English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Recognition by the leukocyte integrins α X β 2 and α M β 2 of complement iC3b-opsonized targets is essential for effector functions including phagocytosis. The integrin-binding sites on iC3b remain incompletely characterized. Here, we describe negative-stain electron microscopy and biochemical studies of α X β 2 and α M β 2 in complex with iC3b. Despite high homology, the two integrins bind iC3b at multiple distinct sites. α X β 2 uses the α X αI domain to bind iC3b on its C3c moiety at one of two sites: a major site at the interface between macroglobulin (MG) 3 and MG4 domains, and a less frequently used site near the C345C domain. In contrast, α M β 2 uses its αI domain to bind iC3b at the thioester domain and simultaneously interacts through a region near the α M β-propeller and β 2 βI domain with a region of the C3c moiety near the C345C domain. Remarkably, there is no overlap between the primary binding site of α X β 2 and the binding site of α M β 2 on iC3b. Distinctive binding sites on iC3b by integrins α X β 2 and α M β 2 may be biologically beneficial for leukocytes to more efficiently capture opsonized pathogens and to avoid subversion by pathogen factors.

Distinct recognition of complement iC3b by integrins αXβ2and αMβ2

Distinct recognition of complement iC3b by integrins α_Xβ₂and α_Mβ₂