Comparative Proteomics and Secretomics Revealed Virulence and Antibiotic Resistance-Associated Factors in Vibrio parahaemolyticus Recovered From Commonly Consumed Aquatic Products

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Comparative Proteomics and Secretomics Revealed Virulence and Antibiotic Resistance-Associated Factors in Vibrio parahaemolyticus Recovered From Commonly Consumed Aquatic Products. / Zhu, Zhuoying; Yang, Lianzhi; Yu, Pan; Wang, Yongjie; Peng, Xu; Chen, Lanming.

I: Frontiers in Microbiology, Bind 11, 1453, 2020.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Zhu, Z, Yang, L, Yu, P, Wang, Y, Peng, X & Chen, L 2020, 'Comparative Proteomics and Secretomics Revealed Virulence and Antibiotic Resistance-Associated Factors in Vibrio parahaemolyticus Recovered From Commonly Consumed Aquatic Products', Frontiers in Microbiology, bind 11, 1453. https://doi.org/10.3389/fmicb.2020.01453

APA

Zhu, Z., Yang, L., Yu, P., Wang, Y., Peng, X., & Chen, L. (2020). Comparative Proteomics and Secretomics Revealed Virulence and Antibiotic Resistance-Associated Factors in Vibrio parahaemolyticus Recovered From Commonly Consumed Aquatic Products. Frontiers in Microbiology, 11, [1453]. https://doi.org/10.3389/fmicb.2020.01453

Vancouver

Zhu Z, Yang L, Yu P, Wang Y, Peng X, Chen L. Comparative Proteomics and Secretomics Revealed Virulence and Antibiotic Resistance-Associated Factors in Vibrio parahaemolyticus Recovered From Commonly Consumed Aquatic Products. Frontiers in Microbiology. 2020;11. 1453. https://doi.org/10.3389/fmicb.2020.01453

Author

Zhu, Zhuoying ; Yang, Lianzhi ; Yu, Pan ; Wang, Yongjie ; Peng, Xu ; Chen, Lanming. / Comparative Proteomics and Secretomics Revealed Virulence and Antibiotic Resistance-Associated Factors in Vibrio parahaemolyticus Recovered From Commonly Consumed Aquatic Products. I: Frontiers in Microbiology. 2020 ; Bind 11.

Bibtex

@article{7af1619b1ad84b79bed12b8a0c71ed88,
title = "Comparative Proteomics and Secretomics Revealed Virulence and Antibiotic Resistance-Associated Factors in Vibrio parahaemolyticus Recovered From Commonly Consumed Aquatic Products",
abstract = "Vibrio parahaemolyticusis a seafoodborne pathogen that can cause severe gastroenteritis and septicemia diseases in humans and even death. The emergence of multidrug-resistantV. parahaemolyticusleads to difficulties and rising costs of medical treatment. The bacterium of environmental origins containing no major virulence genes (tdhandtrh) has been reported to be associated with infectious diarrhea disease as well. Identification of risk factors inV. parahaemolyticusis imperative for assuming food safety. In this study, we obtained secretomic and proteomic profiles ofV. parahaemolyticusisolated from 12 species of commonly consumed aquatic products and identified candidate protein spots by using two-dimensional gel electrophoresis and liquid chromatography tandem mass spectrometry techniques. A total of 11 common and 28 differential extracellular proteins were found from distinct secretomic profiles, including eight virulence-associated proteins: outer membrane channel TolC, maltoporin, elongation factor Tu, enolase, transaldolase, flagellin C, polar flagellin B/D, and superoxide dismutase, as well as five antimicrobial and/or heavy metal resistance-associated ABC transporter proteins. Comparison of proteomic profiles derived from the 12V. parahaemolyticusisolates also revealed five intracellular virulence-related proteins, including aldehyde-alcohol dehydrogenase, outer membrane protein A, alkyl hydroperoxide reductase C, phosphoenolpyruvate-protein phosphotransferase, and phosphoglycerate kinase. Additionally, our data indicated that aquatic product matrices significantly altered proteomic profiles of theV. parahaemolyticusisolates with a number of differentially expressed proteins identified. The results in this study meet the increasing need for novel diagnosis candidates of the leading seafoodborne pathogen worldwide.",
keywords = "Vibrio parahaemolyticus, secretome, proteome, virulence, resistance, aquatic products, HEAVY-METAL RESISTANCE, VIBRIO-PARAHAEMOLYTICUS, VACCINE CANDIDATE, DEHYDROGENASE, DETERMINANTS, VULNIFICUS, MALTOPORIN, SHELLFISH, BACTERIAL, MECHANISM",
author = "Zhuoying Zhu and Lianzhi Yang and Pan Yu and Yongjie Wang and Xu Peng and Lanming Chen",
year = "2020",
doi = "10.3389/fmicb.2020.01453",
language = "English",
volume = "11",
journal = "Frontiers in Microbiology",
issn = "1664-302X",
publisher = "Frontiers Media S.A.",

