Structure of the putative long tail fiber receptor-binding tip of a novel temperate bacteriophage from the Antarctic bacterium Bizionia argentinensis JUB59

Tailed bacteriophages are one of the most widespread biological entities on Earth. Their singular structures, such as spikes or fibers are of special interest given their potential use in a wide range of biotechnological applications. In particular, the long fibers present at the termini of the T4 p...

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Published in:Journal of Structural Biology
Main Authors: Pellizza Pena, Leonardo Agustín, López, José L., Vázquez, Susana Claudia, Sycz, Gabriela, Guimarães, Beatriz G., Rinaldi, Jimena Julieta, Goldbaum, Fernando Alberto, Aran, Martin, Mac Cormack, Walter Patricio, Klinke, Sebastian
Format: Article in Journal/Newspaper
Language:English
Published: Academic Press Inc Elsevier Science
Subjects:
Online Access:http://hdl.handle.net/11336/139179
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author Pellizza Pena, Leonardo Agustín
López, José L.
Vázquez, Susana Claudia
Sycz, Gabriela
Guimarães, Beatriz G.
Rinaldi, Jimena Julieta
Goldbaum, Fernando Alberto
Aran, Martin
Mac Cormack, Walter Patricio
Klinke, Sebastian
author_facet Pellizza Pena, Leonardo Agustín
López, José L.
Vázquez, Susana Claudia
Sycz, Gabriela
Guimarães, Beatriz G.
Rinaldi, Jimena Julieta
Goldbaum, Fernando Alberto
Aran, Martin
Mac Cormack, Walter Patricio
Klinke, Sebastian
author_sort Pellizza Pena, Leonardo Agustín
collection CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas)
container_issue 1
container_start_page 107595
container_title Journal of Structural Biology
container_volume 212
description Tailed bacteriophages are one of the most widespread biological entities on Earth. Their singular structures, such as spikes or fibers are of special interest given their potential use in a wide range of biotechnological applications. In particular, the long fibers present at the termini of the T4 phage tail have been studied in detail and are important for host recognition and adsorption. Although significant progress has been made in elucidating structural mechanisms of model phages, the high-resolution structural description of the vast population of marine phages is still unexplored. In this context, we present here the crystal structure of C24, a putative receptor-binding tip-like protein from Bizionia argentinensis JUB59, a psychrotolerant bacterium isolated from the marine surface waters of Potter Cove, Antarctica. The structure resembles the receptor-binding tip from the bacteriophage T4 long tail fiber yet showing marked differences in its domain organization, size, sequence identity and metal binding nature. We confirmed the viral origin of C24 by induction experiments using mitomycin C. Our results reveal the presence of a novel uncharacterized prophage in the genome of B. argentinensis JUB59, whose morphology is compatible with the order Caudovirales and that carries the nucleotide sequence of C24 in its genome. This work provides valuable information to expand our current knowledge on the viral machinery prevalent in the oceans. Fil: Pellizza Pena, Leonardo Agustín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina Fil: López, José L. Universidad de Buenos Aires. Facultad de Farmacia y Bioquimica. Instituto de Investigaciones En Bacteriologia y Virologia Molecular; Argentina Fil: Vázquez, Susana Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de ...
format Article in Journal/Newspaper
genre Antarc*
Antarctic
Antarctica
genre_facet Antarc*
Antarctic
Antarctica
geographic Antarctic
The Antarctic
Potter Cove
Argentina
Pena
geographic_facet Antarctic
The Antarctic
Potter Cove
Argentina
Pena
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language English
long_lat ENVELOPE(40.562,40.562,63.490,63.490)
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http://hdl.handle.net/11336/139179
Pellizza Pena, Leonardo Agustín; López, José L.; Vázquez, Susana Claudia; Sycz, Gabriela; Guimarães, Beatriz G.; et al.; Structure of the putative long tail fiber receptor-binding tip of a novel temperate bacteriophage from the Antarctic bacterium Bizionia argentinensis JUB59; Academic Press Inc Elsevier Science; Journal Of Structural Biology; 212; 1; 10-2020; 1-10
1047-8477
1095-8657
CONICET Digital
CONICET
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publisher Academic Press Inc Elsevier Science
