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Published on: December 12, 2017
Structural analysis of CACHE domain of the McpA chemoreceptor from Leptospira interrogans
Jademilson C Santos1, Mônica L Vieira2, Jan Abendroth3
1Laboratório de Desenvolvimento de Vacinas, Instituto Butantan, Avenida Vital Brasil, 1500, 05503-900, São Paulo, SP, Brazil.
Abstract:
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 α/β 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.
Insights
We determined the crystal structure of a key chemoreceptor in Leptospira interrogans, revealing insights into how these pathogenic bacteria sense signals and move. This structural understanding is crucial for developing new strategies against leptospirosis.
Area of Science:
- Microbiology
- Structural Biology
- Biochemistry
Background:
- Leptospira are motile spirochete bacteria causing leptospirosis.
- Bacterial chemotaxis and motility are vital for Leptospira pathogenesis and host invasion.
- Methyl-accepting chemotaxis proteins (MCPs) are crucial prokaryotic chemoreceptors for environmental sensing.
Purpose of the Study:
- To determine the first crystal structure of the CACHE domain of methyl-accepting chemotaxis protein A (McpA) from Leptospira interrogans.
- To elucidate the structural basis of chemoreceptor function in Leptospira.
- To identify homologous proteins and conserved functional regions in Leptospira chemoreceptors using bioinformatics.
Main Methods:
- X-ray crystallography to determine the 3D structure of McpA's CACHE domain.
- Structural analysis to identify conserved architectural features and functional interfaces.
- Bioinformatic analyses to identify homologous MCPs and conserved regions in Leptospira.
Main Results:
- The crystal structure of the L. interrogans McpA CACHE domain was determined, revealing an alpha/beta architecture common to bacterial chemoreceptors.
- A functionally significant dimerization interface was identified, crucial for signal transduction.
- Homologous proteins and conserved functional regions were identified across Leptospira species, suggesting conserved chemotaxis mechanisms.
Conclusions:
- The structural and bioinformatics data provide fundamental insights into Leptospira chemoreceptor mechanisms.
- Understanding McpA structure and function aids in deciphering Leptospira's chemotaxis and pathogenesis.
- This work lays the groundwork for future studies on Leptospira signaling pathways and potential therapeutic targets.
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