Towards understanding the biological function of the unusual chaperonin Cpn60.1 (GroEL1) of Mycobacterium tuberculosis

Tuberculosis
Aditi SharmaShekhar C Mande

Abstract

The 60 kDa heat shock proteins, also known as Cpn60s (GroELs) are components of the essential protein folding machinery of the cell, but are also dominant antigens in many infectious diseases. Although generally essential for cellular survival, in some organisms such as Mycobacterium tuberculosis, one or more paralogous Cpn60s are known to be dispensable. In M. tuberculosis, Cpn60.2 (GroEL2) is essential for cell survival, but the biological role of the non-essential Cpn60.1 (GroEL1) is still elusive. To understand the relevance of Cpn60.1 (GroEL1) in M. tuberculosis physiology, detailed transcriptomic analyses for the wild type H37Rv and cpn60.1 knockout (groEL1-KO) were performed under in vitro stress conditions: stationary phase, cold shock, low aeration, mild cold shock and low pH. Additionally, the survival of the groEL1-KO was assessed in macrophages at multiplicity of infection (MOI) of 1:1 and 1:5. We observed that survival under low aeration was significantly compromised in the groEL1-KO. Further, the gene expression analyses under low aeration showed change in expression of several key virulence factors like two component system PhoP/R and MprA/B, sigma factors SigM and C and adversely affected known hypoxia response ...Continue Reading

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Citations

Aug 4, 2018·Journal of Medical Microbiology·Ciamak Ghazaei, Marie Line El Helou
Aug 19, 2020·FEBS Letters·Mohammed Yousuf AnsariShekhar C Mande
Oct 2, 2019·The Indian Journal of Medical Research·Durga Bisht, Laxman S Meena
Aug 20, 2020·Metallomics : Integrated Biometal Science·Dong YangVéronique Fontaine
Apr 27, 2018·Frontiers in Molecular Biosciences·Mohammed Y Ansari, Shekhar C Mande
May 25, 2021·Biofouling·Esmeralda Ivonne Niño-PadillaAdriana Garibay-Escobar

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