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spelling ftconicet:oai:ri.conicet.gov.ar:11336/139179 2025-01-16T19:38:46+00:00 Structure of the putative long tail fiber receptor-binding tip of a novel temperate bacteriophage from the Antarctic bacterium Bizionia argentinensis JUB59 Pellizza Pena, Leonardo Agustín López, José L. Vázquez, Susana Claudia Sycz, Gabriela Guimarães, Beatriz G. Rinaldi, Jimena Julieta Goldbaum, Fernando Alberto Aran, Martin Mac Cormack, Walter Patricio Klinke, Sebastian application/pdf http://hdl.handle.net/11336/139179 eng eng Academic Press Inc Elsevier Science info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1047847720301684 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jsb.2020.107595 http://hdl.handle.net/11336/139179 Pellizza Pena, Leonardo Agustín; López, José L.; Vázquez, Susana Claudia; Sycz, Gabriela; Guimarães, Beatriz G.; et al.; Structure of the putative long tail fiber receptor-binding tip of a novel temperate bacteriophage from the Antarctic bacterium Bizionia argentinensis JUB59; Academic Press Inc Elsevier Science; Journal Of Structural Biology; 212; 1; 10-2020; 1-10 1047-8477 1095-8657 CONICET Digital CONICET info:eu-repo/semantics/restrictedAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ CAUDOVIRALES FLAVOBACTERIACEAE MITOMYCIN C PROPHAGE PROTEIN STRUCTURE X-RAY CRYSTALLOGRAPHY https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1016/j.jsb.2020.107595 2023-09-24T18:58:27Z Tailed bacteriophages are one of the most widespread biological entities on Earth. Their singular structures, such as spikes or fibers are of special interest given their potential use in a wide range of biotechnological applications. In particular, the long fibers present at the termini of the T4 phage tail have been studied in detail and are important for host recognition and adsorption. Although significant progress has been made in elucidating structural mechanisms of model phages, the high-resolution structural description of the vast population of marine phages is still unexplored. In this context, we present here the crystal structure of C24, a putative receptor-binding tip-like protein from Bizionia argentinensis JUB59, a psychrotolerant bacterium isolated from the marine surface waters of Potter Cove, Antarctica. The structure resembles the receptor-binding tip from the bacteriophage T4 long tail fiber yet showing marked differences in its domain organization, size, sequence identity and metal binding nature. We confirmed the viral origin of C24 by induction experiments using mitomycin C. Our results reveal the presence of a novel uncharacterized prophage in the genome of B. argentinensis JUB59, whose morphology is compatible with the order Caudovirales and that carries the nucleotide sequence of C24 in its genome. This work provides valuable information to expand our current knowledge on the viral machinery prevalent in the oceans. Fil: Pellizza Pena, Leonardo Agustín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina Fil: López, José L. Universidad de Buenos Aires. Facultad de Farmacia y Bioquimica. Instituto de Investigaciones En Bacteriologia y Virologia Molecular; Argentina Fil: Vázquez, Susana Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de ... Article in Journal/Newspaper Antarc* Antarctic Antarctica CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Antarctic The Antarctic Potter Cove Argentina Pena ENVELOPE(40.562,40.562,63.490,63.490) Journal of Structural Biology 212 1 107595
spellingShingle CAUDOVIRALES
FLAVOBACTERIACEAE
MITOMYCIN C
PROPHAGE
PROTEIN STRUCTURE
X-RAY CRYSTALLOGRAPHY
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
Pellizza Pena, Leonardo Agustín
López, José L.
Vázquez, Susana Claudia
Sycz, Gabriela
Guimarães, Beatriz G.
Rinaldi, Jimena Julieta
Goldbaum, Fernando Alberto
Aran, Martin
Mac Cormack, Walter Patricio
Klinke, Sebastian
Structure of the putative long tail fiber receptor-binding tip of a novel temperate bacteriophage from the Antarctic bacterium Bizionia argentinensis JUB59
title Structure of the putative long tail fiber receptor-binding tip of a novel temperate bacteriophage from the Antarctic bacterium Bizionia argentinensis JUB59
title_full Structure of the putative long tail fiber receptor-binding tip of a novel temperate bacteriophage from the Antarctic bacterium Bizionia argentinensis JUB59
title_fullStr Structure of the putative long tail fiber receptor-binding tip of a novel temperate bacteriophage from the Antarctic bacterium Bizionia argentinensis JUB59
title_full_unstemmed Structure of the putative long tail fiber receptor-binding tip of a novel temperate bacteriophage from the Antarctic bacterium Bizionia argentinensis JUB59
title_short Structure of the putative long tail fiber receptor-binding tip of a novel temperate bacteriophage from the Antarctic bacterium Bizionia argentinensis JUB59
title_sort structure of the putative long tail fiber receptor-binding tip of a novel temperate bacteriophage from the antarctic bacterium bizionia argentinensis jub59
topic CAUDOVIRALES
FLAVOBACTERIACEAE
MITOMYCIN C
PROPHAGE
PROTEIN STRUCTURE
X-RAY CRYSTALLOGRAPHY
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic_facet CAUDOVIRALES
FLAVOBACTERIACEAE
MITOMYCIN C
PROPHAGE
PROTEIN STRUCTURE
X-RAY CRYSTALLOGRAPHY
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
url http://hdl.handle.net/11336/139179