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Since 2018, all members of this species complex are considered synonyms of M. tuberculosis as far as bacterial nomenclature is concerned. The IJSEM article reports that M. africanum, M. bovis, M. caprae, M. pinnipedii are 99.21–99.92% identical to M. tuberculosis on the whole-genome level, failing the criteria to be considered independent ...
The nature of the host-pathogen interaction between humans and M. tuberculosis is considered to have a genetic component. A group of rare disorders called Mendelian Susceptibility to Mycobacterial Diseases (MSMD) was observed in a subset of individuals with a genetic defect that results in increased susceptibility to Mycobacterial infection.
The ability to construct M. tuberculosis mutants and test individual gene products for specific functions has significantly advanced the understanding of its pathogenesis and virulence factors. Many secreted and exported proteins are known to be important in pathogenesis. [30]
M. tuberculosis is able to reproduce inside the macrophage and will eventually kill the immune cell. The primary site of infection in the lungs, known as the Ghon focus, is generally located in either the upper part of the lower lobe, or the lower part of the upper lobe. [13] Tuberculosis of the lungs may also occur via infection from the blood ...
Lipoarabinomannan, also called LAM, is a glycolipid, and a virulence factor associated with Mycobacterium tuberculosis, the bacteria responsible for tuberculosis. Its primary function is to inactivate macrophages and scavenge oxidative radicals. The inactivation of macrophages allows for the dissemination of mycobacteria to other parts of the body.
H37Rv has continued to be the strain of tuberculosis most used in laboratories, and was the first to have its complete genome published in 1998. [5] It is unclear how much H37Rv may have evolved in more than 100 years under artificial conditions in laboratories from strains in the wild, but its genome is similar to a strain isolated from a 19th ...
Most conserved is the primary sequence of the amino acyl acceptor stem. This portion of the molecule has an invariable A residue in the discriminator position and a G-U pair at position 3 (except in S eculamonas ecuadoriensis , which has a G-C pair); this position is the recognition site for alanyl tRNA synthase.
Cord factor, or trehalose dimycolate (TDM), is a glycolipid molecule found in the cell wall of Mycobacterium tuberculosis and similar species. It is the primary lipid found on the exterior of M. tuberculosis cells. [1] Cord factor influences the arrangement of M. tuberculosis cells into long and slender formations, giving its name. [2]