Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA

Gino Cingolani (), Michael McCauley, Anna Lobley, Alexander J. Bryer, Jordan Wesolowski, Deanna L. Greco, Ravi K. Lokareddy, Erik Ronzone, Juan R. Perilla and Fabienne Paumet ()
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Gino Cingolani: Thomas Jefferson University, Department of Biochemistry and Molecular Biology
Michael McCauley: Thomas Jefferson University, Department of Microbiology and Immunology
Anna Lobley: Thomas Jefferson University, Department of Microbiology and Immunology
Alexander J. Bryer: The University of Delaware, Department of Chemistry and Biochemistry
Jordan Wesolowski: Thomas Jefferson University, Department of Microbiology and Immunology
Deanna L. Greco: The University of Delaware, Department of Chemistry and Biochemistry
Ravi K. Lokareddy: Thomas Jefferson University, Department of Biochemistry and Molecular Biology
Erik Ronzone: Thomas Jefferson University, Department of Microbiology and Immunology
Juan R. Perilla: The University of Delaware, Department of Chemistry and Biochemistry
Fabienne Paumet: Thomas Jefferson University, Department of Microbiology and Immunology

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: Abstract Many intracellular bacteria, including Chlamydia, establish a parasitic membrane-bound organelle inside the host cell that is essential for the bacteria’s survival. Chlamydia trachomatis forms inclusions that are decorated with poorly characterized membrane proteins known as Incs. The prototypical Inc, called IncA, enhances Chlamydia pathogenicity by promoting the homotypic fusion of inclusions and shares structural and functional similarity to eukaryotic SNAREs. Here, we present the atomic structure of the cytoplasmic domain of IncA, which reveals a non-canonical four-helix bundle. Structure-based mutagenesis, molecular dynamics simulation, and functional cellular assays identify an intramolecular clamp that is essential for IncA-mediated homotypic membrane fusion during infection.

Date: 2019
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DOI: 10.1038/s41467-019-10806-9

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