The two-domain LysX protein of Mycobacterium tuberculosis is required for production of lysinylated phosphatidylglycerol and resistance to cationic antimicrobial peptides.
The well-recognized phospholipids (PLs) of Mycobacterium tuberculosis (Mtb) include several acidic species such as phosphatidylglycerol (PG), cardiolipin, phosphatidylinositol and its mannoside derivatives, in addition to a single basic species, phosphatidylethanolamine. Here we demonstrate that an...
Main Authors: | Erin Maloney, Dorota Stankowska, Jian Zhang, Marek Fol, Qi-Jian Cheng, Shichun Lun, William R Bishai, Malini Rajagopalan, Delphi Chatterjee, Murty V Madiraju |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2009-07-01
|
Series: | PLoS Pathogens |
Online Access: | http://europepmc.org/articles/PMC2713425?pdf=render |
Similar Items
-
Alterations in phospholipid catabolism in Mycobacterium tuberculosis lysX mutant
by: Erin A Maloney, et al.
Published: (2011-02-01) -
Mutation on lysX from Mycobacterium avium hominissuis impacts the host–pathogen interaction and virulence phenotype
by: Greana Kirubakar, et al.
Published: (2020-01-01) -
The bacterial defensin resistance protein MprF consists of separable domains for lipid lysinylation and antimicrobial peptide repulsion.
by: Christoph M Ernst, et al.
Published: (2009-11-01) -
Activation of ROP6 GTPase by Phosphatidylglycerol in Arabidopsis
by: Xiuli Han, et al.
Published: (2018-03-01) -
Estimation of phosphatidylglycerol in fluids containing pulmonary surfactant
by: G Cernansky, et al.
Published: (1980-11-01)