ArticleProceedings of the National Academy of Sciences of the United States of America2025
Virion proteomics of genetically intact HCMV reveals a regulator of envelope glycoprotein composition that protects against humoral immunity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Human herpesvirus evasion of humoral immunity and implications for vaccine development.Nature reviews. Microbiology · 2026Review
- Decoding the antiviral potential of eugenol, thymol and vanillin against human cytomegalovirus infection.The Journal of general virology · 2026Article
- A viral glycoprotein targets IgGEMBO molecular medicine · 2026Article
- Progress and prospects for herpesvirus vaccination using gB antigens.Frontiers in immunology · 2026Review
- Selective decoupling of IgG1 binding to viral Fc receptors restores antibody-mediated NK cell activation against HCMV.Cell reports · 2025Article
- Increased infectivity of human cytomegalovirus strain TB40/E conferred by variants of the envelope glycoprotein UL128 and the regulatory protein IE2.Journal of virology · 2025Article
- Advancing antivirals.Nature biotechnology · 2025Article
- Human Cytomegalovirus Immune Evasion of Natural Killer Cells: A Virus for All Seasons?Pathogens (Basel, Switzerland) · 2025Review
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Authors and funding
15 authors.
Funding
Abstract
Human cytomegalovirus (HCMV) is a clinically important herpesvirus that has coevolved for millions of years with its human host, and establishes lifelong persistent infection. A substantial proportion of its 235 kb genome is dedicated to manipulating host immunity through targeting antiviral host proteins for degradation or relocalization. Quantitative proteomics of the infected cell has extensively characterized these processes, but the cell-free virion has been less well studied. We therefore carried out proteomic analysis of a clinical HCMV strain (Merlin) virion. This revealed 18 novel components, including the viral protein gpUL141, which is recognized as an NK immune-evasin that targets several host proteins (CD155, CD112, and TRAILR) when expressed within the cell. Coimmunoprecipitation of gpUL141 from virions identified interactions with viral entry glycoproteins from the trimer (gH/gL/gO), pentamer (gH/gL/UL128/UL130/UL131A), and gH/gpUL116 complexes, as well as gB. Only interactions with gH/gB occurred in the absence of other viral proteins. Analysis supported a model in which gpUL141 homodimers independently interacted with separate gB/gH-containing complexes. gpUL141 encodes an ER retention domain that restricts trafficking through the ER/Golgi, and limited the transport of glycoprotein complexes bound by gpUL141. As a result, gpUL141 reduced levels of multiple glycoprotein complexes on the infected cell surface as well as in the virion. This reduced syncytium formation, inhibited antibody-dependent cellular cytotoxicity (ADCC), and reduced susceptibility to neutralizing antibodies. Thus, gpUL141 represents an immune-evasin that not only targets host proteins to limit NK-cell attack, but also alters the trafficking of multiple viral glycoprotein complexes in order to evade humoral immunity.
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