Open AccessAn ABC transporter Wzm–Wzt catalyzes translocation of lipid-linked galactan across the plasma membrane in mycobacteria
Author(s) -
Karin Savková,
Stanislav Huszár,
Péter Baráth,
Zuzana Pakanová,
Stanislav Kozmon,
Marie Vancová,
Martina Tesařová,
Jaroslav Blaško,
Michal Kaliňák,
Vinayak Singh,
Jana Korduláková,
Katarı́na Mikus̃ová
Publication year - 2021
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2023663118
Subject(s) - atp binding cassette transporter , periplasmic space , peptidoglycan , galactan , biochemistry , biogenesis , cell wall , biology , teichoic acid , mycobacterium , arabinogalactan , mycobacterium smegmatis , lipid ii , transporter , transmembrane protein , microbiology and biotechnology , bacteria , mycobacterium tuberculosis , gene , genetics , escherichia coli , medicine , tuberculosis , receptor , pathology
Significance The cell envelope ofMycobacterium tuberculosis serves as a primary protective barrier of the pathogen, which claims more than a million lives each year. Its basis, the unique mycobacterial cell wall core, is composed of covalently linked peptidoglycan, branched heteropolysaccharide arabinogalactan, and mycolic acids. Construction of this complex structure located on the bacterial surface requires an array of enzymes acting on both sides of the plasma membrane, as well as translocation of metabolic intermediates from the cytoplasm to the periplasmic space. In this work, we characterized an ATP-binding cassette (ABC) transporter involved in the export of galactan polymer produced by cytoplasmic enzymes across the plasma membrane, providing an important insight into the biogenesis of a structure critical for pathogen survival.