In this study, we characterized the role of Rv2617c in the virulence of . Rv2617c is a protein of unknown function unique to complex (MTC) and , this protein interacts with the virulence factor P36 (also named Erp) and KdpF, a protein linked to nitrosative stress. Here, we showed that knockout of the gene in CDC1551 reduced the replication of the pathogen in a mouse model of infection and favored the trafficking of mycobacteria to phagolysosomes. We also demonstrated that Rv2617c and P36 are required for resistance to hydrogen peroxide treatment in and , respectively. These findings indicate Rv2617c and P36 act in concert to prevent bacterial damage upon oxidative stress.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6930017 | PMC |
http://dx.doi.org/10.1080/21505594.2019.1693714 | DOI Listing |
Virulence
December 2019
Institute 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.
In this study, we characterized the role of Rv2617c in the virulence of . Rv2617c is a protein of unknown function unique to complex (MTC) and , this protein interacts with the virulence factor P36 (also named Erp) and KdpF, a protein linked to nitrosative stress. Here, we showed that knockout of the gene in CDC1551 reduced the replication of the pathogen in a mouse model of infection and favored the trafficking of mycobacteria to phagolysosomes.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!