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Lookup NU author(s): Professor Waldemar Vollmer
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
Teichoic acid (TA), a crucial cell wall constituent of the pathobiont Streptococcus pneumoniae, is bound to peptidoglycan (wall teichoic acid, WTA) or to membrane glycolipids (lipoteichoic acid, LTA). Both TA polymers share a common precursor synthesis pathway, but differ in the final transfer of the TA chain to either peptidoglycan or a glycolipid. Here, we show that LTA exhibits a different linkage conformation compared to WTA, and identify TacL (previously known as RafX) as a putative lipoteichoic acid ligase required for LTA assembly. Pneumococcal mutants deficient in TacL lack LTA and show attenuated virulence in mouse models of acute pneumonia and systemic infections, although they grow normally in culture. Hence, LTA is important for S. pneumoniae to establish systemic infections, and TacL represents a potential target for antimicrobial drug development.
Author(s): Hess N, Waldow F, Kohler TP, Rohde M, Kraikemeyer B, Hain T, Schwudke D, Vollmer W, Hammerschmidt S, Gisch N
Publication type: Article
Publication status: Published
Journal: Nature Communications
Online publication date: 12/12/2017
Acceptance date: 11/10/2017
Date deposited: 21/12/2017
ISSN (electronic): 2041-1723
Publisher: Springer Nature
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