Document Type
Article
Publication Date
6-21-2019
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.
Recommended Citation
Cingolani, Gino; McCauley, Michael; Lobley, Anna; Bryer, Alexander J; Wesolowski, Jordan; Greco, Deanna L; Lokareddy, Ravi K; Ronzone, Erik; Perilla, Juan R; and Paumet, Fabienne, "Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA." (2019). Department of Biochemistry and Molecular Biology Faculty Papers. Paper 156.
https://jdc.jefferson.edu/bmpfp/156
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
PubMed ID
31227715
Comments
This article has been peer reviewed. It was published in: Nature Communications.
2019 Jun 21;10(1):2747.
The published version is available at DOI: 10.1038/s41467-019-10806-9
Copyright © 2019, The Author(s).
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