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Biofilm-associated proteins: news from Acinetobacter
BACKGROUND: A giant protein called BAP (biofilm-associated protein) plays a role in biofilm formation and adhesion to host cells in A. baumannii. Most of the protein is made by arrays of 80–110 aa modules featuring immunoglobulin-like (Ig-like) motifs. RESULTS: The survey of 541 A. baumannii sequenc...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4647330/ https://www.ncbi.nlm.nih.gov/pubmed/26572057 http://dx.doi.org/10.1186/s12864-015-2136-6 |
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author | De Gregorio, Eliana Del Franco, Mariateresa Martinucci, Marianna Roscetto, Emanuela Zarrilli, Raffaele Di Nocera, Pier Paolo |
author_facet | De Gregorio, Eliana Del Franco, Mariateresa Martinucci, Marianna Roscetto, Emanuela Zarrilli, Raffaele Di Nocera, Pier Paolo |
author_sort | De Gregorio, Eliana |
collection | PubMed |
description | BACKGROUND: A giant protein called BAP (biofilm-associated protein) plays a role in biofilm formation and adhesion to host cells in A. baumannii. Most of the protein is made by arrays of 80–110 aa modules featuring immunoglobulin-like (Ig-like) motifs. RESULTS: The survey of 541 A. baumannii sequenced strains belonging to 108 STs (sequence types) revealed that BAP is highly polymorphic, distinguishable in three main types for changes both in the repetitive and the COOH region. Analyzing the different STs, we found that 29 % feature type-1, 40 % type-2 BAP, 11 % type-3 BAP, 20 % lack BAP. The type-3 variant is restricted to A. baumannii, type-1 and type-2 BAP have been identified also in other species of the Acinetobacter calcoaceticus-baumannii (ACB) complex. A. calcoaceticus and A. pittii also encode BAP-like proteins in which Ig-like repeats are replaced by long tracts of alternating serine and aspartic acid residues. We have identified in species of the ACB complex two additional proteins, BLP1 and BLP2 (BAP-like proteins 1 and 2) which feature Ig-like repeats, share with BAP a sequence motif at the NH2 terminus, and are similarly expressed in stationary growth phase. The knock-out of either BLP1 or BLP2 genes of the A. baumannii ST1 AYE strain severely affected biofilm formation, as measured by comparing biofilm biomass and thickness, and adherence to epithelial cells. BLP1 is missing in the majority of type-3 BAP strains. BLP2 is largely conserved, but is frequently missing in BAP-negative cells. CONCLUSIONS: Multiple proteins sharing Ig-like repeats seem to be involved in biofilm formation. The uneven distribution of the different BAP types, BLP1, and BLP2 is highly indicative that alternative protein complexes involved in biofilm formation are assembled in different A. baumannii strains. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12864-015-2136-6) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4647330 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-46473302015-11-18 Biofilm-associated proteins: news from Acinetobacter De Gregorio, Eliana Del Franco, Mariateresa Martinucci, Marianna Roscetto, Emanuela Zarrilli, Raffaele Di Nocera, Pier Paolo BMC Genomics Research Article BACKGROUND: A giant protein called BAP (biofilm-associated protein) plays a role in biofilm formation and adhesion to host cells in A. baumannii. Most of the protein is made by arrays of 80–110 aa modules featuring immunoglobulin-like (Ig-like) motifs. RESULTS: The survey of 541 A. baumannii sequenced strains belonging to 108 STs (sequence types) revealed that BAP is highly polymorphic, distinguishable in three main types for changes both in the repetitive and the COOH region. Analyzing the different STs, we found that 29 % feature type-1, 40 % type-2 BAP, 11 % type-3 BAP, 20 % lack BAP. The type-3 variant is restricted to A. baumannii, type-1 and type-2 BAP have been identified also in other species of the Acinetobacter calcoaceticus-baumannii (ACB) complex. A. calcoaceticus and A. pittii also encode BAP-like proteins in which Ig-like repeats are replaced by long tracts of alternating serine and aspartic acid residues. We have identified in species of the ACB complex two additional proteins, BLP1 and BLP2 (BAP-like proteins 1 and 2) which feature Ig-like repeats, share with BAP a sequence motif at the NH2 terminus, and are similarly expressed in stationary growth phase. The knock-out of either BLP1 or BLP2 genes of the A. baumannii ST1 AYE strain severely affected biofilm formation, as measured by comparing biofilm biomass and thickness, and adherence to epithelial cells. BLP1 is missing in the majority of type-3 BAP strains. BLP2 is largely conserved, but is frequently missing in BAP-negative cells. CONCLUSIONS: Multiple proteins sharing Ig-like repeats seem to be involved in biofilm formation. The uneven distribution of the different BAP types, BLP1, and BLP2 is highly indicative that alternative protein complexes involved in biofilm formation are assembled in different A. baumannii strains. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12864-015-2136-6) contains supplementary material, which is available to authorized users. BioMed Central 2015-11-14 /pmc/articles/PMC4647330/ /pubmed/26572057 http://dx.doi.org/10.1186/s12864-015-2136-6 Text en © De Gregorio et al. 2015 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 De Gregorio, Eliana Del Franco, Mariateresa Martinucci, Marianna Roscetto, Emanuela Zarrilli, Raffaele Di Nocera, Pier Paolo Biofilm-associated proteins: news from Acinetobacter |
title | Biofilm-associated proteins: news from Acinetobacter |
title_full | Biofilm-associated proteins: news from Acinetobacter |
title_fullStr | Biofilm-associated proteins: news from Acinetobacter |
title_full_unstemmed | Biofilm-associated proteins: news from Acinetobacter |
title_short | Biofilm-associated proteins: news from Acinetobacter |
title_sort | biofilm-associated proteins: news from acinetobacter |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4647330/ https://www.ncbi.nlm.nih.gov/pubmed/26572057 http://dx.doi.org/10.1186/s12864-015-2136-6 |
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