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Proteomics of Porphyromonas gingivalis within a model oral microbial community

BACKGROUND: Porphyromonas gingivalis is a periodontal pathogen that resides in a complex multispecies microbial biofilm community known as dental plaque. Confocal laser scanning microscopy showed that P. gingivalis can assemble into communities in vitro with Streptococcus gordonii and Fusobacterium...

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Autores principales: Kuboniwa, Masae, Hendrickson, Erik L, Xia, Qiangwei, Wang, Tiansong, Xie, Hua, Hackett, Murray, Lamont, Richard J
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2689231/
https://www.ncbi.nlm.nih.gov/pubmed/19454014
http://dx.doi.org/10.1186/1471-2180-9-98
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author Kuboniwa, Masae
Hendrickson, Erik L
Xia, Qiangwei
Wang, Tiansong
Xie, Hua
Hackett, Murray
Lamont, Richard J
author_facet Kuboniwa, Masae
Hendrickson, Erik L
Xia, Qiangwei
Wang, Tiansong
Xie, Hua
Hackett, Murray
Lamont, Richard J
author_sort Kuboniwa, Masae
collection PubMed
description BACKGROUND: Porphyromonas gingivalis is a periodontal pathogen that resides in a complex multispecies microbial biofilm community known as dental plaque. Confocal laser scanning microscopy showed that P. gingivalis can assemble into communities in vitro with Streptococcus gordonii and Fusobacterium nucleatum, common constituents of dental plaque. Whole cell quantitative proteomics, along with mutant construction and analysis, were conducted to investigate how P. gingivalis adapts to this three species community. RESULTS: 1156 P. gingivalis proteins were detected qualitatively during comparison of the three species model community with P. gingivalis incubated alone under the same conditions. Integration of spectral counting and summed signal intensity analyses of the dataset showed that 403 proteins were down-regulated and 89 proteins up-regulated. The proteomics results were inspected manually and an ontology analysis conducted using DAVID. Significant decreases were seen in proteins involved in cell shape and the formation of the cell envelope, as well as thiamine, cobalamin, and pyrimidine synthesis and DNA repair. An overall increase was seen in proteins involved in protein synthesis. HmuR, a TonB dependent outer membrane receptor, was up-regulated in the community and an hmuR deficient mutant was deficient in three species community formation, but was unimpaired in its ability to form mono- or dual-species biofilms. CONCLUSION: Collectively, these results indicate that P. gingivalis can assemble into a heterotypic community with F. nucleatum and S. gordonii, and that a community lifestyle provides physiologic support for P. gingivalis. Proteins such as HmuR, that are up-regulated, can be necessary for community structure.
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spelling pubmed-26892312009-06-02 Proteomics of Porphyromonas gingivalis within a model oral microbial community Kuboniwa, Masae Hendrickson, Erik L Xia, Qiangwei Wang, Tiansong Xie, Hua Hackett, Murray Lamont, Richard J BMC Microbiol Research article BACKGROUND: Porphyromonas gingivalis is a periodontal pathogen that resides in a complex multispecies microbial biofilm community known as dental plaque. Confocal laser scanning microscopy showed that P. gingivalis can assemble into communities in vitro with Streptococcus gordonii and Fusobacterium nucleatum, common constituents of dental plaque. Whole cell quantitative proteomics, along with mutant construction and analysis, were conducted to investigate how P. gingivalis adapts to this three species community. RESULTS: 1156 P. gingivalis proteins were detected qualitatively during comparison of the three species model community with P. gingivalis incubated alone under the same conditions. Integration of spectral counting and summed signal intensity analyses of the dataset showed that 403 proteins were down-regulated and 89 proteins up-regulated. The proteomics results were inspected manually and an ontology analysis conducted using DAVID. Significant decreases were seen in proteins involved in cell shape and the formation of the cell envelope, as well as thiamine, cobalamin, and pyrimidine synthesis and DNA repair. An overall increase was seen in proteins involved in protein synthesis. HmuR, a TonB dependent outer membrane receptor, was up-regulated in the community and an hmuR deficient mutant was deficient in three species community formation, but was unimpaired in its ability to form mono- or dual-species biofilms. CONCLUSION: Collectively, these results indicate that P. gingivalis can assemble into a heterotypic community with F. nucleatum and S. gordonii, and that a community lifestyle provides physiologic support for P. gingivalis. Proteins such as HmuR, that are up-regulated, can be necessary for community structure. BioMed Central 2009-05-19 /pmc/articles/PMC2689231/ /pubmed/19454014 http://dx.doi.org/10.1186/1471-2180-9-98 Text en Copyright ©2009 Kuboniwa et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research article
Kuboniwa, Masae
Hendrickson, Erik L
Xia, Qiangwei
Wang, Tiansong
Xie, Hua
Hackett, Murray
Lamont, Richard J
Proteomics of Porphyromonas gingivalis within a model oral microbial community
title Proteomics of Porphyromonas gingivalis within a model oral microbial community
title_full Proteomics of Porphyromonas gingivalis within a model oral microbial community
title_fullStr Proteomics of Porphyromonas gingivalis within a model oral microbial community
title_full_unstemmed Proteomics of Porphyromonas gingivalis within a model oral microbial community
title_short Proteomics of Porphyromonas gingivalis within a model oral microbial community
title_sort proteomics of porphyromonas gingivalis within a model oral microbial community
topic Research article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2689231/
https://www.ncbi.nlm.nih.gov/pubmed/19454014
http://dx.doi.org/10.1186/1471-2180-9-98
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