l‐Rhamnosylation of wall teichoic acids promotes efficient surface association of Listeria monocytogenes virulence factors InlB and Ami through interaction with GW domains

Summary Wall teichoic acids (WTAs) are important surface glycopolymers involved in various physiological processes occurring in the Gram‐positive cell envelope. We previously showed that the decoration of Listeria monocytogenes (Lm) WTAs with l‐rhamnose conferred resistance against antimicrobial pep...

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Bibliographic Details
Published in:Environmental microbiology 2018-11, Vol.20 (11), p.3941-3951
Main Authors: Carvalho, Filipe, Sousa, Sandra, Cabanes, Didier
Format: Article
Language:English
Subjects:
Acids
Anchoring
Antimicrobial peptides
Autolysis
Cell surface
Domain walls
Domains
Glycopolymers
Internalin
Listeria
Listeria monocytogenes
Pathogenesis
Pathogens
Peptides
Physiology
Proteins
Rhamnose
Teichoic acids
Virulence
Virulence factors
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Summary:Summary Wall teichoic acids (WTAs) are important surface glycopolymers involved in various physiological processes occurring in the Gram‐positive cell envelope. We previously showed that the decoration of Listeria monocytogenes (Lm) WTAs with l‐rhamnose conferred resistance against antimicrobial peptides. Here, we show that WTA l‐rhamnosylation also contributes to physiological levels of autolysis in Lm through a mechanism that requires efficient association of Ami, a virulence‐promoting autolysin belonging to the GW protein family, to the bacterial cell surface. Importantly, WTA l‐rhamnosylation also controls the surface association of another GW protein, the invasin internalin B (InlB), that promotes Lm invasion of host cells. Whereas WTA N‐acetylglucosaminylation is not a prerequisite for GW protein surface association, lipoteichoic acids appear to also play a role in the surface anchoring of InlB. Strikingly, while the GW domains of Ami, InlB and Auto (another autolysin contributing to cell invasion and virulence) are sufficient to mediate surface association, this is not the case for the GW domains of the remaining six uncharacterized Lm GW proteins. Overall, we reveal WTA l‐rhamnosylation as a bacterial surface modification mechanism that contributes to Lm physiology and pathogenesis by controlling the surface association of GW proteins involved in autolysis and infection.
ISSN:1462-2912
1462-2920
DOI:10.1111/1462-2920.14351