Title: Structural basis of bacterial defense against g-type lysozyme-based innate immunity
Authors: Leysen, Seppe ×
Vanderkelen, Lise
Weeks, Stephen
Michiels, Chris
Strelkov, Sergei #
Issue Date: Mar-2013
Publisher: Birkhäuser Verlag
Series Title: Cellular and Molecular Life Sciences vol:70 issue:6 pages:1113-1122
Abstract: Gram-negative bacteria can produce specific proteinaceous inhibitors to defend themselves against the lytic action of host lysozymes. So far, four different lysozyme inhibitor families have been identified. Here, we report the crystal structure of the Escherichia coli periplasmic lysozyme inhibitor of g-type lysozyme (PliG-Ec) in complex with Atlantic salmon g-type lysozyme (SalG) at a resolution of 0.95 Å, which is exceptionally high for a complex of two proteins. The structure reveals for the first time the mechanism of g-type lysozyme inhibition by the PliG family. The latter contains two specific conserved regions that are essential for its inhibitory activity. The inhibitory complex formation is based on a double 'key-lock' mechanism. The first key-lock element is formed by the insertion of two conserved PliG regions into the active site of the lysozyme. The second element is defined by a distinct pocket of PliG accommodating a lysozyme loop. Computational analysis indicates that this pocket represents a suitable site for small molecule binding, which opens an avenue for the development of novel antibacterial agents that suppress the inhibitory activity of PliG.
ISSN: 1420-682X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Centre for Food and Microbial Technology
× corresponding author
# (joint) last author

Files in This Item:
File Description Status SizeFormat
leysen_cmls_2012[1].pdf Published 1321KbAdobe PDFView/Open Request a copy

These files are only available to some KU Leuven Association staff members


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science