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

2025-01-08

Abstract excerpt

<h4>ABSTRACT</h4> Herpesviruses require membrane fusion for entry and spread, a process facilitated by the fusion glycoprotein B (gB) and the regulatory factor gH/gL. The human cytomegalovirus (HCMV) gH/gL can be modified by the accessory protein gO, or the set of proteins UL128, UL130 and UL131. While the binding of the gH/gL/gO and gH/gL/UL128-131 complexes to cellular receptors including PDFGRα and NRP2 has be...

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Literature Corpus work
79de1cbe-c96f-5f5e-b6ef-ad115f477c01
DOI
10.1101/2025.01.08.631902
Open publication

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Human cytomegalovirus gH/gL/gO binding to PDGFRα provides a regulatory signal activating the fusion protein gB that can be blocked by neutralizing antibodiesDOI 10.1101/2025.01.08.631902
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