Cryo-electron microscopy structures show how the clinically used antimicrobial fidaxomicin binds and inhibits Mycobacterium tuberculosis RNA polymerase by acting like a doorstop to jam the enzyme in an open conformation via the general transcription factor RbpA.
Metabolomics and stable isotope labelling studies of virulent Mycobacterium tuberculosis reveal a de-centralised metabolic network able to utilise various amino acids as nitrogen sources to a better extent than ammonium.
Mycobacterium tuberculosis penetrates the airway mucosa through M cells via the mycobacterial virulence factor EsxA and the host M cell surface receptor scavenger receptor B1.
Time-lapse live cell imaging of single Mycobacterium tuberculosis bacilli growing into small colonies enables their rapid phenotypic characterization including anti-microbial resistance and heteroresistance in clinical isolates.
Time-lapse imaging and the modular recreation of host physiology reveal that alveolar epithelial cells, potential permissive infection sites for Mycobacterium tuberculosis, can restrict early bacterial growth via surfactant secretion.
Intrinsic tolerance of Mycobacterium tuberculosis toward the world's most successful antibacterials, β-lactams, is dependent on cytoplasmic redox potential and an intracellular redox-sensor WhiB4.
Fully assembled DNA methylomes from phylogeographically diverse clinical Mycobacterium tuberculosis complex isolates reveals 'intercellular mosaic methylation' as a source of epigenetic diversity.
A humanized transgenic mouse model reveals that CD1b-restricted, mycolic acid-specific T cells play a protective role during Mycobacterium tuberculosis infection.
SatS of Mycobacterium tuberculosis is a new protein export chaperone with a role in exporting proteins by the specialized SecA2 pathway and a role in intracellular growth in macrophages.
