SARS-CoV-2 integral membrane proteins shape the serological responses of patients with COVID-19

• Published in: iScience Vol. 24; no. 10; p. 103185
• Main Authors: Martin, Sophie, Heslan, Christopher, Jégou, Gwénaële, Eriksson, Leif A., Le Gallo, Matthieu, Thibault, Vincent, Chevet, Eric, Godey, Florence, Avril, Tony
• Format: Journal Article
• Language: English
• Published: Elsevier Inc 22.10.2021; Elsevier
• Subjects: Immunology; Virology; Immunology; Virology
• ISSN: 2589-0042; 2589-0042
• DOI: 10.1016/j.isci.2021.103185

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic has elicited a unique mobilization of the scientific community to develop efficient tools to understand and combat the infection. Like other coronavirae, SARS-CoV-2 hijacks host cell secretory machinery to produce viral proteins that compose the nascent virions; including spike (S), envelope (E), and membrane (M) proteins, the most exposed transmembrane proteins to the host immune system. As antibody response is part of the anti-viral immune arsenal, we investigate the immunogenic potential of S, E, and M using a human cell-based system to mimic membrane insertion and N-glycosylation. Both S and M elicit specific Ig production in patients with SARS-CoV-2. Patients with moderate and severe diseases exhibit elevated Ig responses. Finally, reduced Ig binding was observed with spike G614 compared to D614 variant. Altogether, our assay points toward an unexpected immune response against M and represents a powerful tool to test humoral responses against actively evolving SARS-CoV-2 variants and vaccine effectiveness. [Display omitted] •SARS-CoV-2 membrane proteins antigenicity was evaluated in a human cell-based assay•The assay recapitulates their membrane insertion and post-translational modifications•High Ig response against S and M proteins was observed in severe patients with COVID-19•The D614 variant of spike exhibited an altered structure and reduced Ig binding Immunology; Virology