Review Article: Virulence Factors of Mycobacterium Tuberculosis

Authors

  • Israa N. Al-Asady Department of Biology, College of Education for Pure Sciences, University of Mosul, Mosul, IRAQ.
  • Jassim Fatehi Ali Department of Biology, College of Education for Pure Sciences, University of Mosul, Mosul, IRAQ.

DOI:

https://doi.org/10.55544/jrasb.2.3.31

Keywords:

Mycobacterium tuberculosis, Pathogenicity, pulmonary infectious

Abstract

Mycobacterium tuberculosis (MTB) causes active TB infections that result in pulmonary tuberculosis (PTB), relapse even after treatment, and latent TB. Tuberculosis is a bacterium airborne pulmonary infectious disease. Extra pulmonary tuberculosis (EPTB) results from an illness which is too severe with Mycobacterium tuberculosis entering into the circulatory system. A really bad situation with further multi-drug TB. In the nation, pulmonary TB is spreading as well as reemerging. Recent findings of an increase in cases in the area pose a mortality burden and infection spread risk. The group of bacteria genetically organisms known as the Mycobacterium tuberculosis complex (MTBC) are accountable for human as well as animal tuberculosis. Among the primary reasons of mortality or morbidity worldwide continues to remain this sickness even now. The mycobacteria infiltrate the host via breathing that is phagocytated by macrophage as they reach the respiratory tract. It may cause the bacteria responsible to be quickly destroyed or cause an aggressive TB disease. Precisely a result of its human immunological reaction, multiple distinct virulence indicators have emerged among MTBC subgroups. The purpose of this research is to discuss the bacterial genes or enzymes that are to be crucial to determining the pathogenicity of MTBC strains through in vivo infections paradigm. As a way to eradicate various illnesses as well as get closer to a future without infections such as tuber emerging medicines or therapies must take into account the virulence aspects of MTBC.

Downloads

Download data is not yet available.

Metrics

Metrics Loading ...

References

Cohen A, Mathiasen VD, Schon T, et al. The global prevalence of latent tuberculosis: a systematic review and meta-analysis. Eur Respir J. 2019;54:1900655.

Chee CBE, Reves R, Zhang Y, et al. Latent tuberculosis infection: opportunities and challenges. Respirology. 2018;23:893–900.

Gong W, Wu X. Differential diagnosis of latent tuberculosis infection and active tuberculosis: a key to a successful tuberculosis control strategy. Front Microbiol. 2021;12:745592.

Fatima S, Kumari A, Das G, et al. Tuberculosis vaccine: a journey from BCG to present. Life Sci. 2020;252:117594.

Dockrell HM, Smith SG. What have we learnt about BCG vaccination in the last 20 years? Front Immunol. 2017;8:1134Darrah PA, Zeppa JJ, Maiello P, et al. Prevention of tuberculosis in macaques after intravenous BCG immunization. Nature. 2020;577:95–102.

Irvine EB, O’Neil A, Darrah PA, et al. Robust IgM responses following intravenous vaccination with Bacille Calmette-Guerin associate with prevention of Mycobacterium tuberculosis infection in macaques. Nat Immunol. 2021;22:1515–1523.

Pai M, Behr M. Latent mycobacterium tuberculosis infection and interferon-gamma release assays. Microbiol Spectr. 2016;4. DOI:10.1128/microbiolspec.TBTB2-0023-2016

Takwoingi Y, Whitworth H, Rees-Roberts M, et al. Interferon gamma release assays for Diagnostic Evaluation of Active tuberculosis (IDEA): test accuracy study and economic evaluation. Health Technol Assess. 2019;23:1–152.

Carranza C, Pedraza-Sanchez S, de Oyarzabal-Mendez E, et al. Diagnosis for latent tuberculosis infection: new alternatives. Front Immunol. 2020;11:2006.

Munoz L, Stagg HR, Abubakar I. Diagnosis and management of latent tuberculosis infection: table 1. Cold Spring Harb Perspect Med. 2015;5:a017830.

Huaman MA, Sterling TR. Treatment of latent tuberculosis infection-an update. Clin Chest Med. 2019;40:839–848.

Marx FM, Cohen T, Menzies NA, et al. Cost-effectiveness of post-treatment follow-up examinations and secondary prevention of tuberculosis in a high-incidence setting: a model-based analysis. Lancet Glob Health. 2020;8:e1223–33.

