SARS-CoV-2 membrane protein-specific antibodies from critically ill SARS-CoV-2-infected individuals interact with Fc receptor-expressing cells but do not neutralize the virus.
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| Abstract |
The membrane (M) glycoprotein of SARS-CoV-2 is one of the key viral proteins regulating virion assembly and morphogenesis. Immunologically, the M protein is a major source of peptide antigens driving T cell responses, and most individuals who have been infected with SARS-CoV-2 make antibodies to the N-terminal, surface-exposed peptide of the M protein. We now report that although the M protein is abundant in the viral particle, antibodies to the surface-exposed N-terminal epitope of M do not appear to neutralize the virus. M protein-specific antibodies do, however, activate antibody-dependent cell-mediated cytotoxicity and cytokine secretion by primary human natural killer cells. Interestingly, while patients with severe or mild disease make comparable levels of M antigen-binding antibodies, M-specific antibodies from the serum of critically ill patients are significantly more potent activators of antibody-dependent cell-mediated cytotoxicity than antibodies found in individuals with mild or asymptomatic infection.
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| Authors | Daniel Fernández-Soto, Paula Bueno, Urtzi Garaigorta, Pablo Gastaminza, José L Bueno, Rafael F Duarte, Ricardo Jara, Mar Valés-Gómez, Hugh T Reyburn |
| Journal | Journal of leukocyte biology (J Leukoc Biol) Vol. 115 Issue 5 Pg. 985-991 (Apr 29 2024) ISSN: 1938-3673 [Electronic] England |
| PMID | 38245016 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural) |
| Copyright | © The Author(s) 2024. Published by Oxford University Press on behalf of Society for Leukocyte Biology. |
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