1. Leptospiral cell wall hydrolase (LIC_10271) binding peptidoglycan, lipopolysaccharide, and laminin and the protein show LysM and M23 domains are co-existing in pathogenic species.
- Author
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Sarma A, Dhandapani G, Phukan H, Bhunia PK, De AK, Bhattacharya D, Jebasingh T, and Madanan MG
- Subjects
- Humans, Laminin metabolism, Lipopolysaccharides metabolism, Peptidoglycan metabolism, Hydrolases metabolism, Cell Wall metabolism, Protein Binding, Leptospira interrogans genetics, Leptospira interrogans metabolism, Leptospira genetics
- Abstract
Leptospirosis, a global reemerging zoonosis caused by the spirochete Leptospira, has severe human and veterinary implications. Cell wall hydrolase (LIC_10271) with LytM (peptidase M23) and LysM domains are found to be associated with various pathogenic bacteria. These domains regulate effects on extracellular matrix and biofilm components, which promote cell wall remodeling and pathogen dissemination in the host. In this study, we present the cloning, expression, purification, and characterization of LIC_10271. To determine the localization of LIC_10271 within the inner membrane of Leptospira, Triton X-114 subcellular fractionation and immunoblot studies were performed. Furthermore, r-LIC_10271 binds with peptidoglycan, lipopolysaccharide, and laminin in a dose-dependent manner. Analysis of the signal peptide, M23, and LysM domains revealed conservation primarily within the P1 group of Leptospira, which encompasses the most pathogenic species. Moreover, the presence of native-LIC_10271 in the inner membrane and the distribution of M23 and LysM domains across pathogenic strains indicates their potential involvement in the interaction between the host and Leptospira., Competing Interests: Declaration of competing interest The authors declare no conflict of interest in any aspect., (Copyright © 2023 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.)
- Published
- 2023
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