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Comparative proteomic analysis of outer membrane protein 43 (omp43)-deficient Bartonella henselae
Outer membrane proteins (OMPs) of Gram-negative bacteria constitute the first line of defense protecting cells against environmental stresses including chemical, biophysical, and biological attacks. Although the 43-kDa OMP (OMP43) is major porin protein among Bartonella henselae-derived OMPs, its fu...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Korean Society of Veterinary Science
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5799401/ https://www.ncbi.nlm.nih.gov/pubmed/28693313 http://dx.doi.org/10.4142/jvs.2018.19.1.59 |
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author | Kang, Jun-Gu Lee, Hee-Woo Ko, Sungjin Chae, Joon-Seok |
author_facet | Kang, Jun-Gu Lee, Hee-Woo Ko, Sungjin Chae, Joon-Seok |
author_sort | Kang, Jun-Gu |
collection | PubMed |
description | Outer membrane proteins (OMPs) of Gram-negative bacteria constitute the first line of defense protecting cells against environmental stresses including chemical, biophysical, and biological attacks. Although the 43-kDa OMP (OMP43) is major porin protein among Bartonella henselae-derived OMPs, its function remains unreported. In this study, OMP43-deficient mutant B. henselae (Δomp43) was generated to investigate OMP43 function. Interestingly, Δomp43 exhibited weaker proliferative ability than that of wild-type (WT) B. henselae. To study the differences in proteomic expression between WT and Δomp43, two-dimensional gel electrophoresis-based proteomic analysis was performed. Based on Clusters of Orthologus Groups functional assignments, 12 proteins were associated with metabolism, 7 proteins associated with information storage and processing, and 3 proteins associated with cellular processing and signaling. By semi-quantitative reverse transcriptase polymerase chain reaction, increases in tldD, efp, ntrX, pdhA, purB, and ATPA mRNA expression and decreases in Rho and yfeA mRNA expression were confirmed in Δomp43. In conclusion, this is the first report showing that a loss of OMP43 expression in B. henselae leads to retarded proliferation. Furthermore, our proteomic data provide useful information for the further investigation of mechanisms related to the growth of B. henselae. |
format | Online Article Text |
id | pubmed-5799401 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | The Korean Society of Veterinary Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-57994012018-02-14 Comparative proteomic analysis of outer membrane protein 43 (omp43)-deficient Bartonella henselae Kang, Jun-Gu Lee, Hee-Woo Ko, Sungjin Chae, Joon-Seok J Vet Sci Original Article Outer membrane proteins (OMPs) of Gram-negative bacteria constitute the first line of defense protecting cells against environmental stresses including chemical, biophysical, and biological attacks. Although the 43-kDa OMP (OMP43) is major porin protein among Bartonella henselae-derived OMPs, its function remains unreported. In this study, OMP43-deficient mutant B. henselae (Δomp43) was generated to investigate OMP43 function. Interestingly, Δomp43 exhibited weaker proliferative ability than that of wild-type (WT) B. henselae. To study the differences in proteomic expression between WT and Δomp43, two-dimensional gel electrophoresis-based proteomic analysis was performed. Based on Clusters of Orthologus Groups functional assignments, 12 proteins were associated with metabolism, 7 proteins associated with information storage and processing, and 3 proteins associated with cellular processing and signaling. By semi-quantitative reverse transcriptase polymerase chain reaction, increases in tldD, efp, ntrX, pdhA, purB, and ATPA mRNA expression and decreases in Rho and yfeA mRNA expression were confirmed in Δomp43. In conclusion, this is the first report showing that a loss of OMP43 expression in B. henselae leads to retarded proliferation. Furthermore, our proteomic data provide useful information for the further investigation of mechanisms related to the growth of B. henselae. The Korean Society of Veterinary Science 2018-01 2018-01-23 /pmc/articles/PMC5799401/ /pubmed/28693313 http://dx.doi.org/10.4142/jvs.2018.19.1.59 Text en © 2018 The Korean Society of Veterinary Science http://creativecommons.org/licenses/by-nc/4.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Article Kang, Jun-Gu Lee, Hee-Woo Ko, Sungjin Chae, Joon-Seok Comparative proteomic analysis of outer membrane protein 43 (omp43)-deficient Bartonella henselae |
title | Comparative proteomic analysis of outer membrane protein 43 (omp43)-deficient Bartonella henselae |
title_full | Comparative proteomic analysis of outer membrane protein 43 (omp43)-deficient Bartonella henselae |
title_fullStr | Comparative proteomic analysis of outer membrane protein 43 (omp43)-deficient Bartonella henselae |
title_full_unstemmed | Comparative proteomic analysis of outer membrane protein 43 (omp43)-deficient Bartonella henselae |
title_short | Comparative proteomic analysis of outer membrane protein 43 (omp43)-deficient Bartonella henselae |
title_sort | comparative proteomic analysis of outer membrane protein 43 (omp43)-deficient bartonella henselae |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5799401/ https://www.ncbi.nlm.nih.gov/pubmed/28693313 http://dx.doi.org/10.4142/jvs.2018.19.1.59 |
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