Noemí López-Traba¹, Esther Julián¹ and Gloria G Guerrero²*

¹Departamento de Genética y de Microbiología, Fac de Biociencias, Universidad Autónoma de Barcelona, España, México
²Unidad Académica de Ciencias Biológicas, Universidad Autónoma de Zacatecas, Zacatecas, México

*Corresponding Author: Gloria G Guerrero, Unidad Académica de Ciencias Biológicas, Universidad Autónoma de Zacatecas, Zacatecas, México.

Received: January 21, 2025; Published: February 19, 2025

Abstract

Pathogenic Mycobacteria of the complex Mycobacterium tuberculosis (MTb) are the causative agents of human Tuberculosis. Current reports after COVID-19 pandemic continue to show that pathogenic mycobacteria constitutes a health public problem that is worsen by the increasing multidrug-resistance strains (MDR), and extensive drug resistance (XDR), the co-morbidities and by the lack of long term memory of the actual and official approved vaccine BCG. Approximately 1.7 million deaths annually and morbidity of 10.6 million, remaining with a latent infection, and only a 5% develop active disease. Molecular diagnostic based on real time PCR, Whole genome Sequencing, and single cell multi omics are contributing to the determination of biomarkers of the course and progression of the disease. Furthermore, several studies have highlighted that cell wall lipids of pathogenic mycobacteria play a role as a factor of virulence, and recognized by the innate immune cells, resulting in effective connection with the adaptive immune system, especially those by B and T lymphocytes. In previous work, we isolated Mycobacterium bovis from the bovine’s nostrils in the region of Zacatecas, Mexico. Herein, we are reporting the TLC analysis of mycolic acids and lipids from the mycobacterial cell envelope. From the data, we found subtle differences in the type of mycolic acids and/or lipids profile (polar and apolar) between the M bovis isolates with attenuated Ha and pathogenic H37Rv M. tuberculosis (Hb) and M bovis BCG. T More detailed analysis of the natural subtle variations in composition of the cell envelope of the different geographical mycobacterial isolates is needed and deserve further exploration for potentiate the diagnostic capacity in combination with the serological and molecular techniques.

