title: Receptor binding proteins of Listeria monocytogenes bacteriophages A118 and P35 recognize serovar-specific teichoic acids.
abstract: 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 tail tip structure for the siphovirus group infecting Listeria monocytogenes. The host-range determining factors in two phages, A118 and P35 specific for L. monocytogenes serovar 1/2 have been determined. Two proteins were identified as RBPs in phage A118. Rhamnose residues in wall teichoic acids represent the binding ligands for both proteins. In phage P35, protein gp16 could be identified as RBP and the role of both rhamnose and N-acetylglucosamine in phage adsorption was confirmed. Immunogold-labeling and transmission electron microscopy allowed the creation of a topological model of the A118 phage tail.
authors.affiliation: Institute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland.
authors.forename: Regula
authors.initials: R
authors.lastname: Bielmann
authors.affiliation: Institute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland.
authors.forename: Matthias
authors.initials: M
authors.lastname: Habann
authors.affiliation: Institute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland.
authors.forename: Marcel R
authors.initials: MR
authors.lastname: Eugster
authors.affiliation: Max-Planck Institute for Molecular Genetics, 14195 Berlin, Germany.
authors.forename: Rudi
authors.initials: R
authors.lastname: Lurz
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA.
authors.forename: Richard
authors.initials: R
authors.lastname: Calendar
authors.affiliation: Institute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland. Electronic address: jochen.klumpp@hest.ethz.ch.
authors.forename: Jochen
authors.initials: J
authors.lastname: Klumpp
authors.affiliation: Institute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland.
authors.forename: Martin J
authors.initials: MJ
authors.lastname: Loessner
mesh_terms: D001435:Bacteriophages / Q000502:physiology* / Q000648:ultrastructure; D058507:Host Specificity; D008089:Listeria monocytogenes / Q000145:classification / Q000648:ultrastructure / Q000821:virology*; D016253:Microscopy, Immunoelectron; D011991:Receptors, Virus / Q000378:metabolism*; D065288:Serogroup; D017906:Siphoviridae / Q000502:physiology / Q000648:ultrastructure; D013682:Teichoic Acids / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000378:metabolism; D053585:Virus Attachment
chemical_list: D011991:Receptors, Virus; D013682:Teichoic Acids; D015678:Viral Structural Proteins
keywords: Baseplate model; Caudovirales; Fluorescence microscopy; Immuno-gold labeling; Phage adsorption; Phage crosslink