Wall teichoic acids restrict access of bacteriophage endolysin Ply 118 , 1 Ply 511 , and PlyP 40 cell wall binding domains to the Listeria 2 monocytogenes peptidoglycan 3 4 Marcel
نویسنده
چکیده
4 Marcel R. Eugster and Martin J. Loessner* 5 6 Institute of Food, Nutrition and Health, ETH Zurich, CH-8092 Zurich, Switzerland 7 8 9 10 11 12 13 14 15 Running title: Binding of endolysins to Listeria cell wall 16 17 * Address correspondence to: Martin J. Loessner, [email protected] 18 19 Copyright © 2012, American Society for Microbiology. All Rights Reserved. J. Bacteriol. doi:10.1128/JB.00808-12 JB Accepts, published online ahead of print on 21 September 2012
منابع مشابه
Wall teichoic acids restrict access of bacteriophage endolysin Ply118, Ply511, and PlyP40 cell wall binding domains to the Listeria monocytogenes peptidoglycan.
The C-terminal cell wall binding domains (CBDs) of phage endolysins direct the enzymes to their binding ligands on the bacterial cell wall with high affinity and specificity. The Listeria monocytogenes Ply118, Ply511, and PlyP40 endolysins feature related CBDs which recognize the directly cross-linked peptidoglycan backbone structure of Listeria. However, decoration with fluorescently labeled C...
متن کاملBacteriophage receptors on Listeria monocytogenes cells are the N-acetylglucosamine and rhamnose substituents of teichoic acids or the peptidoglycan itself.
Different approaches were used to examine the function of teichoic acids (TA) as phage receptors among selected Listeria strains, and to identify and characterize specific receptor structures of host cells belonging to different serovars. This included successive removal of cell wall constituents, preparation and purification of TA, and GLC analysis of TA components. Adsorption of Listeria mono...
متن کاملReceptor binding proteins of Listeria monocytogenes bacteriophages A118 and P35 recognize serovar-specific teichoic acids.
Adsorption of a bacteriophage to the host requires recognition of a cell wall-associated receptor by a receptor binding protein (RBP). This recognition is specific, and high affinity binding is essential for efficient virus attachment. The molecular details of phage adsorption to the Gram-positive cell are poorly understood. We present the first description of receptor binding proteins and a ta...
متن کاملGene cloning and expression and secretion of Listeria monocytogenes bacteriophage-lytic enzymes in Lactococcus lactis.
Bacteriophage lysins (Ply), or endolysins, are phage-encoded cell wall lytic enzymes which are synthesized late during virus multiplication and mediate the release of progeny virions. Bacteriophages of the pathogen Listeria monocytogenes encode endolysin enzymes which specifically hydrolyze the cross-linking peptide bridges in Listeria peptidoglycan. Ply118 is a 30.8-kDa L-alanoyl-D-glutamate p...
متن کاملIdentification of a Lipoteichoic Acid Glycosyltransferase Enzyme Reveals that GW-Domain-Containing Proteins Can Be Retained in the Cell Wall of Listeria monocytogenes in the Absence of Lipoteichoic Acid or Its Modifications
UNLABELLED Listeria monocytogenes is a foodborne Gram-positive bacterial pathogen, and many of its virulence factors are either secreted proteins or proteins covalently or noncovalently attached to the cell wall. Previous work has indicated that noncovalently attached proteins with GW (glycine-tryptophan) domains are retained in the cell wall by binding to the cell wall polymer lipoteichoic aci...
متن کامل