.
- W2904685881 startingPage "704" @default.
- W2904685881 abstract "The past few years have brought substantial progress toward understanding how human cytomegalovirus (HCMV) enters the remarkably wide spectrum of cell types and tissues that it infects. Neuropilin-2 and platelet-derived growth factor receptor alpha (PDGFRα) were identified as receptors, respectively, for the trimeric and pentameric glycoprotein H/glycoprotein L (gH/gL) complexes that in large part govern HCMV cell tropism, while CD90 and CD147 were also found to play roles during entry. X-ray crystal structures for the proximal viral fusogen, glycoprotein B (gB), and for the pentameric gH/gL complex (pentamer) have been solved. A novel virion gH complex consisting of gH bound to UL116 instead of gL was described, and findings supporting the existence of a stable complex between gH/gL and gB were reported. Additional work indicates that the pentamer promotes a mode of cell-associated spread that resists antibody neutralization, as opposed to the trimeric gH/gL complex (trimer), which appears to be broadly required for the infectivity of cell-free virions. Finally, viral factors such as UL148 and US16 were identified that can influence the incorporation of the alternative gH/gL complexes into virions. We will review these advances and their implications for understanding HCMV entry and cell tropism." @default.
- W2904685881 created "2018-12-22" @default.
- W2904685881 creator A5006646838 @default.
- W2904685881 creator A5076867590 @default.
- W2904685881 date "2018-12-11" @default.
- W2904685881 modified "2023-10-02" @default.
- W2904685881 title "Pathogen at the Gates: Human Cytomegalovirus Entry and Cell Tropism" @default.
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