Keywords: COVID-19; HIV; M. tuberculosis

References

1. World Health Organization. Global Tuberculosis Report. World Health Organization (2023).
2. Global tuberculosis report 2023. Geneva: World Health Organization (2023).
3. Behr MA., et al. “Is Mycobacterium tuberculosis infection life long?” BMJ 367 (2019): 15770.
4. O'Garra A., et al. “The immune response in tuberculosis”. Annual Reviews in Immunology 31 (2013): 475-527.
5. da Costa AC., et al. “Recombinant BCG: innovations on an old vaccine. Scope of BCG strains and strategies to improve long-lasting memory”. Frontiers in Immunology 5 (2014): 152.
6. Zumla A and Maeurer M. “Host-Directed therapies for tackling multi-drug resistant tuberculosis: learning from the Pasteur-Bechamp debates”. Clinical Infectious Diseases 61 (2015): 1432-1438.
7. Udwada ZF., et al. “Totally drug-resistant tuberculosis in India”. Clinical Infectious Diseases 54 (2012): 579-581.
8. Adams O., et al. “Cryo-EM structure and resistance landscape of M. landscape of M. tuberculosis MmpL3: an emergent target”. Structure 29 (2021): 1182-1191 e4.
9. Daneshvar P., et al. “COVID-19 and tuberculosis coinfection: An overview of case reports/case series and meta- analysis of prevalence studies”. Heliyon 9 (2023): e13637.
10. Booysen P., et al. “Immune interaction between SARS-CoV-2 and Mycobacterium tuberculosis”. Frontiers in Immunology 14 (2023): 1254206.
11. Casanova JL and Abel L. “From rare disorders of immunity to common determinants of infection: Following the mechanistic thread”. Cell 185 (2022): 3086-3103.
12. Laval T., et al. “Not too fat to fight: The emerging role of macrophage fatty acid metabolism in immunity to Mycobacterium tuberculosis”. Immunology Review 301 (2021): 84-97.
13. Chandra P., et al. “Immune evasion and provocation by Mycobacterium tuberculosis”. Nature Reviews Microbiology 11 (2022): 750-767.
14. Ortalo-Magne A., et al. “Identification of the surface-exposed lipids on the cell envelopes of Mycobacterium tuberculosis and other mycobacterial species”. Journal of Bacteriology 178 (1996): 456-461.
15. Chiaradia L., et al. “Dissecting the mycobacterial cell envelope and defining the composition of the native mycomembrane”. Scientific Report 7 (2017): 12807-12825.
16. Dulberger ChL., et al. “The mycobacterial cell envelope — a moving target”. Nature Reviews Microbiology 8 (2020): 47-59.
17. Wang S., et al. “Arabinosyltransferase C mediates multiple drugs intrinsic resistance by altering cell envelope permeability in Mycobacterium abscessus”. Microbiology Spectrum 10 (2022): e0276321.
18. Yang X., et al. “Structural basis for the inhibition of mycobacterial MmpL3 by NTD-949 and SPIRO”. Journal of Molecular Biology 432 (2020): 4426-4424.
19. Chalut C. “MmpL transporter-mediated export of cell-wall associated lipids and siderophores in mycobacteria”. Tuberculosis (Edinb). (2016): 32-45.
20. Jankute M., et al. “Assembly of the Mycobacterial Cell Wall”. Annual Review of Microbiology 69 (2015): 405-23.
21. Bhat ZS., et al. “Cell wall: A versatile fountain of drug targets in Mycobacterium tuberculosis”. Biomed Pharmacotherapy 95 (2017): 1520-1534.
22. Llorens-Fons M., et al. “Trehahalose polyphleates, external cell Wall lipids in Mycobacterium abscessus, are associated with the formation of clumps with cording morphology, which have been associated with virulence”. Frontiers in Microbiology 8 (2017): 1402-1417.
23. Singh P., et al. “Cell envelope lipids in the pathophysiology of Mycobacterium tuberculosis”. Future Microbiology 13 (2018): 689-710.
24. Holzheimer M., et al. “Chemical Synthesis of Cell Wall Constituents of Mycobacterium tuberculosis”. Chemical Review 121 (2021): 9554-9643.
25. Van Schie L., et al. “Exploration of Synergistic Action of Cell Wall-Degrading Enzymes against Mycobacterium tuberculosis”. Antimicrobe Agents Chemotherapy 65 (2021): e0065921.
26. Christensen H., et al. “Lipid domains of mycobacteria studied with fluorescent molecular probes”. Molecular Microbiology 31 (1991): 1561-1572.
27. Burbaud S., et al. “Trehalose polyphleates are produced by a glycolipid biosynthetic pathway conserved across phylogenetically distant mycobacteria”. Cell Chemical Biology 23 (2016): 278-289.
28. Daffé M., et al. “Genetics of capsular polysaccharides and cell envelope (Glyco) lipids”. Microbiology Spectrum 2 (2021): 14.
29. Daffé M and Marrakchi H. “Unraveling the structure of the mycobacterial nvelope”. Microbiology Spectrum 7 (2019): 7-14.
30. Schami A., et al. “Drug-resistant strains of Mycobacterium tuberculosis: cell envelope profiles and interactions with the host”. Frontiers in Microbiology 13 (2020): 1274175.
