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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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			Action	DRS
	MS1CF.group	Other
	MS1CF.wiff	Wiff
	MS1CF__FDR.xlsx	Xlsx
	MS1_pallet.group	Other
	MS1_pallet.wiff	Wiff

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Publications

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

Similar Datasets

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

Project description: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 both Mtb (pathogenic) and Msm (non-pathogenic) remain uniform across all in vitro growth phases. Despite such tight maintenance of PepNs' steady state levels, upon supplementation, Mtb alone allows accumulation of any excessive PepN. In contrast, Msm does not. It not only proteolyzes, but also secretes out the excessive PepN, be it native or foreign. Interestingly, while PepNMtb is required for modulating virulence in vivo, PepNMsm is essential for Msm growth in vitro. Despite such essentiality difference, both PepNMtb and PepNMsm harbor almost identical N-terminal M1-type peptidase domains that significantly align in their amino acid sequences and overlap in their secondary structures. Their C-terminal ERAP1_C-like domains however align much more moderately. Our in vitro macrophage-based infection experiments with MtbΔpepN-expressing pepNMsm reveals PepNMsm also retaining the ability to reach host cytosol. Lastly, but notably, we determined the PepNMtb and PepNMsm interactomes and found them to barely coincide. While PepNMtb chiefly interacts with Mtb's secreted proteins, PepNMsm primarily coimmunoprecipitates with Msm's housekeeping proteins. Thus, despite high sequence homology and several common properties, our comparative analytical study reveals host-centric traits of pathogenic and bacterial-centric traits of non-pathogenic PepNs.

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Macrophage proteome in response to Mycobacterium tuberculosis infection

Project description:This study investigates the proteomic alterations in human monocytic cell line (THP1) subsequent to infection with different strains of mycobacterium tuberculosis (H37Ra, H37Rv, BND433 and JAL2287) using the SWATH-MS strategy. THP1 proteome was analysed after 6, 18, 30 and 42 hours of infection with each strains and compared to that of uninfected cells. Our findings reveal temporal regulation of host response subsequent to Mtb infection.

2020-09-23 | PXD009046 | Pride

Macrophage proteome in response to Mycobacterium tuberculosis infection

2021-01-05 | PXD022352 | Pride

Deciphering Early Pathogenic Changes in Alzheimer's disease

Project description:The aim of the present project is to detect biochemical alterations that can pinpoint specific pathogenic processes at early phases of AD, evaluated in the cerebrospinal fluid, that more closely reflect the pathogenic processes in the brain, and independently of whether an amyloid response was triggered.

2024-05-24 | PXD039563 | Pride

Understanding the antimicrobial mechanism of TiO2-based nanocomposite films in a pathogenic bacterium

Project description:Understanding the antimicrobial mechanism of TiO2-based nanocomposite films in a pathogenic bacterium.

2014-04-16 | PXD000732 | Pride

Global transcriptomic investigation of the human macrophage response towards pathogenic/non-pathogenic mycobacteria

Project description:We present an infection study with pathogenic and non-pathogenic mycobacterial strains that have vastly different characteristics. The early/late host response to infection with these detergent-free cultured strains will be analysed through Ampliseq and further validated through qPCR in an attempt to provide information on the subtleties which may ultimately contribute to the virulent phenotype. Proceeding to the next objective of the study is to knock-down (siRNA)/knock-up (saRNA) selected differentially expressed mRNA to study their role in the intracellular survival of M. tuberculosis

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Global transcriptomic investigation of the human macrophage response towards pathogenic/non-pathogenic mycobacteria

Project description:Global transcriptomic investigation of the human macrophage response towards pathogenic/non-pathogenic mycobacteria

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Colon LC-MSMS of Mouse with experimental colitis

Project description:To detect the protein expression of Mouse with experimental colitis

2022-02-17 | PXD026228 | Pride

Canine subcellular Proteomics

Project description:To facilitate canine proteomics research, we have generated a non-redundant canine protein sequence database, with entry name annotation based on sequence similarity to the human proteome. To evaluate the sequence-based annotation transfer, we performed a shotgun proteomics experiment on subcellular fractions of canine spleen.

2022-03-02 | PXD003847 | Pride

Comparative analysis of homologous aminopeptidase PepN from Mycobacterium tuberculosis and Mycobacterium smegmatis reveals dichotomy of traits

Project description:Bacterial pathogens exploit secreted aminopeptidases to modulate host cellular functions. Mycobacterium tuberculosis (Mtb) secretes PepN, a M1 aminopeptidase with N-terminal peptidase and C-terminal ERAP1_C-like domains. In addition to being conserved across Mtb complex, PepNMtb is also homologous (78% amino acids identity) to PepN of M. smegmatis (Msmeg), a non-pathogenic mycobacterium. Despite high homogeneity, PepNMtb and PepNMsmeg exhibit opposing traits thus providing insights into their plausible bacterial/host-specific functions. Our biochemical studies show that, while both PepNs uniformly accumulate across all stages of in vitro growth, unlike Mtb, Msmeg is intolerant to over accumulation of its PepN and hence robustly proteolyzes it. Our proteomic analyses indicate Msmeg also secreting some of its excess PepN into its culture supernatant. In contrast, Mtb does not excessively secrete or proteolyse its over accumulating PepNMtb. Our fractionation studies show Mtb translocating its full length PepNMtb into its membrane and cell wall fractions. Instead, Msmeg accumulates its full length PepNMsmeg in its cytosol, and promotes its cleaved (~40 kDa) form to locate into subcellular fractions. PepNMtb is redundant for Mtb’s in vitro growth and thus Mtb is readily amenable to ΔpepN generation. Opposingly, PepNMsmeg is necessary but not sufficient for Msmeg growth in vitro. Given such disparity, co-immunoprecipitation studies on both PepNs predictably showed divergent interactomes with minimal common hits. In our in vitro infection studies, PepNMtb localizes host endoplasmic reticulum directing us to its potential host-specific role. In summary, our study provides insights into PepNs dichotomy despite them being conserved across pathogenic and non-pathogenic mycobacterial species.

2019-07-29 | PXD009164 | Pride