title: Immunodominant protein MIP_05962 from Mycobacterium indicus pranii displays chaperone activity.
abstract: 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 lepraeHSP18 protein. The diverse functions of M. lepraeHSP18 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.
authors.affiliation: Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, India.
authors.forename: Ashish
authors.initials: A
authors.lastname: Sharma
authors.affiliation: Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, India.
authors.forename: Md Javed
authors.initials: MJ
authors.lastname: Equbal
authors.affiliation: National Institute of Pathology, Safdarjung Hospital Campus, New Delhi, India.
authors.forename: Saurabh
authors.initials: S
authors.lastname: Pandey
authors.affiliation: National Institute of Pathology, Safdarjung Hospital Campus, New Delhi, India.
authors.forename: Javaid A
authors.initials: JA
authors.lastname: Sheikh
authors.affiliation: National Institute of Pathology, Safdarjung Hospital Campus, New Delhi, India.
authors.forename: Nasreen Z
authors.initials: NZ
authors.lastname: Ehtesham
authors.affiliation: Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, India.|Dr. Reddy's Institute of Life Sciences, University of Hyderabad Campus, India.
authors.forename: Seyed E
authors.initials: SE
authors.lastname: Hasnain
authors.affiliation: Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, India.
authors.forename: Tapan K
authors.initials: TK
authors.lastname: Chaudhuri
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002470:Cell Survival; D002950:Citrate (si)-Synthase / Q000737:chemistry / Q000378:metabolism*; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology / Q000502:physiology; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D050886:HSP20 Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018869:Heat-Shock Response; D006358:Hot Temperature / Q000009:adverse effects; D057927:Hydrophobic and Hydrophilic Interactions; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015269:Mycobacterium avium Complex / Q000378:metabolism*; D066329:Protein Aggregates; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D058849:Protein Refolding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012995:Solubility
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D050886:HSP20 Heat-Shock Proteins; D018832:Molecular Chaperones; D066329:Protein Aggregates; D011993:Recombinant Fusion Proteins; D002950:Citrate (si)-Synthase; D006026:Glycoside Hydrolases; C071233:malZ protein, E coli
keywords: MIP_05962; Mycobacterium indicus pranii (MIP); molecular chaperone; small heat shock protein; α-crystallin domain (ACD)