ArticleThe Journal of biological chemistry2013
Truncated hemoglobin, HbN, is post-translationally modified in Mycobacterium tuberculosis and modulates host-pathogen interactions during intracellular infection.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 35 citations in OpenAlex.
- Group II truncated haemoglobin YjbI prevents reactive oxygen species-induced protein aggregation ineLife · 2022Article
- Effect of Protein O-Mannosyltransferase (MSMEG_5447) onFrontiers in microbiology · 2021Article
- Nitric Oxide Does Not Inhibit but Is Metabolized by the CytochromeInternational journal of molecular sciences · 2020Article
- Regulation of Three Virulence Strategies of Mycobacterium tuberculosis: A Success Story.International journal of molecular sciences · 2018Review
- Nitrosative stress defences of the enterohepatic pathogenic bacterium Helicobacter pullorum.Scientific reports · 2017Article
- Oxidative Phosphorylation as a Target Space for Tuberculosis: Success, Caution, and Future Directions.Microbiology spectrum · 2017Review
- Role of Glycosylation/Deglycolysation Processes inFrontiers in cellular and infection microbiology · 2017Review
- Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin.Cellular and molecular life sciences : CMLS · 2017Review
- Lipoprotein LprI of Mycobacterium tuberculosis Acts as a Lysozyme Inhibitor.The Journal of biological chemistry · 2016Article
- Deciphering the metabolic response of Mycobacterium tuberculosis to nitrogen stress.Molecular microbiology · 2015Article
- Mechanistic insight into the enzymatic reduction of truncated hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A motif in electron cycling.The Journal of biological chemistry · 2014Article
- Nitrosylation mechanisms of Mycobacterium tuberculosis and Campylobacter jejuni truncated hemoglobins N, O, and P.PloS one · 2014Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis (Mtb) is a phenomenally successful human pathogen having evolved mechanisms that allow it to survive within the hazardous environment of macrophages and establish long term, persistent infection in the host against the control of cell-mediated immunity. One such mechanism is mediated by the truncated hemoglobin, HbN, of Mtb that displays a potent O2-dependent nitric oxide dioxygenase activity and protects its host from the toxicity of macrophage-generated nitric oxide (NO). Here we demonstrate for the first time that HbN is post-translationally modified by glycosylation in Mtb and remains localized on the cell membrane and the cell wall. The glycan linkage in the HbN was identified as mannose. The elevated expression of HbN in Mtb and M. smegmatis facilitated their entry within the macrophages as compared with isogenic control cells, and mutation in the glycan linkage of HbN disrupted this effect. Additionally, HbN-expressing cells exhibited higher survival within the THP-1 and mouse peritoneal macrophages, simultaneously increasing the intracellular level of proinflammatory cytokines IL-6 and TNF-α and suppressing the expression of co-stimulatory surface markers CD80 and CD86. These results, thus, suggest the involvement of HbN in modulating the host-pathogen interactions and immune system of the host apart from protecting the bacilli from nitrosative stress inside the activated macrophages, consequently driving cells toward increased infectivity and intracellular survival.
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Registered trials
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