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Two outer membrane proteins are bovine lactoferrin-binding proteins in Mannheimia haemolytica A1
Mannheimia haemolytica is a Gram negative bacterium that is part of the bovine respiratory disease, which causes important economic losses in the livestock industry. In the present work, the interaction between M. haemolytica A1 and bovine lactoferrin (BLf) was studied. This iron-chelating glycoprot...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5013584/ https://www.ncbi.nlm.nih.gov/pubmed/27599994 http://dx.doi.org/10.1186/s13567-016-0378-1 |
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author | Samaniego-Barrón, Luisa Luna-Castro, Sarahí Piña-Vázquez, Carolina Suárez-Güemes, Francisco de la Garza, Mireya |
author_facet | Samaniego-Barrón, Luisa Luna-Castro, Sarahí Piña-Vázquez, Carolina Suárez-Güemes, Francisco de la Garza, Mireya |
author_sort | Samaniego-Barrón, Luisa |
collection | PubMed |
description | Mannheimia haemolytica is a Gram negative bacterium that is part of the bovine respiratory disease, which causes important economic losses in the livestock industry. In the present work, the interaction between M. haemolytica A1 and bovine lactoferrin (BLf) was studied. This iron-chelating glycoprotein is part of the mammalian innate-immune system and is present in milk and mucosal secretions; Lf is also contained in neutrophils secondary granules, which release this glycoprotein at infection sites. It was evidenced that M. haemolytica was not able to use iron-charged BLf (BholoLf) as a sole iron source; nevertheless, iron-lacked BLf (BapoLf) showed a bactericidal effect against M. haemolytica with MIC of 4.88 ± 1.88 and 7.31 ± 1.62 μM for M. haemolytica strain F (field isolate) and M. haemolytica strain R (reference strain), respectively. Through overlay assays and 2-D electrophoresis, two OMP of 32.9 and 34.2 kDa with estimated IP of 8.18 and 9.35, respectively, were observed to bind both BapoLf and BholoLf; these OMP were identified by Maldi-Tof as OmpA (heat-modifiable OMP) and a membrane protein (porin). These M. haemolytica BLf binding proteins could be interacting in vivo with both forms of BLf depending on the iron state of the bovine. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13567-016-0378-1) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5013584 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-50135842016-09-08 Two outer membrane proteins are bovine lactoferrin-binding proteins in Mannheimia haemolytica A1 Samaniego-Barrón, Luisa Luna-Castro, Sarahí Piña-Vázquez, Carolina Suárez-Güemes, Francisco de la Garza, Mireya Vet Res Research Article Mannheimia haemolytica is a Gram negative bacterium that is part of the bovine respiratory disease, which causes important economic losses in the livestock industry. In the present work, the interaction between M. haemolytica A1 and bovine lactoferrin (BLf) was studied. This iron-chelating glycoprotein is part of the mammalian innate-immune system and is present in milk and mucosal secretions; Lf is also contained in neutrophils secondary granules, which release this glycoprotein at infection sites. It was evidenced that M. haemolytica was not able to use iron-charged BLf (BholoLf) as a sole iron source; nevertheless, iron-lacked BLf (BapoLf) showed a bactericidal effect against M. haemolytica with MIC of 4.88 ± 1.88 and 7.31 ± 1.62 μM for M. haemolytica strain F (field isolate) and M. haemolytica strain R (reference strain), respectively. Through overlay assays and 2-D electrophoresis, two OMP of 32.9 and 34.2 kDa with estimated IP of 8.18 and 9.35, respectively, were observed to bind both BapoLf and BholoLf; these OMP were identified by Maldi-Tof as OmpA (heat-modifiable OMP) and a membrane protein (porin). These M. haemolytica BLf binding proteins could be interacting in vivo with both forms of BLf depending on the iron state of the bovine. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13567-016-0378-1) contains supplementary material, which is available to authorized users. BioMed Central 2016-09-06 2016 /pmc/articles/PMC5013584/ /pubmed/27599994 http://dx.doi.org/10.1186/s13567-016-0378-1 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Samaniego-Barrón, Luisa Luna-Castro, Sarahí Piña-Vázquez, Carolina Suárez-Güemes, Francisco de la Garza, Mireya Two outer membrane proteins are bovine lactoferrin-binding proteins in Mannheimia haemolytica A1 |
title | Two outer membrane proteins are bovine lactoferrin-binding proteins in Mannheimia haemolytica A1 |
title_full | Two outer membrane proteins are bovine lactoferrin-binding proteins in Mannheimia haemolytica A1 |
title_fullStr | Two outer membrane proteins are bovine lactoferrin-binding proteins in Mannheimia haemolytica A1 |
title_full_unstemmed | Two outer membrane proteins are bovine lactoferrin-binding proteins in Mannheimia haemolytica A1 |
title_short | Two outer membrane proteins are bovine lactoferrin-binding proteins in Mannheimia haemolytica A1 |
title_sort | two outer membrane proteins are bovine lactoferrin-binding proteins in mannheimia haemolytica a1 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5013584/ https://www.ncbi.nlm.nih.gov/pubmed/27599994 http://dx.doi.org/10.1186/s13567-016-0378-1 |
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