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A conserved aminopeptidase PepN, exhibits divergent traits in pathogenic and non- pathogenic mycobacteria

ABSTRACT: A conserved aminopeptidase PepN, exhibits divergent traits in pathogenic and non- pathogenic mycobacteria

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Mycobacterium Smegmatis (strain Atcc 700084 / Mc(2)155) Mycobacterium Tuberculosis H37rv

DISEASE(S): Tuberculosis

SUBMITTER: Renu Goel

LAB HEAD: Dr Krishnamohan Atmakuri

PROVIDER: PXD008790 | Pride | 2019-11-12

REPOSITORIES: Pride

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Comparative analysis of homologous aminopeptidase PepN from pathogenic and non-pathogenic mycobacteria reveals divergent traits.

Sharma Nishant N Aggarwal Suruchi S Kumar Saravanan S Sharma Rahul R Choudhury Konika K Singh Niti N Jayaswal Praapti P Goel Renu R Wajid Saima S Yadav Amit Kumar AK Atmakuri Krishnamohan K

PloS one 20190410 4

Mycobacterium tuberculosis (Mtb) secretes proteases and peptidases to subjugate its host. Out of its sixty plus proteases, atleast three are reported to reach host macrophages. In this study, we show that Mtb also delivers a lysyl alanine aminopeptidase, PepN (Rv2467) into host macrophage cytosol. Our comparative in silico analysis shows PepNMtb highly conserved across all pathogenic mycobacteria. Non-pathogenic mycobacteria including M. smegmatis (Msm) also encode pepN. PepN protein levels in b ...[more]

PMID: 30969995

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