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Biochim Biophys Acta Proteins Proteom. 2018 May - Jun;1866(5-6):712-721. doi: 10.1016/j.bbapap.2018.04.006. Epub 2018 Apr 12.

Proteomic approach and expression analysis revealed the differential expression of predicted leptospiral proteases capable of ECM degradation.

Author information

1
Regional Medical Research Centre (ICMR), Post Bag No-13, Port Blair 744101, Andaman and Nicobar Islands, India; Department of Chemical Sciences, Ariel University, Ariel 70400, Israel.
2
Regional Medical Research Centre (ICMR), Post Bag No-13, Port Blair 744101, Andaman and Nicobar Islands, India.
3
Institute of Bioinformatics, International Technology Park, Bangalore 560066, India; YU-IOB Center for Systems Biology and Molecular Medicine, Yenepoya University, Mangalore 575018, India.
4
Institute of Bioinformatics, International Technology Park, Bangalore 560066, India; Amrita School of Biotechnology, Amrita Vishwa Vidyapeetham, Kollam 690525, India.
5
Institute of Bioinformatics, International Technology Park, Bangalore 560066, India; Manipal University, Madhava Nagar, Manipal 576104, India.
6
School of Biological Sciences, Madurai Kamaraj University, Madurai 625021, Tamil Nadu, India.
7
Microbiology Division, Jawaharlal Nehru Tropical Botanic Garden, & Research Institute, Pacha, Palode PO, Thiruvananthapuram 695562, Kerala, India; Department of Botany, Institute of Science, Banaras Hindu University, Varanasi 221 005, Uttar Pradesh, India.
8
Institute of Bioinformatics, International Technology Park, Bangalore 560066, India; YU-IOB Center for Systems Biology and Molecular Medicine, Yenepoya University, Mangalore 575018, India; NIMHANS-IOB Proteomics and Bioinformatics Laboratory, Neurobiology Research Centre, National Institute of Mental Health and Neurosciences, Bangalore 560029, India.
9
Regional Medical Research Centre (ICMR), Post Bag No-13, Port Blair 744101, Andaman and Nicobar Islands, India. Electronic address: madanan.mg@icmr.gov.in.

Abstract

Leptospira, the causative agent of leptospirosis is known to have many proteases with potential to degrade extracellular matrix. However, a multipronged approach to identify, classify, characterize and elucidate their role has not been attempted. Our proteomic approach using high-resolution LC-MS/MS analysis of Triton X-114 fractions of Leptospira interrogans resulted in the identification of 104 proteases out of 130 proteases predicted by MEROPS. In Leptospira approximately 3.5% of the genome complements for proteases, which include catalytic types of metallo-, serine-, cysteine-, aspartic-, threonine- and asparagine- peptidases. Comparison of proteases from different serovars revealed that M04, M09B, M14A, M75, M28A, A01 and U73 protease families are exclusively present in pathogenic form. The M23 and S33 protease families are represented with >14 members in Leptospira. The differential expression under physiological temperature (37 °C) and osmolarity (300 mOsM) showed that proteases belonging to the catalytic type of Metallo-peptidases are upregulated significantly in pathogenic conditions. In silico prediction and characterization of the proteases revealed that several proteases are membrane anchored and secretory, classical as well as non-classical system. The study demonstrates the diversity and complexity of proteases, while maintaining conservation across the serovars in Leptospira and their differential expression under pathogenic conditions.

KEYWORDS:

Leptospira; Metalloprotease; Pathogenesis; Protease; Proteomics; Triton X-114

PMID:
29654978
DOI:
10.1016/j.bbapap.2018.04.006
[Indexed for MEDLINE]

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