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Bally, Isabelle; Drumont, Guillaume; Rossi, Véronique; Guseva, Serafima; Botova, Maiia; Reiser, Jean-Baptiste; Thépaut, Michel; Dergan Dylon, Sebastian; Dumestre-Pérard, Chantal; Gaboriaud, Christine; Fieschi, Franck; Blackledge, Martin; Poignard, Pascal; Thielens, Nicole M.

Revisiting the interaction between complement lectin pathway protease MASP-2 and SARS-CoV-2 nucleoprotein

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  • Medientyp: E-Artikel
  • Titel: Revisiting the interaction between complement lectin pathway protease MASP-2 and SARS-CoV-2 nucleoprotein
  • Beteiligte: Bally, Isabelle; Drumont, Guillaume; Rossi, Véronique; Guseva, Serafima; Botova, Maiia; Reiser, Jean-Baptiste; Thépaut, Michel; Dergan Dylon, Sebastian; Dumestre-Pérard, Chantal; Gaboriaud, Christine; Fieschi, Franck; Blackledge, Martin; Poignard, Pascal; Thielens, Nicole M.
  • Erschienen: Frontiers Media SA, 2024
  • Erschienen in: Frontiers in Immunology, 15 (2024)
  • Sprache: Ohne Angabe
  • DOI: 10.3389/fimmu.2024.1419165
  • ISSN: 1664-3224
  • Entstehung:
  • Anmerkungen:
  • Beschreibung: Complement activation is considered to contribute to the pathogenesis of severe SARS-CoV-2 infection, mainly by generating potent immune effector mechanisms including a strong inflammatory response. Involvement of the lectin complement pathway, a major actor of the innate immune anti-viral defense, has been reported previously. It is initiated by recognition of the viral surface Spike glycoprotein by mannose-binding lectin (MBL), which induces activation of the MBL-associated protease MASP-2 and triggers the proteolytic complement cascade. A role for the viral nucleoprotein (N) has also been reported, through binding to MASP-2, leading to protease overactivation and potentiation of the lectin pathway. In the present study, we reinvestigated the interactions of the SARS-CoV-2 N protein, produced either in bacteria or secreted by mammalian cells, with full-length MASP-2 or its catalytic domain, in either active or proenzyme form. We could not confirm the interaction of the N protein with the catalytic domain of MASP-2 but observed N protein binding to proenzyme MASP-2. We did not find a role of the N protein in MBL-mediated activation of the lectin pathway. Finally, we showed that incubation of the N protein with MASP-2 results in proteolysis of the viral protein, an observation that requires further investigation to understand a potential functional significance in infected patients.
  • Zugangsstatus: Freier Zugang