N-terminal GST fusion protein with C-terminal 6xHis tagged antigen TB22.2(Rv3036c) (M. Tuberculosis/H37Rv)(a.a.1-231) (Genbank Accession No. NP_217552). Conserved secreted protein, with putative N-terminal signal peptide, highly similar to secreted immunogenic protein MPT64/MPB64|P19996|Rv1980c| MTCY39.39 from Mycobacterium tuberculosis and Mycobacterium bovis (228 aa), FASTA scores: opt: 681, E(): 2.5e-35, (45.8% identity in 227 aa overlap). Predicted to be an outer membrane protein.
Nature
Recombinant
Tag/Conjugate
His, GST
Alternative Names
M. Tuberculosis 63 kDa protein; Mycobacterium tuberculosis 98 kDa protein; Mycobacterium tuberculosis; M. tuberculosis; MTB; TB antigen
Purity
>95% , based on SDS PAGE
Format
Each vial contains 100 μg of lyophilized protein in PBS with 8M Urea.
Concentration
Batch dependent - please inquire should you have specific requirements.
Preservative
None
Reconstitution
Reconstitute the protein with 100 μl of Millipore water.
Antigen Description
Mycobacterium tuberculosis is an obligate pathogenic bacterial species in the family Mycobacteriaceae and the causative agent of tuberculosis First discovered in 1897 by Robert Koch, M. tuberculosis has an unusual, waxy coating on its cell surface (primar
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Background
Tuberculosis is a chronic bacterial zoonotic infectious disease that has a very high rate of morbidity and mortality. Although many tuberculosis controls have been in place by international organisations and countries around the world, it is still a leading public health concern on a global scale because of its subtle early symptoms, duration of incubation, high infection rate and unreliable prevention and treatment. Tuberculosis is caused by the main cause, Mycobacterium tuberculosis (Mtb). Most people with LTBI suffer from latent tuberculosis infection, where the virus can slip past the immune system and live passively in the lesions, balancing host and bacteria by producing granulomas. As host immunity is lowered, Mtb can reactivate and about 5-15% of LTBI cases develop active TB.
Mtb spreads mostly by respiratory route, with MTB aerosol inhalation being the most common source of infection. In the mouse model of infection, Mtb gets into the alveoli through the airways, and attacks AMs first and foremost in the first two weeks of infection. Two weeks later, infected AMs migrate from the alveoli to the lung interstitium (a response that requires the presence of host IL-1β and the ESX-1 type VII secretion system). Mtb attacks a variety of cell types once it has arrived in the lung interstitium, such as monocyte macrophages, tissue macrophages, polymorphonuclear neutrophils and dendritic cells.
Figure 1. Evasion of T cell recognition versus T cell activation by Mtb-infected antigen-presenting cells (Source: Boom WH, et al. 2021)
Through long-term co-evolution with its host, Mtb has developed complex immune evasion mechanisms during infection. It encodes virulence proteins and lipid effector molecules that inhibit host immune defense functions such as phagosome maturation, apoptosis, oxidative stress, and autophagy regulation. They also restrict adaptive immune responses that result from Mtb infection. Mtb's cell wall molecule lipoarabinomannan (LAM) also has a number of bioactivities that can control host immune responses. LAM escapes from the bacteria in chronic tuberculosis patients, and plays immunomodulatory roles that prevent Mtb from maturing phagosomes. Components of the Mtb cell wall and secreted proteins can evade host phagocytosis by inhibiting phagosome maturation, acidification, and fusion with lysosomes, facilitating survival and dissemination within host cells. Additionally, Mtb regulates host autophagy through various effector proteins to promote its own survival and spread.
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References
VapBC22 toxin-antitoxin system from Mycobacterium tuberculosis is required for pathogenesis and modulation of host immune response
Virulence-associated protein B and C toxin-antitoxin (TA) systems are widespread in prokaryotes, but their precise role in physiology is poorly understood. We have functionally characterized the VapBC22 TA system from Mycobacterium tuberculosis. Transcriptome analysis revealed that overexpression of VapC22 toxin in M. tuberculosis results in reduced levels of metabolic enzymes and increased levels of ribosomal proteins. Proteomics studies showed reduced expression of virulence-associated proteins and increased levels of cognate antitoxin, VapB22 in the Delta vapC22 mutant strain. Furthermore, both the Delta vapC22 mutant and VapB22 overexpression strains of M. tuberculosis were susceptible to killing upon exposure to oxidative stress and showed attenuated growth in guinea pigs and mice. Host transcriptome analysis suggests upregulation of the transcripts involved in innate immune responses and tissue remodeling in mice infected with the Delta vapC22 mutant strain. Together, we demonstrate that the VapBC22 TA system belongs to a key regulatory network and is essential for M. tuberculosis pathogenesis.
A proposed carbon-utilization and virulence protein A, CuvA (Rv1422), from Mycobacterium tuberculosis H37Rv: crystallization, X-ray diffraction analysis and ligand binding
Mycobacterium tuberculosis possesses the ability to undergo physiological adaptations in order to persist during the prolonged course of infection despite the active immune response of the host and in order to overcome multiple environmental changes. Previous studies have proposed that M. tuberculosis CuvA (Rv1422; MtCuvA) might play a critical role in the adaptation of the bacterium to environmental changes, such as nutrient utilization and alteration of the growth rate. However, the detailed function of MtCuvA still remains unclear owing to a lack of structural information. To better understand its role in host adaptation, MtCuvA was purified to homogeneity and was crystallized for the first time using the hanging-drop vapor-diffusion method. The crystal of MtCuvA diffracted to a resolution of 2.1 angstrom and belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 47.27, b = 170.93, c = 178.10 angstrom. The calculated Matthews coefficient (V-M) was 2.4 angstrom(3) Da(-1), with a solvent content of 48.02%, and thus four molecules appeared to be present in the asymmetric unit. Moreover, it is reported that MtCuvA can bind to the cell-wall precursor components uridine diphosphate (UDP)-glucose and UDP-N-acetyl-glucosamine.
COA
Publication 
Figure 1. Evasion of T cell recognition versus T cell activation by Mtb-infected antigen-presenting cells
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