Maria Rosalia Pasca

TL;DR: The synthesis and characterization of 1,3-benzothiazin-4-ones (BTZs), a new class of antimycobacterial agents that kill Mycobacterium tuberculosis in vitro, ex vivo, and in mouse models of TB are described.

TL;DR: Electrophoretic mobility shift experiments demonstrated that Zur binds to this palindrome in a zinc-dependent manner, suggesting its direct regulation of these genes.

TL;DR: The screening of genomic libraries and whole-genome sequencing found that all the characterized mutants showed mutations in the mmpL3 gene, allowing us to conclude that resistance to BM212 maps to the MMPL3 protein, a member of the MmpL (mycobacterial membrane protein, large) family.

TL;DR: The crystal structure of the mycobacterial DprE1 reveals how the TB drug benzothiazinone BTZ043 blocks this microbial enzyme target, and structural and kinetic analysis provides both insight into a critical epimerization reaction and a platform for structure-based design of improved inhibitors.

TL;DR: The Mycobacterium tuberculosis Rv2686c-Rv2687c-rv2688c operon, encoding an ABC transporter, conferred resistance to ciprofloxacin and, to a lesser extent, norfloxACin, moxifloxacIn, and sparfloxAcin to Myc Cobacterium smegmatis.