Work

Distinct recognition of complement iC3b by integrins α X β 2 and α M β 2

Year: 2017

Type: article

Abstract: Significance Complement is deposited on foreign antigens and particles and marks them for recognition by immune cells and removal by phagocytes. Immune cells have two homologous integrins, α X β 2 and α M β 2 , that recognize the complement fragment iC3b. Although it might have been suspected that these integrins would bind to the same site on iC3b, direct comparisons here show they do not. Using negative stain electron microscopy and purified integrin fragments and iC3b, we show that α X β 2 binds to two distinct sites on iC3b. A single α M β 2 integrin binds to two different sites on iC3b, each of which is distinct from those to which α X β 2 binds. Our findings reveal remarkable diversity among integrins that recognize complement and suggest possible cooperative responses.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.1620881114

Authors: Shutong Xu, Jianchuan Wang, Jia-Huai Wang, Timothy A. Springer

Institutions: Dana-Farber Cancer Institute, Boston Children's Hospital, Harvard University

Language: English

Topic: Cell Adhesion Molecules Research

Subfield: Immunology and Allergy

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: green

Funders: National Heart, Lung, and Blood Institute, National Institute of Allergy and Infectious Diseases