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Rv2617c and P36 are virulence factors of pathogenic mycobacteria involved in resistance to oxidative stress

Marina A Forrellad1, Cristina L Vázquez1, Federico C Blanco1

  • 1Institute of Biotechnology, National Institute of Agricultural Technology (INTA, Instituto de Biotecnología, Instituto Nacional de Tecnología Agropecuaria) and IABIMO-National Scientific and Technical Research Council (CONICET, Consejo Nacional de Investigaciones Científicas y Tecnológicas), Hurlingham, Buenos Aires, Argentine.

Virulence
|November 30, 2019
PubMed

Insights

Rv2617c, a protein unique to Mycobacterium tuberculosis, is crucial for pathogen virulence. Its absence impairs replication and enhances phagolysosomal trafficking, highlighting its role in oxidative stress resistance.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Immunology

Background:

  • Rv2617c is a protein of unknown function found in Mycobacterium tuberculosis complex (MTC) and Mycobacterium leprae.
  • Rv2617c interacts with virulence factor P36 (Erp) and KdpF, a protein associated with nitrosative stress.

Purpose of the Study:

  • To characterize the role of Rv2617c in Mycobacterium tuberculosis virulence.
  • To investigate the involvement of Rv2617c and P36 in oxidative stress resistance.

Main Methods:

  • Gene knockout of Rv2617c in Mycobacterium tuberculosis CDC1551.
  • Infection of a mouse model.
  • In vitro hydrogen peroxide treatment assays.
  • Analysis of protein interactions.

Main Results:

  • Rv2617c knockout reduced Mycobacterium tuberculosis replication in mice.
  • Absence of Rv2617c favored mycobacteria trafficking to phagolysosomes.
  • Rv2617c and P36 are essential for resistance to hydrogen peroxide in Mycobacterium tuberculosis and Mycobacterium bovis, respectively.

Conclusions:

  • Rv2617c plays a significant role in Mycobacterium tuberculosis virulence.
  • Rv2617c and P36 function together to protect bacteria from oxidative stress damage.
Keywords:
ErpMycobacterium tuberculosisRv2617coxidative stressvirulence factor

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