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Article

Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry.

PLoS pathogens - 1 Apr 2017

Wu Yiquan, Prager Adrian, Boos Simone, Resch Moritz, Brizic Ilija, Mach Michael, Wildner Sabrina, Scrivano Laura, Adler Barbara

Abstract excerpt

Herpesvirus gH/gL envelope glycoprotein complexes are key players in virus entry as ligands for host cell receptors and by promoting fusion of viral envelopes with cellular membranes. Human cytomegalovirus (HCMV) has two alternative gH/gL complexes, gH/gL/gO and gH/gL/UL128,130,131A which both shape the HCMV tropism. By studying binding of HCMV particles to fibroblasts, we could for the first time show that...

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Identifiers

PMID: 28403202
DOI: 10.1371/journal.ppat.1006281
PMCID: PMC5389851

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry.PMID 28403202Read ↗

Human cytomegalovirus gH/gL/gO binding to PDGFRα provides a regulatory signal activating the fusion protein gB that can be blocked by neutralizing antibodiesSemantic proximity Read ↗

Human cytomegalovirus gH/gL/gO binding to PDGFRα provides a regulatory signal activating the fusion protein gB that can be blocked by neutralizing antibodiesSemantic proximity Read ↗

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The N Terminus of Human Cytomegalovirus Glycoprotein O Is Important for Binding to the Cellular Receptor PDGFRαSemantic proximity Read ↗

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Human Cytomegalovirus gH/gL Forms a Stable Complex with the Fusion Protein gB in VirionsSemantic proximity Read ↗

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