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A Naturally Occurring Antibody Fragment Neutralizes Infectivity of Diverse Infectious Agents
A phosphorylated peptide, named K40H, derived from the constant region of IgMs was detected in human serum by liquid chromatography coupled to high-resolution mass spectrometry. Synthetic K40H proved to exert a potent in vitro activity against fungal pathogens, and to inhibit HIV-1 replication in vi...
Autores principales: | , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5057116/ https://www.ncbi.nlm.nih.gov/pubmed/27725769 http://dx.doi.org/10.1038/srep35018 |
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author | Polonelli, Luciano Ciociola, Tecla Elviri, Lisa Zanello, Pier Paolo Giovati, Laura Arruda, Denise C. Muñoz, Julián E. Mortara, Renato A. Morace, Giulia Borghi, Elisa Galati, Serena Marin, Oriano Casoli, Claudio Pilotti, Elisabetta Ronzi, Paola Travassos, Luiz R. Magliani, Walter Conti, Stefania |
author_facet | Polonelli, Luciano Ciociola, Tecla Elviri, Lisa Zanello, Pier Paolo Giovati, Laura Arruda, Denise C. Muñoz, Julián E. Mortara, Renato A. Morace, Giulia Borghi, Elisa Galati, Serena Marin, Oriano Casoli, Claudio Pilotti, Elisabetta Ronzi, Paola Travassos, Luiz R. Magliani, Walter Conti, Stefania |
author_sort | Polonelli, Luciano |
collection | PubMed |
description | A phosphorylated peptide, named K40H, derived from the constant region of IgMs was detected in human serum by liquid chromatography coupled to high-resolution mass spectrometry. Synthetic K40H proved to exert a potent in vitro activity against fungal pathogens, and to inhibit HIV-1 replication in vitro and ex vivo. It also showed a therapeutic effect against an experimental infection by Candida albicans in the invertebrate model Galleria mellonella. K40H represents the proof of concept of the innate role that naturally occurring antibody fragments may exert against infectious agents, shedding a new light upon the posthumous role of antibodies and opening a new scenario on the multifaceted functionality of humoral immunity. |
format | Online Article Text |
id | pubmed-5057116 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-50571162016-10-24 A Naturally Occurring Antibody Fragment Neutralizes Infectivity of Diverse Infectious Agents Polonelli, Luciano Ciociola, Tecla Elviri, Lisa Zanello, Pier Paolo Giovati, Laura Arruda, Denise C. Muñoz, Julián E. Mortara, Renato A. Morace, Giulia Borghi, Elisa Galati, Serena Marin, Oriano Casoli, Claudio Pilotti, Elisabetta Ronzi, Paola Travassos, Luiz R. Magliani, Walter Conti, Stefania Sci Rep Article A phosphorylated peptide, named K40H, derived from the constant region of IgMs was detected in human serum by liquid chromatography coupled to high-resolution mass spectrometry. Synthetic K40H proved to exert a potent in vitro activity against fungal pathogens, and to inhibit HIV-1 replication in vitro and ex vivo. It also showed a therapeutic effect against an experimental infection by Candida albicans in the invertebrate model Galleria mellonella. K40H represents the proof of concept of the innate role that naturally occurring antibody fragments may exert against infectious agents, shedding a new light upon the posthumous role of antibodies and opening a new scenario on the multifaceted functionality of humoral immunity. Nature Publishing Group 2016-10-11 /pmc/articles/PMC5057116/ /pubmed/27725769 http://dx.doi.org/10.1038/srep35018 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Polonelli, Luciano Ciociola, Tecla Elviri, Lisa Zanello, Pier Paolo Giovati, Laura Arruda, Denise C. Muñoz, Julián E. Mortara, Renato A. Morace, Giulia Borghi, Elisa Galati, Serena Marin, Oriano Casoli, Claudio Pilotti, Elisabetta Ronzi, Paola Travassos, Luiz R. Magliani, Walter Conti, Stefania A Naturally Occurring Antibody Fragment Neutralizes Infectivity of Diverse Infectious Agents |
title | A Naturally Occurring Antibody Fragment Neutralizes Infectivity of Diverse Infectious Agents |
title_full | A Naturally Occurring Antibody Fragment Neutralizes Infectivity of Diverse Infectious Agents |
title_fullStr | A Naturally Occurring Antibody Fragment Neutralizes Infectivity of Diverse Infectious Agents |
title_full_unstemmed | A Naturally Occurring Antibody Fragment Neutralizes Infectivity of Diverse Infectious Agents |
title_short | A Naturally Occurring Antibody Fragment Neutralizes Infectivity of Diverse Infectious Agents |
title_sort | naturally occurring antibody fragment neutralizes infectivity of diverse infectious agents |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5057116/ https://www.ncbi.nlm.nih.gov/pubmed/27725769 http://dx.doi.org/10.1038/srep35018 |
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