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Immunodominant protein MIP _05962 from Mycobacterium indicus pranii displays chaperone activity
Author(s) -
Sharma Ashish,
Equbal Md. Javed,
Pandey Saurabh,
Sheikh Javaid A.,
Ehtesham Nasreen Z.,
Hasnain Seyed E.,
Chaudhuri Tapan K.
Publication year - 2017
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14057
Subject(s) - proteome , chaperone (clinical) , proteostasis , protein aggregation , heat shock protein , biology , mycobacterium tuberculosis , escherichia coli , biochemistry , microbiology and biotechnology , chemistry , tuberculosis , medicine , pathology , gene
Tuberculosis, a contagious disease of infectious origin is currently a major cause of deaths worldwide. Mycobacterium indicus pranii ( MIP ), a saprophytic nonpathogen and a potent immunomodulator is currently being investigated as an intervention against tuberculosis along with many other diseases with positive outcome. The apparent paradox of multiple chaperones in mycobacterial species and enigma about the cellular functions of the client proteins of these chaperones need to be explored. Chaperones are the known immunomodulators; thus, there is need to exploit the proteome of MIP for identification and characterization of putative chaperones. One of the immunogenic proteins, MIP _05962 is a member of heat shock protein ( HSP ) 20 family due to the presence of α‐crystallin domain, and has amino acid similarity with Mycobacterium leprae HSP 18 protein. The diverse functions of M. leprae HSP 18 in stress conditions implicate MIP _05962 as an important protein that needs to be explored. Biophysical and biochemical characterization of the said protein proved it to be a chaperone. The observations of aggregation prevention and refolding of substrate proteins in the presence of MIP _05962 along with interaction with non‐native proteins, surface hydrophobicity, formation of large oligomers, in‐vivo thermal rescue of Escherichia coli expressing MIP _05962, enhancing solubility of insoluble protein maltodextrin glucosidase (MalZ) under in‐vivo conditions, and thermal stability and reversibility confirmed MIP _05962 as a molecular chaperone.