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Identification of a Peptide Produced by Bifidobacterium longum CECT 7210 with Antirotaviral Activity

Rotavirus is one of the main causes of acute diarrhea and enteritis in infants. Currently, studies are underway to assess the use of probiotics to improve rotavirus vaccine protection. A previous work demonstrated that the probiotic strain Bifidobacterium longum subsp. infantis CECT 7210 is able to...

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Autores principales: Chenoll, Empar, Casinos, Beatriz, Bataller, Esther, Buesa, Javier, Ramón, Daniel, Genovés, Salvador, Fábrega, Joan, Rivero Urgell, Montserrat, Moreno Muñoz, José A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4855034/
https://www.ncbi.nlm.nih.gov/pubmed/27199974
http://dx.doi.org/10.3389/fmicb.2016.00655
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author Chenoll, Empar
Casinos, Beatriz
Bataller, Esther
Buesa, Javier
Ramón, Daniel
Genovés, Salvador
Fábrega, Joan
Rivero Urgell, Montserrat
Moreno Muñoz, José A.
author_facet Chenoll, Empar
Casinos, Beatriz
Bataller, Esther
Buesa, Javier
Ramón, Daniel
Genovés, Salvador
Fábrega, Joan
Rivero Urgell, Montserrat
Moreno Muñoz, José A.
author_sort Chenoll, Empar
collection PubMed
description Rotavirus is one of the main causes of acute diarrhea and enteritis in infants. Currently, studies are underway to assess the use of probiotics to improve rotavirus vaccine protection. A previous work demonstrated that the probiotic strain Bifidobacterium longum subsp. infantis CECT 7210 is able to hinder rotavirus replication both in vitro and in vivo. The present study takes a systematic approach in order to identify the molecule directly involved in rotavirus inhibition. Supernatant protease digestions revealed both the proteinaceous nature of the active substance and the fact that the molecule responsible for inhibiting rotavirus replication is released to the supernatant. Following purification by cationic exchange chromatography, active fractions were obtained and the functional compound was identified as an 11-amino acid peptide (MHQPHQPLPPT, named 11-mer peptide) with a molecular mass of 1.282 KDa. The functionality of 11-mer was verified using the synthesized peptide in Wa, Ito, and VA70 rotavirus infections of both HT-29 and MA-104 cell lines. Finally, protease activity was detected in B. longum subsp. infantis CECT 7210 supernatant, which releases 11-mer peptide. A preliminary identification of the protease is also included in the study.
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spelling pubmed-48550342016-05-19 Identification of a Peptide Produced by Bifidobacterium longum CECT 7210 with Antirotaviral Activity Chenoll, Empar Casinos, Beatriz Bataller, Esther Buesa, Javier Ramón, Daniel Genovés, Salvador Fábrega, Joan Rivero Urgell, Montserrat Moreno Muñoz, José A. Front Microbiol Microbiology Rotavirus is one of the main causes of acute diarrhea and enteritis in infants. Currently, studies are underway to assess the use of probiotics to improve rotavirus vaccine protection. A previous work demonstrated that the probiotic strain Bifidobacterium longum subsp. infantis CECT 7210 is able to hinder rotavirus replication both in vitro and in vivo. The present study takes a systematic approach in order to identify the molecule directly involved in rotavirus inhibition. Supernatant protease digestions revealed both the proteinaceous nature of the active substance and the fact that the molecule responsible for inhibiting rotavirus replication is released to the supernatant. Following purification by cationic exchange chromatography, active fractions were obtained and the functional compound was identified as an 11-amino acid peptide (MHQPHQPLPPT, named 11-mer peptide) with a molecular mass of 1.282 KDa. The functionality of 11-mer was verified using the synthesized peptide in Wa, Ito, and VA70 rotavirus infections of both HT-29 and MA-104 cell lines. Finally, protease activity was detected in B. longum subsp. infantis CECT 7210 supernatant, which releases 11-mer peptide. A preliminary identification of the protease is also included in the study. Frontiers Media S.A. 2016-05-04 /pmc/articles/PMC4855034/ /pubmed/27199974 http://dx.doi.org/10.3389/fmicb.2016.00655 Text en Copyright © 2016 Chenoll, Casinos, Bataller, Buesa, Ramón, Genovés, Fábrega, Rivero Urgell and Moreno Muñoz. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Chenoll, Empar
Casinos, Beatriz
Bataller, Esther
Buesa, Javier
Ramón, Daniel
Genovés, Salvador
Fábrega, Joan
Rivero Urgell, Montserrat
Moreno Muñoz, José A.
Identification of a Peptide Produced by Bifidobacterium longum CECT 7210 with Antirotaviral Activity
title Identification of a Peptide Produced by Bifidobacterium longum CECT 7210 with Antirotaviral Activity
title_full Identification of a Peptide Produced by Bifidobacterium longum CECT 7210 with Antirotaviral Activity
title_fullStr Identification of a Peptide Produced by Bifidobacterium longum CECT 7210 with Antirotaviral Activity
title_full_unstemmed Identification of a Peptide Produced by Bifidobacterium longum CECT 7210 with Antirotaviral Activity
title_short Identification of a Peptide Produced by Bifidobacterium longum CECT 7210 with Antirotaviral Activity
title_sort identification of a peptide produced by bifidobacterium longum cect 7210 with antirotaviral activity
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4855034/
https://www.ncbi.nlm.nih.gov/pubmed/27199974
http://dx.doi.org/10.3389/fmicb.2016.00655
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