Proteomic identification of membrane proteins regulating antimicrobial peptide resistance in<i>Vibrio parahaemolyticus</i>

Shen, Chi-Tsung; Kuo, Tsun-Yung; Lin, Chai-Ching; Chow, Lu-Ping; Chen, W.-J.

doi:10.1111/j.1365-2672.2009.04544.x

Cited by 35 publications

(35 citation statements)

References 47 publications

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“…Dihydrolipoamide dehydrogenase provides acetyl-CoA required for TCA cycle and biosynthesis of fatty acids. High levels of dihydrolipoamide dehydrogenase was also reported in several other microorganisms like antimicrobial peptide-resistant Vibrio parahaemolyticus [46], toluene-resistant Pseudomonas putida [47] and tellurite- resistant E. coli [48]; suggesting the need of the enzyme for addition energy requirement in survival.…”

Section: Resultsmentioning

confidence: 81%

Comparative Proteomics of Inner Membrane Fraction from Carbapenem-Resistant Acinetobacter baumannii with a Reference Strain

et al. 2012

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Acinetobacter baumannii has been identified by the Infectious Diseases Society of America as one of the six pathogens that cause majority of hospital infections. Increased resistance of A. baumannii even to the latest generation of β-lactams like carbapenem is an immediate threat to mankind. As inner-membrane fraction plays a significant role in survival of A. baumannii, we investigated the inner-membrane fraction proteome of carbapenem-resistant strain of A. baumannii using Differential In-Gel Electrophoresis (DIGE) followed by DeCyder, Progenesis and LC-MS/MS analysis. We identified 19 over-expressed and 4 down-regulated proteins (fold change>2, p <0.05) in resistant strain as compared to reference strain. Some of the upregulated proteins in resistant strain and their association with carbapenem resistance in A. baumannii are: i) β-lactamases, AmpC and OXA-51: cleave and inactivate carbapenem ii) metabolic enzymes, ATP synthase, malate dehydrogenase and 2-oxoglutarate dehydrogenase: help in increased energy production for the survival and iii) elongation factor Tu and ribosomal proteins: help in the overall protein production. Further, entry of carbapenem perhaps is limited by controlled production of OmpW and low levels of surface antigen help to evade host defence mechanism in developing resistance in A. baumannii . Present results support a model for the importance of proteins of inner-membrane fraction and their synergistic effect in the mediation of resistance of A. baumannii to carbapenem.

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Section: Resultsmentioning

confidence: 81%

Comparative Proteomics of Inner Membrane Fraction from Carbapenem-Resistant Acinetobacter baumannii with a Reference Strain

et al. 2012

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“…Indeed, several studies have reported that flagellin appeared on 2‐DE gels when bacterial membranes were isolated by ultracentrifugation and dissolved in SLS (Xu et al. 2004; Shen et al. 2010).…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis reveals responsive proteins of Vibrio parahaemolyticus on exposure to cationic antimicrobial peptides

Chiu

Kuo

Lin

et al. 2010

Journal of Applied Microbiology

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Aims: To investigate whether Vibrio parahaemolyticus 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 V. parahaemolyticus on exposure to AMP Q6. Differential expression patterns of the outer membrane, inner membrane and cytoplasmic proteins (OMPs, IMPs and CPs) from the bacteria with or without Q6 treatment were obtained using two‐dimensional gel electrophoresis (2‐DE). Three OMPs (maltoporin, flagellin and OmpV), two IMPs (ATP synthase F1, alpha subunit; and OmpV) and three CPs (pyruvate dehydrogenase subunit E1, glyceraldehyde‐3‐phosphate dehydrogenase and inositol‐5‐monophosphate dehydrogenase) were identified using LC‐ESI‐Q‐TOF MS/MS and Mascot program. Real‐time quantitative polymerase chain reaction was also performed to determine the mRNA expression level of the target genes. Conclusions: Our results suggested that V. parahaemolyticus may directly respond to AMPs through the upregulation of the efflux channel, increased yield of energy, effective repair of damaged membranes and downregulation of carbohydrate and nucleotide metabolism for energy preservation. Significance and Impact of the Study: AMP‐responsive proteins identified in the current study could serve as attractive targets for developing more effective antimicrobial agents.

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“…Additionally, peptidomic approaches tackle the study of resistance mechanisms, in support of the development of more sustainable antimicrobial agents (Shen et al 2010). For example, proteins regulating AMP resistance in Vibrio parahaemolyticus have been discovered using membrane subproteome analysis (Shen et al 2010).…”

Section: Peptidomicsmentioning

confidence: 99%

“…For example, proteins regulating AMP resistance in Vibrio parahaemolyticus have been discovered using membrane subproteome analysis (Shen et al 2010). …”

Section: Peptidomicsmentioning

confidence: 99%

New trends in peptide-based anti-biofilm strategies: a review of recent achievements and bioinformatic approaches

2012

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Antimicrobial peptides (AMPs) have a broad spectrum of activity and unspecific mechanisms of action. Therefore, they are seen as valid alternatives to overcome clinically relevant biofilms and reduce the chance of acquired resistance. This paper reviews AMPs and anti-biofilm AMP-based strategies and discusses ongoing and future work. Recent studies report successful AMP-based prophylactic and therapeutic strategies, several databases catalogue AMP information and analysis tools, and novel bioinformatics tools are supporting AMP discovery and design. However, most AMP studies are performed with planktonic cultures, and most studies on sessile cells test AMPs on growing rather than mature biofilms. Promising preliminary synergistic studies have to be consubstantiated and the study of functionalized coatings with AMPs must be further explored. Standardized operating protocols, to enforce the repeatability and reproducibility of AMP anti-biofilm tests, and automated means of screening and processing the ever-expanding literature are still missing.

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Proteomic identification of membrane proteins regulating antimicrobial peptide resistance inVibrio parahaemolyticus

Cited by 35 publications

References 47 publications

Comparative Proteomics of Inner Membrane Fraction from Carbapenem-Resistant Acinetobacter baumannii with a Reference Strain

Comparative Proteomics of Inner Membrane Fraction from Carbapenem-Resistant Acinetobacter baumannii with a Reference Strain

Proteomic analysis reveals responsive proteins of Vibrio parahaemolyticus on exposure to cationic antimicrobial peptides

New trends in peptide-based anti-biofilm strategies: a review of recent achievements and bioinformatic approaches

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