Cryo-EM reveals structural basis for human AIM/CD5L recognition of polymeric immunoglobulin M.

Autor: Chen Q; Structural Biology Science Technology Platform, The Francis Crick Institute, London, UK., Ishii K; The Institute for AIM Medicine, Tokyo, Japan.; Department of Physiological Chemistry and Metabolism, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan., Mori H; The Institute for AIM Medicine, Tokyo, Japan., Nishijima A; The Institute for AIM Medicine, Tokyo, Japan., Arai S; The Institute for AIM Medicine, Tokyo, Japan. arai.satoko@iamaim.jp., Miyazaki T; The Institute for AIM Medicine, Tokyo, Japan. tm@iamaim.jp.; LEAP, Japan Agency for Medical Research and Development, Tokyo, Japan. tm@iamaim.jp.; Laboratoire d'ImmunoRhumatologie Moléculaire, Plateforme GENOMAX, Institut National de la Santé et de la Recherche Médicale UMR_S 1109, Faculté de Médecine, Fédération Hospitalo-Universitaire OMICARE, Fédération de Médecine Translationnelle de Strasbourg, Laboratory of Excellence TRANSPLANTEX, Université de Strasbourg, Strasbourg, France. tm@iamaim.jp., Rosenthal PB; Structural Biology of Cells and Viruses Laboratory, The Francis Crick Institute, London, UK. Peter.Rosenthal@crick.ac.uk.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2024 Oct 30; Vol. 15 (1), pp. 9387. Date of Electronic Publication: 2024 Oct 30.
DOI: 10.1038/s41467-024-53615-5
Abstrakt: Cell surface scavenger receptors contribute to homoeostasis and the response to pathogens and products associated with damage by binding to common molecular features on a wide range of targets. Apoptosis inhibitor of macrophage (AIM/CD5L) is a soluble protein belonging to the scavenger receptor cysteine-rich (SRCR) superfamily that contributes to prevention of a wide range of diseases associated with infection, inflammation, and cancer. AIM forms complexes with IgM pentamers which helps maintain high-levels of circulating AIM in serum for subsequent activation on release from the complex. The structural basis for AIM recognition of IgM as well as other binding targets is unknown. Here we apply cryogenic electron microscopy imaging (cryo-EM) to show how interfaces on both of AIM's C-terminal SRCR domains interact with the Fcμ constant region and J chain components of the IgM core. Both SRCR interfaces are also shown to contribute interactions important for AIM binding to damage-associated molecular patterns (DAMPs).
(© 2024. The Author(s).)
Databáze: MEDLINE
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