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Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae
BACKGROUND: Mycoplasma agalactiae is the main etiological agent of Contagious Agalactia syndrome of small ruminants notifiable to the World Organization for Animal Health. Despite serious economic losses, successful vaccines are unavailable, largely because its colonization and invasion factors are...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8991494/ https://www.ncbi.nlm.nih.gov/pubmed/35395771 http://dx.doi.org/10.1186/s12866-022-02512-2 |
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author | Barbosa, Maysa Santos Marques, Lucas Miranda Timenetsky, Jorge Rosengarten, Renate Spergser, Joachim Chopra-Dewasthaly, Rohini |
author_facet | Barbosa, Maysa Santos Marques, Lucas Miranda Timenetsky, Jorge Rosengarten, Renate Spergser, Joachim Chopra-Dewasthaly, Rohini |
author_sort | Barbosa, Maysa Santos |
collection | PubMed |
description | BACKGROUND: Mycoplasma agalactiae is the main etiological agent of Contagious Agalactia syndrome of small ruminants notifiable to the World Organization for Animal Health. Despite serious economic losses, successful vaccines are unavailable, largely because its colonization and invasion factors are not well understood. This study evaluates the role of two recently identified antigenic proteins (MAG_1560, MAG_6130) and the cytadhesin P40 in pathogenicity related phenotypes. RESULTS: Adhesion to HeLa and sheep primary mammary stromal cells (MSC) was evaluated using ELISA, as well as in vitro adhesion assays on monolayer cell cultures. The results demonstrated MAG_6130 as a novel adhesin of M. agalactiae whose capacity to adhere to eukaryotic cells was significantly reduced by specific antiserum. Additionally, these proteins exhibited significant binding to plasminogen and extracellular matrix (ECM) proteins like lactoferrin, fibrinogen and fibronectin, a feature that could potentially support the pathogen in host colonization, tissue migration and immune evasion. Furthermore, these proteins played a detrimental role on the host cell proliferation and viability and were observed to activate pro-apoptotic genes indicating their involvement in cell death when eukaryotic cells were infected with M. agalactiae. CONCLUSIONS: To summarize, the hypothetical protein corresponding to MAG_6130 has not only been assigned novel adhesion functions but together with P40 it is demonstrated for the first time to bind to lactoferrin and ECM proteins thereby playing important roles in host colonization and pathogenicity. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12866-022-02512-2. |
format | Online Article Text |
id | pubmed-8991494 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-89914942022-04-09 Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae Barbosa, Maysa Santos Marques, Lucas Miranda Timenetsky, Jorge Rosengarten, Renate Spergser, Joachim Chopra-Dewasthaly, Rohini BMC Microbiol Research BACKGROUND: Mycoplasma agalactiae is the main etiological agent of Contagious Agalactia syndrome of small ruminants notifiable to the World Organization for Animal Health. Despite serious economic losses, successful vaccines are unavailable, largely because its colonization and invasion factors are not well understood. This study evaluates the role of two recently identified antigenic proteins (MAG_1560, MAG_6130) and the cytadhesin P40 in pathogenicity related phenotypes. RESULTS: Adhesion to HeLa and sheep primary mammary stromal cells (MSC) was evaluated using ELISA, as well as in vitro adhesion assays on monolayer cell cultures. The results demonstrated MAG_6130 as a novel adhesin of M. agalactiae whose capacity to adhere to eukaryotic cells was significantly reduced by specific antiserum. Additionally, these proteins exhibited significant binding to plasminogen and extracellular matrix (ECM) proteins like lactoferrin, fibrinogen and fibronectin, a feature that could potentially support the pathogen in host colonization, tissue migration and immune evasion. Furthermore, these proteins played a detrimental role on the host cell proliferation and viability and were observed to activate pro-apoptotic genes indicating their involvement in cell death when eukaryotic cells were infected with M. agalactiae. CONCLUSIONS: To summarize, the hypothetical protein corresponding to MAG_6130 has not only been assigned novel adhesion functions but together with P40 it is demonstrated for the first time to bind to lactoferrin and ECM proteins thereby playing important roles in host colonization and pathogenicity. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12866-022-02512-2. BioMed Central 2022-04-08 /pmc/articles/PMC8991494/ /pubmed/35395771 http://dx.doi.org/10.1186/s12866-022-02512-2 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Research Barbosa, Maysa Santos Marques, Lucas Miranda Timenetsky, Jorge Rosengarten, Renate Spergser, Joachim Chopra-Dewasthaly, Rohini Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae |
title | Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae |
title_full | Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae |
title_fullStr | Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae |
title_full_unstemmed | Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae |
title_short | Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae |
title_sort | host cell interactions of novel antigenic membrane proteins of mycoplasma agalactiae |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8991494/ https://www.ncbi.nlm.nih.gov/pubmed/35395771 http://dx.doi.org/10.1186/s12866-022-02512-2 |
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