Dela Cruz CS, Lyons PG, Pasnick S, et al. Treatment of drug-susceptible tuberculosis. Ann Am Thorac Soc. 2016;13:2060–2063.

Nahid P, Dorman SE, Alipanah N, et al. Official American Thoracic Society/Centers for Disease Control and Prevention/Infectious Diseases Society of America Clinical Practice Guidelines: treatment of drug-susceptible tuberculosis. Clin Infect Dis. 2016;63:e147–95.

Peloquin CA, Davies GR. The treatment of tuberculosis. Clin Pharmacol Ther. 2021;110:1455–1466.

Ramachandran G, Swaminathan S. Safety and tolerability profile of second-line anti-tuberculosis medications. Drug Saf. 2015;38:253–269.

Quenard F, Fournier PE, Drancourt M, et al. Role of second-line injectable antituberculosis drugs in the treatment of MDR/XDR tuberculosis. Int J Antimicrob Agents. 2017;50:252–254. - PubMed

Scorpio A, Lindholm-Levy P, Heifets L, et al. Characterization of pncA mutations in pyrazinamide-resistant Mycobacterium tuberculosis. Antimicrob Agents Chemother. 1997;41:540–543. - PMC - PubMed

Conradie F, Diacon AH, Ngubane N, et al. Treatment of highly drug-resistant pulmonary tuberculosis. N Engl J Med. 2020;382:893–902.

Smith CM, Baker RE, Proulx MK, et al. Host-pathogen genetic interactions underlie tuberculosis susceptibility in genetically diverse mice. Elife. 2022;11. DOI:10.7554/eLife.74419.

Coscolla M, Gagneux S, Menardo F, et al. Phylogenomics of Mycobacterium africanum reveals a new lineage and a complex evolutionary history. Microb Genom. 2021;7. DOI:10.1099/mgen.0.000477.

Cardona PJ, Catala M, Prats C. Origin of tuberculosis in the Paleolithic predicts unprecedented population growth and female resistance. Sci Rep. 2020;10:42.

Napier G, Campino S, Merid Y, et al. Robust barcoding and identification of Mycobacterium tuberculosis lineages for epidemiological and clinical studies. Genome Med. 2020;12:114.

Rodrigues TS, Conti BJ, Fraga-Silva TFC, et al. Interplay between alveolar epithelial and dendritic cells and Mycobacterium tuberculosis. J Leukocyte Biol. 2020;108:1139–1156.

Khan HS, Nair VR, Ruhl CR, et al. Identification of scavenger receptor B1 as the airway microfold cell receptor for Mycobacterium tuberculosis. Elife. 2020;9. DOI:10.7554/eLife.52551.

Nair VR, Franco LH, Zacharia VM, et al. Microfold cells actively translocate mycobacterium tuberculosis to initiate infection. Cell Rep. 2016;16:1253–1258.

Cohen SB, Gern BH, Delahaye JL, et al. Alveolar macrophages provide an early mycobacterium tuberculosis niche and initiate dissemination. Cell Host Microbe. 2018;24:439–46 e4.

Lovey A, Verma S, Kaipilyawar V, et al. Early alveolar macrophage response and IL-1R-dependent T cell priming determine transmissibility of Mycobacterium tuberculosis strains. Nat Commun. 2022;13:884.

Carpenter SM, Lu LL. Leveraging antibody, B cell and Fc receptor interactions to understand heterogeneous immune responses in tuberculosis. Front Immunol. 2022;13:830482.

Cronan MR. In the thick of it: formation of the tuberculous granuloma and its effects on host and therapeutic responses. Front Immunol. 2022;13:820134.

Cohen SB, Gern BH, Urdahl KB. The tuberculous granuloma and preexisting immunity. Annu Rev Immunol. 2022;40:589–614.

Behr MA, Kaufmann E, Duffin J, et al. Latent tuberculosis: two centuries of confusion. Am J Respir Crit Care Med. 2021;204:142–148.

Behr MA, Edelstein PH, Ramakrishnan L. Is Mycobacterium tuberculosis infection life long? BMJ. 2019;367:l5770.

Lerner TR, Queval CJ, Lai RP, et al. Mycobacterium tuberculosis cords within lymphatic endothelial cells to evade host immunity. JCI Insight. 2020;5. DOI:10.1172/jci.insight.136937.

Barr DA, Schutz C, Balfour A, et al. Serial measurement of M. tuberculosis in blood from critically-ill patients with HIV-associated tuberculosis. EBioMedicine. 2022;78:103949.

