Salmonella effector SopD promotes plasma membrane scission by inhibiting Rab10

Kirsten C. Boddy, Hongxian Zhu, Vanessa M. D’Costa, Caishuang Xu, Ksenia Beyrakhova, Miroslaw Cygler, Sergio Grinstein, Etienne Coyaud, Estelle M. N. Laurent, Jonathan St-Germain, Brian Raught and John H. Brumell ()
Additional contact information
Kirsten C. Boddy: Hospital for Sick Children
Hongxian Zhu: Hospital for Sick Children
Vanessa M. D’Costa: Hospital for Sick Children
Caishuang Xu: University of Saskatchewan
Ksenia Beyrakhova: University of Saskatchewan
Miroslaw Cygler: University of Saskatchewan
Sergio Grinstein: Hospital for Sick Children
Etienne Coyaud: University Health Network
Estelle M. N. Laurent: University Health Network
Jonathan St-Germain: University Health Network
Brian Raught: University Health Network
John H. Brumell: Hospital for Sick Children

Nature Communications, 2021, vol. 12, issue 1, 1-15

Abstract: Abstract Salmonella utilizes translocated virulence proteins (termed effectors) to promote host cell invasion. The effector SopD contributes to invasion by promoting scission of the plasma membrane, generating Salmonella-containing vacuoles. SopD is expressed in all Salmonella lineages and plays important roles in animal models of infection, but its host cell targets are unknown. Here we show that SopD can bind to and inhibit the small GTPase Rab10, through a C-terminal GTPase activating protein (GAP) domain. During infection, Rab10 and its effectors MICAL-L1 and EHBP1 are recruited to invasion sites. By inhibiting Rab10, SopD promotes removal of Rab10 and recruitment of Dynamin-2 to drive scission of the plasma membrane. Together, our study uncovers an important role for Rab10 in regulating plasma membrane scission and identifies the mechanism used by a bacterial pathogen to manipulate this function during infection.

Date: 2021
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DOI: 10.1038/s41467-021-24983-z

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