31. Lu Y., et al. “Deletion of the Mycobacterium tuberculosis cyp138 gene leads to changes in membrane-related lipid composition and antibiotic susceptibility”. Frontiers in Microbiology 15 (2024): 1301204.
32. Fisher JF and Mobashery S. “Constructing and deconstructing the bacterial cell wall”. Protein Science 29 (2020): 629-646.
33. Witwinowski J., et al. “An ancient divide in outer membrane tethering systems in bacteria suggests a mechanism for the diderm-to-monoderm transition”. Nature Microbiology 7 (2022): 411-422.
34. Léonard RR., et al. “Was the Last Bacterial Common Ancestor a Monoderm after All?” Genes (Basel) 13 (2022): 376.
35. Berry PRM., et al. “An interferon-inducible neutrophil-driven blood transcriptional signature in human tuberculosis”. Letter to Nature 466 (2010): 973-97.
36. Mayorquín LAG., et al. “A study of the global in vivo gene expression profile in cattle from Mexico”. Current Analytical Biotechnology (2018).
37. Guerrero GG. “Omics technologies. A hope for translational research in bovine tuberculosis”. Journal of Infectious Diseases and Therapy 7 (2019): 2.
38. Sánchez-Garza JJ., et al. “Direct DNA Modified CTAB preparation from nasal exudate in live M. bovis infected cattle in Mexico, provide with a valuable assay extrapolated to Human TB diagnostic test”. Journal of Tropical Diseases and Public Health 7 (2019): 325-343.
39. Favela-Hernández JM., et al. “Evaluation of Mycobacterium bovis isolated from cattle in Mexico for serum reactivity and antigen production kinetics”. Journal of Medical Microbiology and Diagnosis (2019).
40. Guerrero GG., et al. “Clinical, and Diagnostic characteristics of an unsuspected course of urinary Tuberculosis: A Brief Report”. ASM 5 (2022): 1-8.
41. Pirson Ch., et al. “Differential effects of Mycobacterium bovis-derived polar and apolar lipid fractions on bovine innate immune cells”. Veterinary Research 43 (2016): 54-65.
42. Nelson DR. “Cytochrome P450 diversity in the tree of life”. Biochimica et Biophysica Acta - Proteins and Proteomics 2018 (2018): 141-154.
43. Pankjurst LJ., et al. “Rapid comprenhensive and affordable mycobacteria diagnosis with whole-genome sequencing: a prospective study”. Lancet Respiratory Medicine 4 (2016): 49-58.
44. Perez-Riverol Y., et al. “The PRIDE database resources in 2022: a hub for mass spectrometry-based proteomics evidences”. Nucleic Acids Research 50 (2022): D543-D552.
45. Guerrero GG., et al. “Boosting with mycobacterial heparin-binding hemagglutinin enhanced protection of Mycobacterium bovis BCG vaccinated newborns mice against M. tuberculosis”. Vaccine 28 (2010): 4340-4347.
46. Minnikin DE., et al. “Thin-layer chromatography of methanolysates of mycolic acidcontaining bacteria”. Journal of Chromatography 188 (1980): 221-233.
47. Gorocica P., et al. “Structural components of the envelope of Mycobacterium tuberculosis that intervene in the pathogenesis of tuberculosis”. INER 18 (2005): 1-15
48. Onwueme K C., et al. “The dimycocerosate ester polyketide virulence factors of mycobacteria”. Progress Lipid Research 44 (2005): 259-302.
49. Msomi NN., et al. “In Silico Analysis of P450s and their role in secondary metabolism in the bacterial class gammaproteobacteria”. Molecules 26 (2021): 1538.
50. Plocinski P., et al. “Mycobacterium tuberculosis CwsA interacts with CrgA and Wag31, and the CrgACwsA complex is involved in peptidoglycan synthesis and cell shape determination”. Journal of Bacteriology 194 (2012): 6398-6409.
51. Maurya RK., et al. “Triacylglycerols: Fuelling the Hibernating Mycobacterium tuberculosis”. Frontiers in Cellular and Infection Microbiology 8 (2018): 450.
52. Skerry C., et al. “TLR2 modulating lipoproteins of the mycobacterium tuberculosis complex enhance the HIV infectivity of CD4+T cells”. PLoS ONE 11 (2016): e0147192.
53. Batt SM., et al. “Antibiotics and resistance: the two- sided coin of the mycobacterial cell wall”. Cell Surface 6 (2020): 100044.
54. Degiacomi G., et al. “Promiscuous targets for antitubercular drug discovery ; the paradigm of DprE1 and MmpL3”. Applied Science 10 (2020): 823.
55. Shao M., et al. “MmpL3 inhibitors as antituberculous drugs”. European Journal of Medicinal Chemistry 200 (2020): 112390.
56. Ortega Ugalde S., et al. “Function, essentiality, and expression of cytochrome P450 enzymes and their cognate redox partners in Mycobacterium tuberculosis: are they drug targets?” Applied Microbiology and Biotechnology 103 (2019): 3597-3614.

Citation

Citation: Gloria G Guerrero.,et al. “Mycolic Acids and Lipids TLC Analysis of the Cell Envelope of Mycobacterium bovis Strains Isolated from Zacatecas, México".Acta Scientific Microbiology 8.3 (2025): 27-36.

Copyright

Copyright: © 2025 Gloria G Guerrero.,et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.