Ruhl CR, Pasko BL, Khan HS, et al. Mycobacterium tuberculosis Sulfolipid-1 activates nociceptive neurons and induces cough. Cell. 2020;181:293–305 e11.

Shiloh MU. Mechanisms of mycobacterial transmission: how does Mycobacterium tuberculosis enter and escape from the human host. Future Microbiol. 2016;11:1503–1506.

Haas MK, Belknap RW. Updates in the treatment of active and latent tuberculosis. Semin Respir Crit Care Med. 2018;39:297–309.

Kock R, Michel AL, Yeboah-Manu D, et al. Zoonotic tuberculosis - the changing landscape. Int J Infect Dis. 2021;113 Suppl 1:S68–72.

Peterson EJ, Bailo R, Rothchild AC, et al. Path-seq identifies an essential mycolate remodeling program for mycobacterial host adaptation. Mol Syst Biol. 2019;15:e8584.

Batt SM, Minnikin DE, Besra GS. The thick waxy coat of mycobacteria, a protective layer against antibiotics and the host’s immune system. Biochem J. 2020;477:1983–2006.

Rahlwes KC, Sparks IL, Morita YS. Cell walls and membranes of actinobacteria. Subcell Biochem. 2019;92:417–469. Dulberger CL, Rubin EJ, Boutte CC. The mycobacterial cell envelope - a moving target. Nat Rev Microbiol. 2020;18:47–59.

Jackson M, Stevens CM, Zhang L, et al. Transporters involved in the biogenesis and functionalization of the mycobacterial cell envelope. Chem Rev. 2021;121:5124–5157.

Zamyatina A, Heine H. Lipopolysaccharide recognition in the crossroads of TLR4 and Caspase-4/11 mediated inflammatory pathways. Front Immunol. 2020;11:585146.

Layre E. Trafficking of mycobacterium tuberculosis envelope components and release within extracellular vesicles: host-pathogen interactions beyond the wall. Front Immunol. 2020;11:1230.

Augenstreich J, Briken V. Host cell targets of released lipid and secreted protein effectors of mycobacterium tuberculosis. Front Cell Infect Microbiol. 2020;10:595029.

Rens C, Chao JD, Sexton DL, et al. Roles for phthiocerol dimycocerosate lipids in Mycobacterium tuberculosis pathogenesis. Microbiology (Reading). 2021;167. DOI:10.1099/mic.0.001042 .

Iizasa E, Chuma Y, Uematsu T, et al. TREM2 is a receptor for non-glycosylated mycolic acids of mycobacteria that limits anti-mycobacterial macrophage activation. Nat Commun. 2021;12:2299.

Sharma NK, Rathor N, Sinha R, et al. Expression of mycolic acid in response to stress and association with differential clinical manifestations of tuberculosis. Int J Mycobacteriol. 2019;8:237–243.

Buter J, Cheng TY, Ghanem M, et al. Mycobacterium tuberculosis releases an antacid that remodels phagosomes. Nat Chem Biol. 2019;15:889–899.

Ghanem M, Dube JY, Wang J, et al. Heterologous production of 1-Tuberculosinyladenosine in mycobacterium kansasii models pathoevolution towards the transcellular lifestyle of mycobacterium tuberculosis. MBio. 2020;11. DOI:10.1128/mBio.02645-20.

Buter J, Heijnen D, Wan IC, et al. Stereoselective synthesis of 1-tuberculosinyl adenosine; a virulence factor of mycobacterium tuberculosis. J Org Chem. 2016;81:6686–6696.

Mishra M, Adhyapak P, Dadhich R, et al. Dynamic remodeling of the host cell membrane by virulent mycobacterial sulfoglycolipid-1. Sci Rep. 2019;9:12844.

Patin EC, Geffken AC, Willcocks S, et al. Trehalose dimycolate interferes with FcgammaR-mediated phagosome maturation through Mincle, SHP-1 and FcgammaRIIB signalling. PLoS ONE. 2017;12:e0174973.

Bowker N, Salie M, Schurz H, et al. Polymorphisms in the pattern recognition receptor mincle gene (CLEC4E) and association with tuberculosis. Lung. 2016;194:763–767.

Huber A, Kallerup RS, Korsholm KS, et al. Trehalose diester glycolipids are superior to the monoesters in binding to Mincle, activation of macrophages in vitro and adjuvant activity in vivo. Innate Immun. 2016;22:405–418.

