ReviewAdvances in experimental medicine and biology2026
Contribution of Proteins to Membrane and Cell Wall Structures in Mycobacterium tuberculosis.
Review in Advances in experimental medicine and biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cell wall of Mycobacterium tuberculosis (Mtb) is an exceptionally complex, multilayered structure that is fundamental to the bacterium's survival, pathogenicity, and resistance to both host immune defenses and antibiotics. This cell envelope consists of several distinct components: a surface capsule, an outer membrane, and a peptidoglycan layer that is covalently attached to arabinogalactan. The arabinogalactan is further esterified with mycolic acids, forming the characteristic mycolyl-arabinogalactan-peptidoglycan (mAGP) complex, which is anchored to the underlying plasma membrane. The assembly and maintenance of this intricate architecture depend on a suite of specialized proteins that regulate lipid transport, enzymatic modifications, and structural integrity. Among these, the Antigen 85 Complex (Ag85) is particularly important, as it catalyzes the transfer of mycolic acids to arabinogalactan, facilitating the synthesis of trehalose dimycolate (TDM), a major virulence factor. The inner membrane transporter MmpL3 is critical for translocating trehalose monomycolate (TMM) across the plasma membrane, a prerequisite for TDM synthesis and cell wall stability. Additionally, the MmpS4/MmpL4 and MmpS5/MmpL5 complexes mediate the secretion of siderophores, which are essential for iron acquisition under nutrient-limited conditions and thereby support bacterial growth. Enzymes such as cyclopropane synthases (e.g., CmaA2) and methyltransferases (e.g., MmaA3) chemically modify mycolic acids, enhancing the pathogen's ability to evade host immune responses. Outer membrane proteins (OMPs), including Rv1698 and Rv1973, contribute to the structural integrity and selective permeability of the cell envelope, although their precise biological functions are still being elucidated. Collectively, these membrane- and cell wall-associated proteins orchestrate the biosynthesis, modification, and transport of essential cell wall components, underpinning the unique composition of the Mtb cell envelope that confers intrinsic resistance to antibiotics and host defenses. A comprehensive understanding of these proteins is crucial for the development of novel antituberculosis therapeutics and vaccines, as they represent promising targets for disrupting the protective barrier of Mtb.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.