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Structural and functional characterization of the receptor binding proteins of Escherichia coli O157 phages EP75 and EP335

Bacteriophages (phages) are widely used as biocontrol agents in food and as antibacterial agents for treatment of food production plant surfaces. An important feature of such phages is broad infectivity towards a given pathogenic species. Phages attach to the surfaces of bacterial cells using recept...

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Autores principales: Witte, Sander, Zinsli, Léa V., Gonzalez-Serrano, Rafael, Matter, Cassandra I., Loessner, Martin J., van Mierlo, Joël T., Dunne, Matthew
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8217332/
https://www.ncbi.nlm.nih.gov/pubmed/34194667
http://dx.doi.org/10.1016/j.csbj.2021.06.001
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author Witte, Sander
Zinsli, Léa V.
Gonzalez-Serrano, Rafael
Matter, Cassandra I.
Loessner, Martin J.
van Mierlo, Joël T.
Dunne, Matthew
author_facet Witte, Sander
Zinsli, Léa V.
Gonzalez-Serrano, Rafael
Matter, Cassandra I.
Loessner, Martin J.
van Mierlo, Joël T.
Dunne, Matthew
author_sort Witte, Sander
collection PubMed
description Bacteriophages (phages) are widely used as biocontrol agents in food and as antibacterial agents for treatment of food production plant surfaces. An important feature of such phages is broad infectivity towards a given pathogenic species. Phages attach to the surfaces of bacterial cells using receptor binding proteins (RBPs), namely tail fibers or tailspikes (TSPs). The binding range of RBPs is the primary determinant of phage host range and infectivity, and therefore dictates a phage’s suitability as an antibacterial agent. Phages EP75 and EP335 broadly infect strains of E. coli serotype O157. To better understand host recognition by both phages, here we focused on characterizing the structures and functions of their RBPs. We identified two distinct tail fibers in the genome of the podovirus EP335: gp12 and gp13. Using fluorescence microscopy, we reveal how gp13 recognizes strains of E. coli serotypes O157 and O26. Phage EP75 belongs to the Kuttervirus genus within the Ackermannviridae family and features a four TSP complex (TSPs 1–4) that is universal among such phages. We demonstrate enzymatic activity of TSP1 (gp167) and TSP2 (gp168) toward the O18A and O157 O-antigens of E. coli, respectively, as well as TSP3 activity (gp169.1) against O4, O7, and O9 Salmonella O-antigens. TSPs of EP75 present high similarity to TSPs from E. coli phages CBA120 (TSP2) and HK620 (TSP1) and Salmonella myovirus Det7 (TSP3), which helps explain the cross-genus infectivity observed for EP75.
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spelling pubmed-82173322021-06-29 Structural and functional characterization of the receptor binding proteins of Escherichia coli O157 phages EP75 and EP335 Witte, Sander Zinsli, Léa V. Gonzalez-Serrano, Rafael Matter, Cassandra I. Loessner, Martin J. van Mierlo, Joël T. Dunne, Matthew Comput Struct Biotechnol J Research Article Bacteriophages (phages) are widely used as biocontrol agents in food and as antibacterial agents for treatment of food production plant surfaces. An important feature of such phages is broad infectivity towards a given pathogenic species. Phages attach to the surfaces of bacterial cells using receptor binding proteins (RBPs), namely tail fibers or tailspikes (TSPs). The binding range of RBPs is the primary determinant of phage host range and infectivity, and therefore dictates a phage’s suitability as an antibacterial agent. Phages EP75 and EP335 broadly infect strains of E. coli serotype O157. To better understand host recognition by both phages, here we focused on characterizing the structures and functions of their RBPs. We identified two distinct tail fibers in the genome of the podovirus EP335: gp12 and gp13. Using fluorescence microscopy, we reveal how gp13 recognizes strains of E. coli serotypes O157 and O26. Phage EP75 belongs to the Kuttervirus genus within the Ackermannviridae family and features a four TSP complex (TSPs 1–4) that is universal among such phages. We demonstrate enzymatic activity of TSP1 (gp167) and TSP2 (gp168) toward the O18A and O157 O-antigens of E. coli, respectively, as well as TSP3 activity (gp169.1) against O4, O7, and O9 Salmonella O-antigens. TSPs of EP75 present high similarity to TSPs from E. coli phages CBA120 (TSP2) and HK620 (TSP1) and Salmonella myovirus Det7 (TSP3), which helps explain the cross-genus infectivity observed for EP75. Research Network of Computational and Structural Biotechnology 2021-06-04 /pmc/articles/PMC8217332/ /pubmed/34194667 http://dx.doi.org/10.1016/j.csbj.2021.06.001 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Research Article
Witte, Sander
Zinsli, Léa V.
Gonzalez-Serrano, Rafael
Matter, Cassandra I.
Loessner, Martin J.
van Mierlo, Joël T.
Dunne, Matthew
Structural and functional characterization of the receptor binding proteins of Escherichia coli O157 phages EP75 and EP335
title Structural and functional characterization of the receptor binding proteins of Escherichia coli O157 phages EP75 and EP335
title_full Structural and functional characterization of the receptor binding proteins of Escherichia coli O157 phages EP75 and EP335
title_fullStr Structural and functional characterization of the receptor binding proteins of Escherichia coli O157 phages EP75 and EP335
title_full_unstemmed Structural and functional characterization of the receptor binding proteins of Escherichia coli O157 phages EP75 and EP335
title_short Structural and functional characterization of the receptor binding proteins of Escherichia coli O157 phages EP75 and EP335
title_sort structural and functional characterization of the receptor binding proteins of escherichia coli o157 phages ep75 and ep335
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8217332/
https://www.ncbi.nlm.nih.gov/pubmed/34194667
http://dx.doi.org/10.1016/j.csbj.2021.06.001
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