Walton EM, Cronan MR, Cambier CJ, et al. Cyclopropane modification of trehalose dimycolate drives granuloma angiogenesis and mycobacterial growth through VEGF signaling. Cell Host Microbe. 2018;24:514–25 e6.

Feinberg H, Rambaruth ND, Jegouzo SA, et al. Binding sites for acylated trehalose analogs of glycolipid ligands on an extended carbohydrate recognition domain of the macrophage receptor mincle. J Biol Chem. 2016;291:21222–21233.

Kalscheuer R, Palacios A, Anso I, et al. The Mycobacterium tuberculosis capsule: a cell structure with key implications in pathogenesis. Biochem J. 2019;476:1995–2016.

Yuan C, Qu ZL, Tang XL, et al. Mycobacterium tuberculosis mannose-capped lipoarabinomannan induces IL-10-producing B cells and hinders CD4(+)Th1 immunity. iScience. 2019;11:13–30.

Stoop EJ, Mishra AK, Driessen NN, et al. Mannan core branching of lipo(arabino)mannan is required for mycobacterial virulence in the context of innate immunity. Cell Microbiol. 2013;15:2093–2108.

Toyonaga K, Torigoe S, Motomura Y, et al. C-Type lectin receptor DCAR recognizes mycobacterial phosphatidyl-inositol mannosides to promote a Th1 response during infection. Immunity. 2016;45:1245–1257.

Lugo-Villarino G, Troegeler A, Balboa L, et al. The C-Type lectin receptor DC-SIGN has an anti-inflammatory role in human M(IL-4) macrophages in response to mycobacterium tuberculosis. Front Immunol. 2018;9:1123.

Reijneveld JF, Holzheimer M, Young DC, et al. Synthetic mycobacterial diacyl trehaloses reveal differential recognition by human T cell receptors and the C-type lectin Mincle. Sci Rep. 2021;11:1.

Holzheimer M, Reijneveld JF, Ramnarine AK, et al. Asymmetric total synthesis of mycobacterial diacyl trehaloses demonstrates a role for lipid structure in immunogenicity. ACS Chem Biol. 2020;15:1835–1841.

Decout A, Silva-Gomes S, Drocourt D, et al. Rational design of adjuvants targeting the C-type lectin Mincle. Proc Natl Acad Sci U S A. 2017;114:2675–2680.

Rajaram MVS, Arnett E, Azad AK, et al. M. tuberculosis-initiated human mannose receptor signaling regulates macrophage recognition and vesicle trafficking by FcRgamma-Chain, Grb2, and SHP-1. Cell Rep. 2017;21:126–140.

Ishida E, Corrigan DT, Malonis RJ, et al. Monoclonal antibodies from humans with Mycobacterium tuberculosis exposure or latent infection recognize distinct arabinomannan epitopes. Commun Biol. 2021;4:1181.

Chang DPS, Guan XL. Metabolic versatility of mycobacterium tuberculosis during infection and dormancy. Metabolites. 2021;11:11.

Collins AC, Cai H, Li T, et al. Cyclic GMP-AMP synthase is an innate immune DNA sensor for mycobacterium tuberculosis. Cell Host Microbe. 2015;17:820–828.

Ehrt S, Schnappinger D, Rhee KY. Metabolic principles of persistence and pathogenicity in Mycobacterium tuberculosis. Nat Rev Microbiol. 2018;16:496–507.

Eoh H, Wang Z, Layre E, et al. Metabolic anticipation in Mycobacterium tuberculosis. Nat Microbiol. 2017;2:17084.

Collins JM, Walker DI, Jones DP, et al. High-resolution plasma metabolomics analysis to detect Mycobacterium tuberculosis-associated metabolites that distinguish active pulmonary tuberculosis in humans. PLoS ONE. 2018;13:e0205398.

Moopanar K, Mvubu NE. Lineage-specific differences in lipid metabolism and its impact on clinical strains of Mycobacterium tuberculosis. Microb Pathog. 2020;146:104250.

Hansen M, Peltier J, Killy B, et al. Macrophage phosphoproteome analysis reveals MINCLE-dependent and -independent mycobacterial cord factor signaling. Mol Cell Proteomics. 2019;18:669–685.

Downloads

Published

2023-07-08

How to Cite

Al-Asady, I. N., & Ali, J. F. (2023). Review Article: Virulence Factors of Mycobacterium Tuberculosis. Journal for Research in Applied Sciences and Biotechnology, 2(3), 221–237. https://doi.org/10.55544/jrasb.2.3.31

Issue

Section

Articles