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Molecular and Cellular Interactions of Scavenger Receptor SR-F1 With Complement C1q Provide Insights Into Its Role in the Clearance of Apoptotic Cells by Wicker-Planquart, Catherine; Dufour, Samy; Tacnet-Delorme, Pascale; Bally, Isabelle; Delneste, Yves; Frachet, Philippe; Housset, Dominique; Thielens, Nicole M. is a Immunology and Microbiology article available to read on EtoBox.

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The scavenger receptor SR-F1 binds to and mediates the internalization of a wide range of ligands, and is involved in several immunological processes. We produced recombinant SR-F1 ectodomain and fragments deleted from the last 2 or 5 C-terminal epidermal growth factor-like modules and investigated their role in the binding of acetylated low density lipoprotein (AcLDL), complement C1q, and calreticulin (CRT). C1q measured affinity was in the 100 nM range and C1q interaction occurs __via__ its collagen-like region. We identified two different binding regions on SR-F1: the N-terminal moiety interacts with C1q and CRT whereas the C-terminal moiety binds AcLDL. The role of SR-F1 N-linked glycans was also tested by mutating each of the three glycosylated asparagines. The three mutants retained binding activities for both AcLDL and C1q. A stable THP-1 cell line overexpressing SR-F1 was generated and C1q was shown to bind more strongly to the surface of SR-F1 overexpressing macrophages, with C1q/SR-F1 colocalization observed in some membrane areas. We also observed a higher level of CRT internalization for THP-1 SR-F1 cells. Increasing SR-F1 negatively modulated the uptake of apoptotic ce

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Author

Wicker-Planquart, Catherine; Dufour, Samy; Tacnet-Delorme, Pascale; Bally, Isabelle; Delneste, Yves; Frachet, Philippe; Housset, Dominique; Thielens, Nicole M.

Publisher

Frontiers; Frontiers Media SA; Frontiers Media S.A.; Lausanne: Frontiers Media S.A., 2010- (ISSN 1664-3224)

Published

2020

Language

EN

Field

Immunology and Microbiology (Life Sciences)