Abstract:
:Intracellular pathogens like Shigella flexneri enter host cells by phagocytosis. Once inside, the pathogen breaks the vacuolar membrane for cytosolic access. The fate and function of the vacuolar membrane remnants are not clear. Examining Shigella-infected nonmyeloid cells, we observed that proteins associated with vacuolar membrane remnants are polyubiquinated, recruit the autophagy marker LC3 and adaptor p62, and are targeted to autophagic degradation. Further, inflammasome components and caspase-1 were localized to these membranes and correlated with dampened inflammatory response and necrotic cell death. In Atg4B mutant cells in which autophagosome maturation is blocked, polyubiquitinated proteins and P62 accumulated on membrane remnants, and as in autophagy-deficient Atg5(-/-) cells, the early inflammatory and cytokine response was exacerbated. Our results suggest that host membranes, after rupture by an invading cytoplasm-targeted bacterium, contribute to the cellular responses to infection by acting as a signaling node, with autophagy playing a central role in regulating these responses.
journal_name
Cell Host Microbejournal_title
Cell host & microbeauthors
Dupont N,Lacas-Gervais S,Bertout J,Paz I,Freche B,Van Nhieu GT,van der Goot FG,Sansonetti PJ,Lafont Fdoi
10.1016/j.chom.2009.07.005subject
Has Abstractpub_date
2009-08-20 00:00:00pages
137-49issue
2eissn
1931-3128issn
1934-6069pii
S1931-3128(09)00250-9journal_volume
6pub_type
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