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Biology subjects

Sze, N.

Publications and source records attributed to Sze, N..

2 recordsLinked to original sources

Bacterial suppression of intestinal fungi via activation of human gut γδ T-cells

Gut symbionts condition mucosal immunity to resist infection by enteropathogens, but the specific microbes and mechanisms involved differ significantly between host species. In higher primates, bacterial metabolite HMB-PP is sensed by a specialized population of V{gamma}9V{delta}2+T-cells, which we now report can potently suppress growth of endogenous fungi in human intestinal organ cultures. In healthy intestine, HMB-PP-stimulated V{delta}2+T-cells restricted outgrowth of keystone fungus Candida albicans via a mechanism that required IL-22. In contrast, Crohns disease (CD) patients with reduced V{delta}2+T-cell numbers displayed outgrowth of C. albicans strains that readily formed toxin-producing filaments, triggered neutrophil extracellular traps, and induced macrophage IL-1{beta} release ex vivo. Genomic and proteomic analysis of the Candida isolates suggested increased tissue adhesion of CD-derived strains, which rapidly invaded the gut barrier in an intestine-on-a-chip model. These data reveal that bacterial activation of V{delta}2+T-cells suppresses fungal pathobionts in human gut via an IL-22-dependent mechanism that is dysregulated in CD.

immunology↗

Enterovirus-A71 exploits Rab11 to recruit chaperones for virus morphogenesis

Enterovirus 71 (EV-A71) causes Hand, Foot and Mouth Disease (HFMD) in children and has been associated with neurological complications. A siRNA screen in EV-A71 infected-motor neurons identified small GTPase Rab11a as a pro-viral host factor. Rab11a and Rab11b isoforms were interchangeably exploited by strains from major EV-A71 genogroups and Coxsackievirus 16, another major causative agent of HFMD. We showed that Rab11 did not play a role in viral entry, IRES-mediated protein translation, or viral genome replication, although it co-localized with replication organelles. GTPase-defective Rab11 mutants had no effect on EV-A71 replication, ruling out Rab11 involvement in intracellular trafficking of viral or host components. Instead, reduced VP2:VP0 ratio in siRab11-treated cells supported a role in provirion maturation. Co-immunoprecipitation and mass spectrometry revealed chaperones as Rab11 top interacting partners during infection. Among which, CCT8 subunit of the chaperone complex TRiC/CCT was found to interact with viral structural proteins specifically. Together, this study describes a novel, unconventional role for Rab11 during viral infection, where it participates in the complex process of virus morphogenesis by recruiting essential chaperone proteins.

microbiology↗