ArticleGlycobiology2026
Site-specific and global glycan analysis of the human cytomegalovirus pentameric glycoprotein by high resolution mass spectrometry.
Article in Glycobiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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6 authors.
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Abstract
The Human Cytomegalovirus (HCMV) gH/gL/UL128/UL130/UL131A complex (Pentamer) is among the candidates for the development of a vaccine against HCMV; indeed, it brought to more immunogenic formulations which were able to protect the fetus against vertical transmission in pregnant women. Pentamer-specific antibodies have shown to be hundredfold more potent than gB or gH/gL antibodies, endowed with strong neutralizing activity. The often inadequate antibody immune response elicited by glycoprotein antigen has been, in part, attributed to the abundance of glycosylation on the protein. Here, we determine the composite glycan population of each of the N-linked and O-linked glycosylation sites present on the Pentamer by multienzymatic proteolysis and mass spectrometry; furthermore, total N-glycans profiles of Pentamer expressed in different cell systems have been compared exploiting the glycan fluorescent labeling and the immunogenicity of Pentamer with different glycosylation patterns has been investigated. Our analysis reveals the presence of underprocessed oligomannose-type glycans on some glycosylation sequons, which are probably derived as a result of sterically reduced accessibility to glycan processing enzymes. Furthermore, the antigen glycosylation pattern affects the elicitation of neutralizing antibodies in mice.
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