Brucella activates the host RIDD pathway to subvert BLOS1-directed immune defense

Elife. 2022 May 19:11:e73625. doi: 10.7554/eLife.73625.

Abstract

The phagocytosis and destruction of pathogens in lysosomes constitute central elements of innate immune defense. Here, we show that Brucella, the causative agent of brucellosis, the most prevalent bacterial zoonosis globally, subverts this immune defense pathway by activating regulated IRE1α-dependent decay (RIDD) of Bloc1s1 mRNA encoding BLOS1, a protein that promotes endosome-lysosome fusion. RIDD-deficient cells and mice harboring a RIDD-incompetent variant of IRE1α were resistant to infection. Inactivation of the Bloc1s1 gene impaired the ability to assemble BLOC-1-related complex (BORC), resulting in differential recruitment of BORC-related lysosome trafficking components, perinuclear trafficking of Brucella-containing vacuoles (BCVs), and enhanced susceptibility to infection. The RIDD-resistant Bloc1s1 variant maintains the integrity of BORC and a higher-level association of BORC-related components that promote centrifugal lysosome trafficking, resulting in enhanced BCV peripheral trafficking and lysosomal destruction, and resistance to infection. These findings demonstrate that host RIDD activity on BLOS1 regulates Brucella intracellular parasitism by disrupting BORC-directed lysosomal trafficking. Notably, coronavirus murine hepatitis virus also subverted the RIDD-BLOS1 axis to promote intracellular replication. Our work establishes BLOS1 as a novel immune defense factor whose activity is hijacked by diverse pathogens.

Keywords: BLOS1; Brucella; Brucella-containing vacuoles/lysosomes (BCVs); coronavirus; infectious disease; intracellular parasitism; microbiology; mouse; regulated IRE1α-dependent decay (RIDD).

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Brucella*
  • Brucellosis* / metabolism
  • Brucellosis* / microbiology
  • Endoribonucleases / metabolism
  • Endosomes / metabolism
  • Mice
  • Protein Serine-Threonine Kinases

Substances

  • Protein Serine-Threonine Kinases
  • Endoribonucleases