Biochemical characterization of evasion from peptidoglycan recognition by Staphylococcus aureus D-alanylated wall teichoic acid in insect innate immunity.

Abstract:

:We recently reported that D-alanylation of Staphylococcus aureus wall teichoic acid (WTA) mitigates an induction of the Toll-mediated humoral response in Drosophila by interfering with peptidoglycan (PG) recognition by PG recognition protein-SA (PGRP-SA). Here, we investigated the mode of this interference by using an in vitro cell free system from larvae of the coleoptran insect Tenebrio molitor. WTA modification on PG had a potent inhibitory effect on PGRP-SA-mediated Toll proteolytic cascade activation, and the D-alanylation of WTA enhanced its inhibitory effect. Purified D-alanylated WTA released from PG lost its inhibitory action on both Toll cascade activation and PGRP-SA binding to insoluble PG. The inhibition of PGRP-SA binding to PG by D-alanylated WTA took place not only on polymeric PG but also on WTA-attached disaccharide units of monomeric PG. These results suggest that D-alanylation-mediated evasion requires the covalent bonding of D-alanylated WTA to PG, but not net-like cross-linking structure of PG.

journal_name

Dev Comp Immunol

authors

Kurokawa K,Gong JH,Ryu KH,Zheng L,Chae JH,Kim MS,Lee BL

doi

10.1016/j.dci.2011.03.001

subject

Has Abstract

pub_date

2011-08-01 00:00:00

pages

835-9

issue

8

eissn

0145-305X

issn

1879-0089

pii

S0145-305X(11)00059-0

journal_volume

35

pub_type

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