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- Title
LygA retention on the surface of Listeria monocytogenes via its interaction with wall teichoic acid modulates bacterial homeostasis and virulence.
- Authors
Yao, Hao; Li, Guo; Xiong, Xianglian; Jin, Fanxin; Li, Sirui; Xie, Xinyu; Zhong, Dan; Zhang, Renling; Meng, Fanzeng; Yin, Yuelan; Jiao, Xin'an
- Abstract
Wall teichoic acid (WTA) is the abundant cell wall-associated glycopolymer in Gram-positive bacteria, playing crucial roles in surface proteins retention, bacterial homeostasis, and virulence. Hypervirulent serovar (SV) 4h Listeria monocytogenes is a newly designated serotype with only galactosylated (Gal) type II WTA. Although the surface association of some proteins relies on the WTA glycosylation, the nature and function of the noncovalent interactions between cell wall-associated proteins and WTA are less known. In this study, we found Gal-WTA plays a key role in modulating the novel glycine-tryptophan (GW) domain-containing autolysin protein LygA through direct interactions. An SV 4h strain deficient in WTA galactosylation (XYSNΔgalT) showed a dramatic reduction of LygA on the cell surface, significantly decreasing the autolytic activity, impairing the bacterial colonization in colon and brain. Notably, we demonstrated LygA binds to Gal-WTA with high affinity through the GW domain and that the extent of binding increases with the number of GW domains. Moreover, we confirmed the direct Gal-dependent binding of the GW protein Auto from the type I WTA strain, which has no interaction with l-rhamnosylated WTA, indicating that the complexity of both WTA and GW proteins can affect the coordination patterns. Altogether, our findings suggest that both the glycosylation patterns of WTA and a fixed numbers of GW domains are closely associated with the retention of LygA on the cell surface, which facilitates L. monocytogenes infection by promoting bacteria colonization in intestine and brain. Author summary: Wall teichoic acid (WTA) of Listeria monocytogenes is involved in several key physiological functions through direct interaction with canonical virulence factors on the bacterial surface. However, how WTA modifies the retention of Listeria surface proteins and contributes to virulence remains unclear. Here, we found Gal-WTA mediates the anchoring of a novel autolysin LygA in SV 4h L. monocytogenes through interaction with the C-terminal GW domains. Both the WTA glycosylation and the composition of GW domains are necessary in the surface association of GW proteins. LygA facilitates bacteria to break through the intestinal barrier and blood-brain barrier. Collectively, our findings reveal that the specific interactions between WTA and GW-containing protein LygA contribute to L. monocytogenes homeostasis and pathogenesis.
- Subjects
HOMEOSTASIS; LISTERIA monocytogenes; BACTERIAL colonies; BACTERIAL cell surfaces; BLOOD-brain barrier; GRAM-positive bacteria; CARRIER proteins
- Publication
PLoS Pathogens, 2023, Vol 18, Issue 6, p1
- ISSN
1553-7366
- Publication type
Article
- DOI
10.1371/journal.ppat.1011482