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Publication Abstract from PubMed

Leptospira is a genus of spirochete bacteria highly motile that includes pathogenic species responsible to cause leptospirosis disease. Chemotaxis and motility are required for Leptospira infectivity, pathogenesis, and invasion of bacteria into the host. In prokaryotes, the most common chemoreceptors are methyl-accepting chemotaxis proteins that have a role play to detect the chemical signals and move to a favorable environment for its survival. Here, we report the first crystal structure of CACHE domain of the methyl-accepting chemotaxis protein (McpA) of L. interrogans. The structural analysis showed that McpA adopts similar alpha/beta architecture of several other bacteria chemoreceptors. We also found a typical dimerization interface that appears to be functionally crucial for signal transmission and chemotaxis. In addition to McpA structural analyses, we have identified homologous proteins and conservative functional regions using bioinformatics techniques. These results improve our understanding the relationship between chemoreceptor structures and functions of Leptospira species.

Structural analysis of CACHE domain of the McpA chemoreceptor from Leptospira interrogans.,Santos JC, Vieira ML, Abendroth J, Lin T, Staker BL, Myler PJ, Nascimento ALTO Biochem Biophys Res Commun. 2020 Dec 17;533(4):1323-1329. doi: , 10.1016/j.bbrc.2020.10.013. Epub 2020 Oct 21. PMID:33097187^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.