ArticleJournal of inflammation research2024
Role of Xenosialylation in Post-Infectious and Post-Vaccination Complications, Including Covid-19 and Anti-SARS-CoV-2 Vaccination.
Article in Journal of inflammation research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- Xenosialylation as immunological chimerism: a host-centered unifying model for viral and post-vaccination immune complications.European cytokine network · 2026Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The host glycosylation mechanism, with sialic acids as a key component, is essential for synthesizing carbohydrate components in viral glycoproteins. We hypothesize a correlation between the presence of the Neu5Gc on the host tissue and the development of infectious complications, adverse vaccine reactions, and autoimmune diseases. In certain mammals, including humans, the loss of the Cytidine Monophospho-N-Acetylneuraminic Acid Hydroxylase gene (negative-CMAH) prevents the synthesis of Neu5Gc, which acts as a Mammalian-associated Carbohydrate Antigen (MCA), (XeSiAs-Neu5Gc). When negative-CMAH species consume products from positive-CMAH mammals or are exposed to non-human cell-derived medicines, Neu5Gc can be integrated into their glycocalyx through a process called xenosialylation, eliciting an inflammatory response (xenosialitis) and prompting the production of circulating anti-Neu5Gc antibodies aimed at eliminating Neu5Gc. We hypothesize that in the case of xenosialylation, neutralizing antiviral antibodies from infections or vaccinations-including those for SARS-CoV-2-may cross-react with the XeSiAs-Neu5Gc glycans, as these resemble viral envelope antigens produced by the host's glycosylation. Additionally, circulating anti-Neu5Gc antibodies may also react with other circulating antibodies, including newly formed antiviral ones with a XeSiAs-Neu5Gc-contaminated Fc region. This can lead to the serum removal of the anti-inflammatory antibodies, leaving only hyperinflammatory IgG agalactosylated antibodies. Such conditions are also seen in various inflammatory and autoimmune diseases. We hypothesize that the combination of antibody cross-reaction and the removal of the XeSiAs-Neu5Gc-contaminated Fc region anti-inflammatory antibodies may intensify severe inflammatory responses like cytokine storms and coagulopathies in COVID-19 patients and those vaccinated. Assessing serum levels of total XeSiAs-Neu5Gc antibodies could be a valuable method for identifying patients at risk of severe complications from viral infections and vaccinations, including SARS-CoV-2. This strategy may also deepen our understanding of the pathogenesis of autoimmune diseases linked to post-infectious and post-vaccination complications, particularly for viruses utilizing the host glycosylation machinery, such as SARS-CoV-2, IAV, EBV, and others.
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