Proteome-scale identification and characterization of mitochondria targeting proteins of Mycobacterium avium

Aarti Rana1, Devender Kumar1, Abdur Rub2

  • 1School of Life Sciences, Central University of Himachal Pradesh, Shahpur, District-Kangra, 176206 Himachal Pradesh, India.

Mitochondrion
|June 7, 2015
PubMed

Insights

Mycobacterium avium subsp. paratuberculosis causes Johne's Disease in ruminants by targeting host mitochondria. Researchers identified 46 potential proteins that may help the bacteria survive and evade immune responses.

Area of Science:

  • Microbiology
  • Veterinary Science
  • Molecular Biology

Background:

  • Mycobacterium avium subsp. paratuberculosis (MAP) is the causative agent of Johne's Disease in ruminants.
  • MAP infection leads to physiological abnormalities in the host.
  • Mitochondria are crucial cellular components and potential targets for pathogens.

Purpose of the Study:

  • To identify proteins expressed by MAP that target host mitochondria.
  • To understand the role of these proteins in bacterial virulence and host immune evasion.

Main Methods:

  • A proteome-wide analysis was conducted.
  • Sequence and structural signatures were used to predict mitochondrial targeting.
  • Bioinformatic approaches were employed to identify candidate proteins.

Main Results:

  • 46 MAP proteins were identified as potential mitochondrial targeting factors.
  • These proteins may contribute to bacterial persistence within host cells.
  • The identified proteins could be virulence factors modulating mitochondrial function.

Conclusions:

  • MAP utilizes specific proteins to target host mitochondria for survival and immune evasion.
  • These identified proteins represent potential targets for therapeutic interventions against Johne's Disease.

Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
13.8K
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
6.0K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
5.2K