Interaction of Erp Protein of Mycobacterium tuberculosis with Rv2212 Enhances Intracellular Survival of Mycobacterium smegmatis.

Ganaie, Arsheed Ahmad and Trivedi, Garima and Kaur, Amanpreet and Jha, Sidharth Shankar and Anand, Shashi and Rana, Vibhuti and Singh, Amit and Kumar, Shekhar and Sharma, Charu (2016) Interaction of Erp Protein of Mycobacterium tuberculosis with Rv2212 Enhances Intracellular Survival of Mycobacterium smegmatis. Journal of bacteriology, 198 (20). pp. 2841-52. ISSN 1098-5530

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Official URL: http://jb.asm.org/content/198/20/2841.long

Abstract

The Mycobacterium tuberculosis exported repetitive protein (RvErp) is a crucial virulence-associated factor as determined by its role in the survival and multiplication of mycobacteria in cultured macrophages and in vivo Although attempts have been made to understand the function of Erp protein, its exact role in Mycobacterium pathogenesis is still elusive. One way to determine this is by searching for novel interactions of RvErp. Using a yeast two-hybrid assay, an adenylyl cyclase (AC), Rv2212, was found to interact with RvErp. The interaction between RvErp and Rv2212 is direct and occurs at the endogenous level. The Erp protein of Mycobacterium smegmatis (MSMEG_6405, or MsErp) interacts neither with Rv2212 nor with Ms_4279, the M. smegmatis homologue of Rv2212. Deletion mutants of Rv2212 revealed its adenylyl cyclase domain to be responsible for the interaction. RvErp enhances Rv2212-mediated cyclic AMP (cAMP) production. Also, the biological significance of the interaction between RvErp and Rv2212 was demonstrated by the enhanced survival of M. smegmatis within THP-1 macrophages. Taken together, these studies address a novel mechanism by which Erp executes its function.

Item Type: Article
Additional Information: Copyright of this article belongs to ASM.
Uncontrolled Keywords: M. tuberculosis.
Subjects: Q Science > QR Microbiology
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 29 Sep 2016 10:47
Last Modified: 29 Sep 2016 10:47
URI: http://crdd.osdd.net/open/id/eprint/1865

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