}

RIS

TY - JOUR

T1 - Comparative Proteomics and Secretomics Revealed Virulence and Antibiotic Resistance-Associated Factors in Vibrio parahaemolyticus Recovered From Commonly Consumed Aquatic Products

AU - Zhu, Zhuoying

AU - Yang, Lianzhi

AU - Yu, Pan

AU - Wang, Yongjie

AU - Peng, Xu

AU - Chen, Lanming

PY - 2020

Y1 - 2020

N2 - Vibrio parahaemolyticusis a seafoodborne pathogen that can cause severe gastroenteritis and septicemia diseases in humans and even death. The emergence of multidrug-resistantV. parahaemolyticusleads to difficulties and rising costs of medical treatment. The bacterium of environmental origins containing no major virulence genes (tdhandtrh) has been reported to be associated with infectious diarrhea disease as well. Identification of risk factors inV. parahaemolyticusis imperative for assuming food safety. In this study, we obtained secretomic and proteomic profiles ofV. parahaemolyticusisolated from 12 species of commonly consumed aquatic products and identified candidate protein spots by using two-dimensional gel electrophoresis and liquid chromatography tandem mass spectrometry techniques. A total of 11 common and 28 differential extracellular proteins were found from distinct secretomic profiles, including eight virulence-associated proteins: outer membrane channel TolC, maltoporin, elongation factor Tu, enolase, transaldolase, flagellin C, polar flagellin B/D, and superoxide dismutase, as well as five antimicrobial and/or heavy metal resistance-associated ABC transporter proteins. Comparison of proteomic profiles derived from the 12V. parahaemolyticusisolates also revealed five intracellular virulence-related proteins, including aldehyde-alcohol dehydrogenase, outer membrane protein A, alkyl hydroperoxide reductase C, phosphoenolpyruvate-protein phosphotransferase, and phosphoglycerate kinase. Additionally, our data indicated that aquatic product matrices significantly altered proteomic profiles of theV. parahaemolyticusisolates with a number of differentially expressed proteins identified. The results in this study meet the increasing need for novel diagnosis candidates of the leading seafoodborne pathogen worldwide.

AB - Vibrio parahaemolyticusis a seafoodborne pathogen that can cause severe gastroenteritis and septicemia diseases in humans and even death. The emergence of multidrug-resistantV. parahaemolyticusleads to difficulties and rising costs of medical treatment. The bacterium of environmental origins containing no major virulence genes (tdhandtrh) has been reported to be associated with infectious diarrhea disease as well. Identification of risk factors inV. parahaemolyticusis imperative for assuming food safety. In this study, we obtained secretomic and proteomic profiles ofV. parahaemolyticusisolated from 12 species of commonly consumed aquatic products and identified candidate protein spots by using two-dimensional gel electrophoresis and liquid chromatography tandem mass spectrometry techniques. A total of 11 common and 28 differential extracellular proteins were found from distinct secretomic profiles, including eight virulence-associated proteins: outer membrane channel TolC, maltoporin, elongation factor Tu, enolase, transaldolase, flagellin C, polar flagellin B/D, and superoxide dismutase, as well as five antimicrobial and/or heavy metal resistance-associated ABC transporter proteins. Comparison of proteomic profiles derived from the 12V. parahaemolyticusisolates also revealed five intracellular virulence-related proteins, including aldehyde-alcohol dehydrogenase, outer membrane protein A, alkyl hydroperoxide reductase C, phosphoenolpyruvate-protein phosphotransferase, and phosphoglycerate kinase. Additionally, our data indicated that aquatic product matrices significantly altered proteomic profiles of theV. parahaemolyticusisolates with a number of differentially expressed proteins identified. The results in this study meet the increasing need for novel diagnosis candidates of the leading seafoodborne pathogen worldwide.

KW - Vibrio parahaemolyticus

KW - secretome

KW - proteome

KW - virulence

KW - resistance

KW - aquatic products

KW - HEAVY-METAL RESISTANCE

KW - VIBRIO-PARAHAEMOLYTICUS

KW - VACCINE CANDIDATE

KW - DEHYDROGENASE

KW - DETERMINANTS

KW - VULNIFICUS

KW - MALTOPORIN

KW - SHELLFISH

KW - BACTERIAL

KW - MECHANISM

U2 - 10.3389/fmicb.2020.01453

DO - 10.3389/fmicb.2020.01453

M3 - Journal article

C2 - 32765437

VL - 11

JO - Frontiers in Microbiology

JF - Frontiers in Microbiology

SN - 1664-302X

M1 - 1453

ER -

ID: 247155140