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Showing 1–12 of 12 results
Advanced filters: Author: Michael Niederweis Clear advanced filters

  • Tuberculosis necrotizing toxin (TNT) is secreted by Mycobacterium tuberculosis to kill host cells. Here, Tak, Dokland and Niederweis show that proteins EsxE and EsxF form membrane-spanning hetero-oligomeric pores that are important for TNT secretion.

    • Uday Tak
    • Terje Dokland
    • Michael Niederweis
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-17

  • Mycobacterium tuberculosis uses five ESX systems to secrete multiple effector proteins that are essential for the pathogen’s growth and virulence. Here, Nair et al. identify a protein complex that is required for outer-membrane localization and for secretion of all ESX-dependent proteins into the cytosol of infected macrophages.

    • Rashmi Ravindran Nair
    • Virginia Meikle
    • Michael Niederweis
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-20

  • Mycobacteria produce small molecules (mycobactins) to acquire the essential nutrient iron. Here, Earp et al determine the cryo-EM structures of the mycobactin exporter MmpL4, which also effluxes the TB drug bedaquiline.

    • Jennifer C. Earp
    • Alisa A. Garaeva
    • Markus A. Seeger
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-13

  • The cryo-EM structure of Mycobacterium smegmatis arabinosyltransferase B EmbB involved in mycobacterial cell wall biosynthesis provides insights into the substrate binding and reaction mechanism. Mapping of the ethambutol resistance associated mutations onto the structure suggests the location of the drug binding site.

    • Yong Zi Tan
    • José Rodrigues
    • Filippo Mancia
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • Protein nanopores are being developed as sensors that could perform rapid, electronic sequencing of long single molecules of DNA. Manrao et al. report the first demonstration of single nucleotide–resolution current traces from a nanopore, and show that these data can be mapped to known DNA sequences.

    • Elizabeth A Manrao
    • Ian M Derrington
    • Jens H Gundlach
    Research
    Nature Biotechnology
    Volume: 30, P: 349-353

  • Lokareddy et al. determine the complete structure of DEV, a lytic virus that infects Pseudomonas aeruginosa, using a combination of cryo-electron microscopy, biochemical methods, and genetic knockouts. They propose that the virion-associated RNA polymerase may be part of a genome ejection motor.

    • Ravi K. Lokareddy
    • Chun-Feng David Hou
    • Gino Cingolani
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-20

  • The tuberculosis necrotizing toxin (TNT) is the major cytotoxicity factor of M. tuberculosis (Mtb). Mtb possesses five type VII secretion systems (ESX). Pajuelo et al. show that the ESX-4 system is required for TNT secretion and that ESX-2 and ESX-4 systems work in concert with ESX-1 to permeabilize the phagosomal membrane and enable trafficking of TNT into the cytoplasm of macrophages infected with Mtb.

    • David Pajuelo
    • Uday Tak
    • Michael Niederweis
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-13

  • Iron is essential for growth of Mycobacterium tuberculosis, but most of the iron in the human body is stored in heme within hemoglobin. Here, Mitra et al. identify two heme uptake mechanisms in M. tuberculosis, one dependent on the inner-membrane Dpp importer and the other dependent on host albumin.

    • Avishek Mitra
    • Ying-Hui Ko
    • Michael Niederweis
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-14

  • Inflammasome activation is a response to bacterial infection but can cause damage and spread infection. Here, the authors use live single-cell imaging to show two mechanisms by which M. tuberculosis causes damage to human macrophage cell plasma membranes, resulting in activation of the NLRP3 inflammasome, pyroptosis and release of infectious particles.

    • Kai S. Beckwith
    • Marianne S. Beckwith
    • Trude H. Flo
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-18

  • The Mycobacterium tuberculosis necrotizing toxin (TNT) is shown to cause toxicity by hydrolyzing NAD+ in the host cell. The crystal structure of TNT bound to its immunity factor reveals a new NAD+ glycohydrolase fold.

    • Jim Sun
    • Axel Siroy
    • Michael Niederweis
    Research
    Nature Structural & Molecular Biology
    Volume: 22, P: 672-678