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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Structural analysis of CACHE domain of the McpA chemoreceptor from Leptospira interrogans

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Author(s):
Santos, Jademilson C. [1] ; Vieira, Monica L. [2] ; Abendroth, Jan [3, 4] ; Lin, Tao [5] ; Staker, Bart L. [6, 4] ; Myler, Peter J. [6, 4, 7, 8] ; Nascimento, Ana Lucia T. O. [1]
Total Authors: 7
Affiliation:
[1] Inst Butantan, Lab Desenvolvimento Vacinas, Ave Vital Brasil 1500, BR-05503900 Sao Paulo, SP - Brazil
[2] Univ Fed Minas Gerais UFMG, Inst Ciencias Biol ICB, Dept Microbiol, Belo Horizonte, MG - Brazil
[3] UCB Pharma SA, 7869 NE Day Rd West, Bainbridge Isl, WA 98110 - USA
[4] Seattle Struct Genom Ctr Infect Dis, Seattle, WA 98109 - USA
[5] Baylor Coll Med, Dept Mol Virol & Microbiol, Houston, TX 77030 - USA
[6] Seattle Childrens Res Inst, Seattle, WA 98109 - USA
[7] Univ Washington, Dept Pediat, Dept Biomed Informat & Hlth Educ, Seattle, WA 98105 - USA
[8] Univ Washington, Dept Global Hlth, Seattle, WA 98105 - USA
Total Affiliations: 8
Document type: Journal article
Source: Biochemical and Biophysical Research Communications; v. 533, n. 4, p. 1323-1329, DEC 17 2020.
Web of Science Citations: 0
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 a/b 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. (C) 2020 Elsevier Inc. All rights reserved. (AU)

FAPESP's process: 17/25167-6 - Structural characterization of surface proteins of Leptospira interrogans and thermodynamics of the interaction with host-components
Grantee:Jademilson Celestino dos Santos
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 14/50981-0 - Search for surface proteins among the genome sequences of Leptospira interrogans: functional and immunological characterization to understanding mechanisms involved in the bacterial pathogenesis
Grantee:Ana Lucia Tabet Oller do Nascimento
Support Opportunities: Research Projects - Thematic Grants