Legionella DotM structure reveals a role in effector recruiting to the Type 4B secretion system

Amit Meir, David Chetrit, Luying Liu, Craig R. Roy and Gabriel Waksman ()
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Amit Meir: Institute of Structural and Molecular Biology
David Chetrit: Yale University
Luying Liu: Yale University
Craig R. Roy: Yale University
Gabriel Waksman: Institute of Structural and Molecular Biology

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract Legionella pneumophila, a causative agent of pneumonia, utilizes the Type 4B secretion (T4BS) system to translocate over 300 effectors into the host cell during infection. T4BS systems are encoded by a large gene cluster termed dot/icm, three components of which, DotL, DotM, and DotN, form the “coupling complex”, which serves as a platform for recruitment of effector proteins. One class of effectors includes proteins containing Glu-rich/E-block sequences at their C terminus. However, the protein or region of the coupling complex mediating recruitment of such effectors is unknown. Here we present the crystal structure of DotM. This all alpha-helical structure exhibits patches of positively charged residues. We show that these regions form binding sites for acidic Glu-rich peptides and that mutants targeting these patches are defective in vivo in the translocation of acidic Glu-rich motif-containing effectors. We conclude that DotM forms the interacting surface for recruitment of acidic Glu-rich motif-containing Legionella effectors.

Date: 2018
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DOI: 10.1038/s41467-017-02578-x

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