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Browsing by Subject Mycobacterium tuberculosis

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Showing results 1 to 7 of 7
  • OER000002394.pdf.jpg
  • Ebooks (Sách điện tử)

  • Chemical inhibition of histidine biosynthesis curtails M. tuberculosis infection

    • Authors : Tiwari, Satish (2023)

  • To overcome the drug resistance crisis and shorten the current duration of human tuberculosis (TB) therapy, new anti-TB molecules is required. In an earlier study, we have shown that Mycobacterium tuberculosis (Mtb), the causative agent of TB, with a fractured de novo histidine biosynthesis fails to mount TB infection in mouse model, emboldening that disrupting the function of this pathway may constitute a novel strategy to curtailing TB infection.&...
  • OER000004010.pdf.jpg
  • Journal article

  • Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria

    • Authors : Tan, Yong Zi; Zhang, Lei; Rodrigues, José (-)

  • Mycobacterium tuberculosis causes tuberculosis, a disease that kills over one million people each year. Its cell envelope is a common antibiotic target and has a unique structure due, in part, to two lipidated polysaccharides – arabinogalactan and lipoarabinomannan. Arabinofuranosyltransferase D (AftD) is an essential enzyme involved in assembling these glycolipids. We present the 2.9 Å resolution structure of M. abscessus AftD determined by single particle cryo-e...
  • OER000000778.pdf.jpg
  • Journal article

  • Membrane Insertion of Mycobacterium tuberculosis EsxA in Cultured Lung Epithelial Cells

    • Authors : Zhang, Qi; Aguilera, Javier; Reyes, Salvador Vazquez (2020)

  • EsxA has long been recognized as an important virulence factor of Mycobacterium tuberculosis (Mtb) that plays an essential role in Mtb virulence. However, current data regarding to its role in Mtb virulence are controversial. Here, we have obtained evidence showing that the cytolytic activity of EsxA at neutral pH is due to contamination of ASB-14, a detergent used in EsxA preparation. Moreover, it is for the first time we have found ...
  • OER000000744.pdf.jpg
  • Journal article

  • Membrane Insertion of Mycobacterium tuberculosis EsxA in Cultured Lung Epithelial Cells

    • Authors : Zhang, Qi; Aguilera, Javier (2020)

  • EsxA has long been recognized as an important virulence factor of Mycobacterium tuberculosis (Mtb) that plays an essential role in Mtb virulence. However, current data regarding to its role in Mtb virulence are controversial. Here, we have obtained evidence showing that the cytolytic activity of EsxA at neutral pH is due to contamination of ASB-14, a detergent used in EsxA preparation. Moreover, it is for the first time we have found ...
  • OER000001599.pdf.jpg
  • Journal article

  • Nα-acetylation of EsxA is required for mycobacterial cytosolic translocation and virulence

    • Authors : Aguilera, Javier; Karki, Chitra B; Li, Lin (2020)

  • Mycobacterium tuberculosis virulence factors, EsxA and EsxB, are secreted as a heterodimer (EsxA:B) and play an essential role in mycobacterial phagosomal escape and cytosolic translocation. Current studies support a model that EsxA must dissociate from its chaperon EsxB at low pH in order for EsxA to interact with host membranes. However, the mechanism of the heterodimer separation is not clear. In the present study, we have obtained evidence that&...
  • OER000004030.pdf.jpg
  • Journal article

  • Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site

    • Authors : Chaton, Catherine T; Rodriguez, Emily S; Reed, Robert W (2019)

  • Mycobacterium tuberculosis is the cause of the world’s most deadly infectious disease. Efforts are underway to target the methionine biosynthesis pathway, as it is not part of the host metabolism. The homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of this pathway. In order to facilitate structure-based drug design, we determined the high-resolution crystal structures of three MetX proteins, including M. tuberculosis&...