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  Receptor binding proteins of Listeria monocytogenes bacteriophages A118 and P35 recognize serovar-specific teichoic acids

Bielmann, R., Habann, M., Eugster, M. R., Lurz, R., Calendar, R., Klumpp, J., et al. (2015). Receptor binding proteins of Listeria monocytogenes bacteriophages A118 and P35 recognize serovar-specific teichoic acids. Virology, 477, 110-118.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-A96C-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-A96D-8
Genre: Journal Article

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 Creators:
Bielmann, Regula1, Author
Habann, Matthias 1, Author
Eugster, Marcel R. 1, Author
Lurz, Rudi2, Author              
Calendar, Richard3, Author
Klumpp, Jochen1, Author
Loessner, Martin J. 1, Author
Affiliations:
1Institute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland, ou_persistent22              
2Imaging/Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              
3Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA, ou_persistent22              

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Free keywords: Baseplate model; Caudovirales; Fluorescence microscopy; Immuno-gold labeling; Phage adsorption; Phage crosslink
 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.

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Language(s): eng - English
 Dates: 2014-12-222015-02-212015-03
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Virology
Source Genre: Journal
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Publ. Info: Elsevier, Inc.
Pages: - Volume / Issue: 477 Sequence Number: - Start / End Page: 110 - 118 Identifier: ISSN: 0042-6822
CoNE: https://pure.mpg.de/cone/journals/resource/954922647063