Photobacterium damselae subsp. piscicida responds to antimicrobial peptides through phage-shock-protein A (PspA)-related extracytoplasmic stress response system

W. C. Tsai, T. Y. Kuo, C. Y. Lin, J. C. Lin, W. J. Chen

研究成果: 雜誌貢獻文章

3 引文 (Scopus)

摘要

Aims: To investigate whether Photobacterium damselae subsp. piscicida (Phdp) can sense and directly respond to the presence of cationic antimicrobial peptides (AMPs). Methods and Results: We performed proteomic methodologies to investigate the responsive proteins of Phdp on exposure to AMP Q6. Proteins significantly altered were analysed by two-dimensional gel electrophoresis (2-DE) and LC-ESI-Q-TOF MS/MS, thus resulting in five outer membrane proteins (OMPs), seven inner membrane proteins (IMPs) and 17 cytoplasmic proteins (CPs) identified. Quantitative real-time PCR was also applied to monitor the mRNA expression level of these target proteins. Conclusions: COG analysis revealed that upon exposure to AMP Q6, the majority of the upregulated proteins were involved in signal transduction mechanism, carbohydrate transport and metabolism, post-translational modification, protein turnover and chaperones, while the downregulated proteins were mainly related to energy production and conversion. Among them, phage-shock-protein A (PspA)-related stress response system was considered to play a crucial role. Significance and Impact of the Study: To the best of our knowledge, this is the first report elucidating Phdp AMP-response mechanism using proteomics approach. AMP-responsive proteins identified in this study could serve as attractive targets for developing more effective antimicrobial agents against Phdp and other marine bacterial pathogens.
原文英語
頁(從 - 到)27-38
頁數12
期刊Journal of Applied Microbiology
118
發行號1
DOIs
出版狀態已發佈 - 一月 1 2015

指紋

Photobacterium
Staphylococcal Protein A
Bacteriophages
Shock
Peptides
Proteins
Proteomics
Membrane Proteins
Antimicrobial Cationic Peptides
Electrophoresis, Gel, Two-Dimensional
Carbohydrate Metabolism
Post Translational Protein Processing
Anti-Infective Agents
Real-Time Polymerase Chain Reaction
Signal Transduction
Down-Regulation
Messenger RNA

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Biotechnology

引用此文

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title = "Photobacterium damselae subsp. piscicida responds to antimicrobial peptides through phage-shock-protein A (PspA)-related extracytoplasmic stress response system",
abstract = "Aims: To investigate whether Photobacterium damselae subsp. piscicida (Phdp) can sense and directly respond to the presence of cationic antimicrobial peptides (AMPs). Methods and Results: We performed proteomic methodologies to investigate the responsive proteins of Phdp on exposure to AMP Q6. Proteins significantly altered were analysed by two-dimensional gel electrophoresis (2-DE) and LC-ESI-Q-TOF MS/MS, thus resulting in five outer membrane proteins (OMPs), seven inner membrane proteins (IMPs) and 17 cytoplasmic proteins (CPs) identified. Quantitative real-time PCR was also applied to monitor the mRNA expression level of these target proteins. Conclusions: COG analysis revealed that upon exposure to AMP Q6, the majority of the upregulated proteins were involved in signal transduction mechanism, carbohydrate transport and metabolism, post-translational modification, protein turnover and chaperones, while the downregulated proteins were mainly related to energy production and conversion. Among them, phage-shock-protein A (PspA)-related stress response system was considered to play a crucial role. Significance and Impact of the Study: To the best of our knowledge, this is the first report elucidating Phdp AMP-response mechanism using proteomics approach. AMP-responsive proteins identified in this study could serve as attractive targets for developing more effective antimicrobial agents against Phdp and other marine bacterial pathogens.",
keywords = "Antimicrobial peptides, Phage-shock-protein A (PspA), Photobacterium damselae subsp. piscicida, Proteomics, Stress response",
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AU - Tsai, W. C.

AU - Kuo, T. Y.

AU - Lin, C. Y.

AU - Lin, J. C.

AU - Chen, W. J.

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N2 - Aims: To investigate whether Photobacterium damselae subsp. piscicida (Phdp) can sense and directly respond to the presence of cationic antimicrobial peptides (AMPs). Methods and Results: We performed proteomic methodologies to investigate the responsive proteins of Phdp on exposure to AMP Q6. Proteins significantly altered were analysed by two-dimensional gel electrophoresis (2-DE) and LC-ESI-Q-TOF MS/MS, thus resulting in five outer membrane proteins (OMPs), seven inner membrane proteins (IMPs) and 17 cytoplasmic proteins (CPs) identified. Quantitative real-time PCR was also applied to monitor the mRNA expression level of these target proteins. Conclusions: COG analysis revealed that upon exposure to AMP Q6, the majority of the upregulated proteins were involved in signal transduction mechanism, carbohydrate transport and metabolism, post-translational modification, protein turnover and chaperones, while the downregulated proteins were mainly related to energy production and conversion. Among them, phage-shock-protein A (PspA)-related stress response system was considered to play a crucial role. Significance and Impact of the Study: To the best of our knowledge, this is the first report elucidating Phdp AMP-response mechanism using proteomics approach. AMP-responsive proteins identified in this study could serve as attractive targets for developing more effective antimicrobial agents against Phdp and other marine bacterial pathogens.

AB - Aims: To investigate whether Photobacterium damselae subsp. piscicida (Phdp) can sense and directly respond to the presence of cationic antimicrobial peptides (AMPs). Methods and Results: We performed proteomic methodologies to investigate the responsive proteins of Phdp on exposure to AMP Q6. Proteins significantly altered were analysed by two-dimensional gel electrophoresis (2-DE) and LC-ESI-Q-TOF MS/MS, thus resulting in five outer membrane proteins (OMPs), seven inner membrane proteins (IMPs) and 17 cytoplasmic proteins (CPs) identified. Quantitative real-time PCR was also applied to monitor the mRNA expression level of these target proteins. Conclusions: COG analysis revealed that upon exposure to AMP Q6, the majority of the upregulated proteins were involved in signal transduction mechanism, carbohydrate transport and metabolism, post-translational modification, protein turnover and chaperones, while the downregulated proteins were mainly related to energy production and conversion. Among them, phage-shock-protein A (PspA)-related stress response system was considered to play a crucial role. Significance and Impact of the Study: To the best of our knowledge, this is the first report elucidating Phdp AMP-response mechanism using proteomics approach. AMP-responsive proteins identified in this study could serve as attractive targets for developing more effective antimicrobial agents against Phdp and other marine bacterial pathogens.

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KW - Photobacterium damselae subsp. piscicida

KW - Proteomics

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