Enzymatic Synthesis and Immunochemistry of α- and β-N-Acetylglucosaminylribitol Linkages in Teichoic Acids from Several Strains of Staphylococcus aureus

Nathenson, Stanley G.; Ishimoto, Nobutoshi; Anderson, John S.; Strominger, Jack L.

doi:10.1016/s0021-9258(18)96887-0

Cited by 45 publications

(1 citation statement)

References 34 publications

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“…The ternary complex structure of TarM(Se) G117R bound to UDP and 4RboP-glucose provides, for the first time, clear evidence that a glycosyltransferase glycosylates WTA in a processive manner. This is in line with the observations that WTAs extracted from bacterial cells are heavily modified with sugars ( 23 , 47 ), and the WTA chains contain sugars with exclusive α or β configuration ( 48 , 49 ). The enzyme activity and theoretical potential for the processive ability of the TarM(Sa) homotrimer and TarM(Sa) G11R monomer are similar, suggesting that the trimerization does not affect the substrate binding, catalysis, and processivity ( 33 ).…”

Section: Discussionsupporting

confidence: 91%

Invasive Staphylococcus epidermidis uses a unique processive wall teichoic acid glycosyltransferase to evade immune recognition

Guo,

Du,

Krusche

et al. 2023

Sci. Adv.

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Staphylococcus epidermidis expresses glycerol phosphate wall teichoic acid (WTA), but some health care–associated methicillin-resistant S. epidermidis (HA-MRSE) clones produce a second, ribitol phosphate (RboP) WTA, resembling that of the aggressive pathogen Staphylococcus aureus . RboP-WTA promotes HA-MRSE persistence and virulence in bloodstream infections. We report here that the TarM enzyme of HA-MRSE [TarM(Se)] glycosylates RboP-WTA with glucose, instead of N -acetylglucosamine (GlcNAc) by TarM(Sa) in S. aureus . Replacement of GlcNAc with glucose in RboP-WTA impairs HA-MRSE detection by human immunoglobulin G, which may contribute to the immune-evasion capacities of many invasive S. epidermidis . Crystal structures of complexes with uridine diphosphate glucose (UDP-glucose), and with UDP and glycosylated poly(RboP), reveal the binding mode and glycosylation mechanism of this enzyme and explain why TarM(Se) and TarM(Sa) link different sugars to poly(RboP). These structural data provide evidence that TarM(Se) is a processive WTA glycosyltransferase. Our study will support the targeted inhibition of TarM enzymes, and the development of RboP-WTA targeting vaccines and phage therapies.

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