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Details on Person Mannose-binding lectin (MBL2), a soluble pattern recognition...
| Class:Id | Summation:9957092 |
|---|---|
| _displayName | Mannose-binding lectin (MBL2), a soluble pattern recognition... |
| _timestamp | 2026-01-22 18:05:17 |
| created | [InstanceEdit:9957084] Shamovsky, Veronica, 2025-06-17 |
| literatureReference | [LiteratureReference:182411] Mannose-binding lectin binds to a range of clinically relevant microorganisms and promotes complement deposition [LiteratureReference:9957190] Mannose-binding lectin: the pluripotent molecule of the innate immune system [LiteratureReference:9957082] Complement lectin pathway activation is associated with COVID-19 disease severity, independent of MBL2 genotype subgroups [LiteratureReference:9957162] Recognition and inhibition of SARS-CoV-2 by humoral innate immunity pattern recognition molecules [LiteratureReference:9957129] Analysis of the N-glycosylation profiles of the spike proteins from the Alpha, Beta, Gamma, and Delta variants of SARS-CoV-2 [LiteratureReference:9758537] Lectin Pathway Mediates Complement Activation by SARS-CoV-2 Proteins [LiteratureReference:9957123] Structural biology of SARS-CoV-2: open the door for novel therapies [LiteratureReference:9957121] Molecular Architecture of the SARS-CoV-2 Virus [LiteratureReference:9957130] Unraveling the impact of SARS-CoV-2 mutations on immunity: insights from innate immune recognition to antibody and T cell responses [LiteratureReference:9957158] A likely association between low mannan-binding lectin level and brain fog onset in long COVID patients [LiteratureReference:9957155] The Soluble Lectin Families as Novel Biomarkers for COVID-19 Pneumonia [LiteratureReference:9758568] Endothelial injury and thrombotic microangiopathy in COVID-19: Treatment with the lectin-pathway inhibitor narsoplimab [LiteratureReference:9957094] Mannose binding lectin gene 2 (rs1800450) missense variant may contribute to development and severity of COVID-19 infection [LiteratureReference:9957090] Revisiting the interaction between complement lectin pathway protease MASP-2 and SARS-CoV-2 nucleoprotein [LiteratureReference:9957139] SARS-CoV-2 Nucleocapsid Protein Is Not Responsible for Over-Activation of Complement Lectin Pathway [LiteratureReference:9957106] Highly pathogenic coronavirus N protein aggravates inflammation by MASP-2-mediated lectin complement pathway overactivation |
| modified | [InstanceEdit:9979897] Shamovsky, Veronica, 2026-01-22 |
| text | Mannose-binding lectin (MBL2), a soluble pattern recognition receptor that recognizes and binds specific surface-bound carbohydrate motifs, such as mannose and fucose, in a Ca²⁺-dependent manner (Turner MW, 1996; Neth O et al., 2000), binds to the spike (S) protein of SARS-CoV-2 (Ali YM et al., 2021; Stravalaci M et al., 2022; Hurler L et al., 2023; Bayarri-Olmos R et al., 2024). The heavily glycosylated viral S contains several oligomannose-type N-glycans ( Watanabe Y et al., 2020; Wang D et al., 2023), which serve as potential binding sites of MBL2 (Stravalaci M et al., 2022; Bayarri-Olmos R et al., 2024). The viral S protein is incorporated into mature virions as a structural component within the S3:M:E:encapsidated SARS coronavirus genomic RNA:7a:O-glycosyl 3a tetramer complex (Yao H et al., 2020; Yan W et al., 2022). MBL2 binding can sterically hinder the interaction between the viral S protein and its receptor, angiotensin-converting enzyme 2 (ACE2), thereby limiting viral entry into host cells (Stravalaci M et al., 2022). Upon binding to the viral S protein, MBL2 activates the lectin pathway of the complement cascade by associating with MBL-associated serine proteases (MASP1 and MASP2), leading to opsonization, membrane attack complex (MAC) formation, and enhanced viral clearance (Ali YM et al., 2021; Stravalaci M et al., 2022). In addition, the nucleocapsid (N) protein of SARS-CoV-2 is thought to contribute to MBL-dependent, MASP2-mediated activation of the lectin pathway (Ali YM et al., 2021; Gao T et al., 2022). However, the precise mechanism of N protein involvement remains unclear, with studies reporting contradictory findings (Bally I et al., 2024; Kocsis A et al., 2024). Complement activation via MBL2 also contributes to the production of pro-inflammatory anaphylatoxins (C3a and C5a), which recruit immune cells and amplify cytokine production. Although complement activation supports viral clearance, excessive or uncontrolled activation may promote hyperinflammation and tissue injury, implicating the lectin pathway in COVID-19-related-immunopathologies (Rambaldi A et al., 2020; Medetalibeyoglu A et al., 2021; Stravalaci M et al., 2022; Hurler L et al., 2023; Bulla R et al., 2023; Takenaka H et al., 2023). |
| (summation) | [Reaction:9957161] MBL2 binds SARS-CoV-2 S [Homo sapiens] |
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