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

Significance IgA is the most abundantly produced antibody in the body (in humans, &gt;5 g/d) and plays a crucial role in mucosal immunity. IgA forms a dimer that covalently associates with the joining (J) chain, which is essential for IgA transport into the gut. We show that MZB1 is required for the secretion of IgA, but not IgG, by antibody-secreting plasma cells. MZB1 mediates the stabilization of Igα heavy-chain–light-chain complexes and, more importantly, promotes J-chain binding to IgA. Mice lacking MZB1 are impaired in secreting large amounts of IgA into the gut in response to acute inflammatory stimuli and develop severe colitis. The present study reveals an important mechanism that controls the quantity, quality, and function of IgA.

MZB1 promotes the secretion of J-chain–containing dimeric IgA and is critical for the suppression of gut inflammation