Journal
CELL BIOLOGY INTERNATIONAL
Volume 41, Issue 4, Pages 433-446Publisher
WILEY
DOI: 10.1002/cbin.10739
Keywords
host-pathogen interaction; Rab34; Salmonella; SopD2
Categories
Funding
- National Health and Medical Research Council (NHMRC) of Australia [606788, APP1098710]
- Australian Research Council [DP150100364]
- Australian Research Council Discovering Early Career Researcher Award [DE120102321]
- NHMRC Senior Research Fellowship [APP1041929, APP1003021]
- Australian Research Council [DE120102321] Funding Source: Australian Research Council
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Many intracellular pathogens have evolved highly specialized mechanisms to isolate themselves from the host cell's innate immune response while still obtaining the necessary nutrients to survive. Salmonella utilizes type 3 secretion systems (T3SSs) to deliver bacterial proteins called effectors, across the encompassing Salmonella Containing vacuole (SCV) membrane, to subvert the host's membrane trafficking pathways and alter other cellular processes. The Salmonella Pathogenicity Island (SPI)-2 effector SopD2 has recently been demonstrated to modulate multiple members of the Rab GTPase family such as Rab7, Rab8, Rab10, and Rab32 (D'Costa et al., 2015, Cell Reports, 12: 1508-18; Spano et al., 2016, Cell Host & Microbe, 19: 216-26). Here, we demonstrate the additional capacity of SopD2 to bind Rab34 and modulate its function. Our data indicate that depletion of Rab34 delays maturation of the SCV, and consequently, inhibits intracellular Salmonella enterica serotype typhimurium (S. typhimurium) growth. Interestingly, intracellular growth of the S. typhimurium lacking SopD2 was severely impaired in Rab34-depleted cells, suggesting a compounding virulence effect. Overall this study reveals an additional member of the Rab GTPase family, Rab34, that is modulated by SopD2 and provides insight into its role in Salmonella biology.
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