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Revisiting the interaction between complement lectin pathway protease MASP-2 and SARS-CoV-2 nucleoprotein.
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.
Affiliation
  • Bally I; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Drumont G; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Rossi V; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Guseva S; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Botova M; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Reiser JB; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Thépaut M; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Dergan Dylon S; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Dumestre-Pérard C; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Gaboriaud C; Laboratory of Immunology, Grenoble Alpes University Hospital, Grenoble, France.
  • Fieschi F; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Blackledge M; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Poignard P; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
  • Thielens NM; Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.
Front Immunol ; 15: 1419165, 2024.
Article in En | MEDLINE | ID: mdl-38911852
ABSTRACT
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Complement Pathway, Mannose-Binding Lectin / Mannose-Binding Protein-Associated Serine Proteases / SARS-CoV-2 / COVID-19 Limits: Humans Language: En Journal: Front Immunol Year: 2024 Document type: Article Affiliation country: France

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Complement Pathway, Mannose-Binding Lectin / Mannose-Binding Protein-Associated Serine Proteases / SARS-CoV-2 / COVID-19 Limits: Humans Language: En Journal: Front Immunol Year: 2024 Document type: Article Affiliation country: France