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Rapid detection of porins by matrix-assisted laser desorption/ionization-time of flight mass spectrometry.

The rapid and cost-efficient determination of carbapenem resistance is an important prerequisite for the choice of an adequate antibiotic therapy. A MALDI-TOF MS-based assay was set up to detect porins in the current study. A loss of the components of porin alone such as OmpK35/OmpK36 or together wi... Full description

Journal Title: Frontiers in microbiology 2015, Vol.6, p.784
Main Author: Hu, Yan-Yan
Other Authors: Cai, Jia-Chang , Zhou, Hong-Wei , Zhang, Rong , Chen, Gong-Xiang
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 1664-302X ; DOI: 10.3389/fmicb.2015.00784
Link: http://search.proquest.com/docview/1706575556/?pq-origsite=primo
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title: Rapid detection of porins by matrix-assisted laser desorption/ionization-time of flight mass spectrometry.
format: Article
creator:
  • Hu, Yan-Yan
  • Cai, Jia-Chang
  • Zhou, Hong-Wei
  • Zhang, Rong
  • Chen, Gong-Xiang
subjects:
  • E. Coli
  • K. Pneumoniae
  • Maldi-Tof MS
  • SDS-Page
  • Outer Membrane Protein
ispartof: Frontiers in microbiology, 2015, Vol.6, p.784
description: The rapid and cost-efficient determination of carbapenem resistance is an important prerequisite for the choice of an adequate antibiotic therapy. A MALDI-TOF MS-based assay was set up to detect porins in the current study. A loss of the components of porin alone such as OmpK35/OmpK36 or together with the production of carbapenemases will augment the carbapenem resistance. Ten strains of E. coli and eight strains of K. pneumoniae were conducted for both SDS-PAGE and MALDI-TOF MS analysis. MALDI-TOF/TOF MS analysis was then performed to verify the corrospondence of proteins between SDS-PAGE and MALDI-TOF MS. The results indicated that the mass spectrum of ca. 35,000-m/z, 37,000-m/z and 38,000-m/z peaks of E. coli ATCC 25922 corresponded to OmpA, OmpC and OmpF with molecular weight of approximately ca. 38 kDa, 40 kDa and 41 kDa in SDS-PAGE gel, respectively. The band of OmpC and OmpF porins were unable to be distinguished by SDS-PAGE, whereas it was easy to be differentiated by MALDI-TOF MS. As for K. pneumoniae isolates, the mass spectrum of ca. 36,000-m/z and 38,600-m/z peaks was observed corresponding to OmpA and OmpK36 with molecular weight of approximately ca. 40 kDa and 42 kDa in SDS-PAGE gel, respectively. Porin OmpK35 was not observed in the current SDS-PAGE, while a 37,000-m/z peak was found in K. pneumoniae ATCC 13883 and carbapenem-susceptible strains by MALDI-TOF MS which was presumed to be the characteristic peak of the OmpK35 porin. Compared with SDS-PAGE, MALDI-TOF MS is able to rapidly identify the porin-deficient strains within half an hour with better sensitivity, less cost, and is easier to operate and has less interference.
language: eng
source:
identifier: ISSN: 1664-302X ; DOI: 10.3389/fmicb.2015.00784
fulltext: fulltext
issn:
  • 1664302X
  • 1664-302X
url: Link


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titleRapid detection of porins by matrix-assisted laser desorption/ionization-time of flight mass spectrometry.
creatorHu, Yan-Yan ; Cai, Jia-Chang ; Zhou, Hong-Wei ; Zhang, Rong ; Chen, Gong-Xiang
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identifierISSN: 1664-302X ; DOI: 10.3389/fmicb.2015.00784
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descriptionThe rapid and cost-efficient determination of carbapenem resistance is an important prerequisite for the choice of an adequate antibiotic therapy. A MALDI-TOF MS-based assay was set up to detect porins in the current study. A loss of the components of porin alone such as OmpK35/OmpK36 or together with the production of carbapenemases will augment the carbapenem resistance. Ten strains of E. coli and eight strains of K. pneumoniae were conducted for both SDS-PAGE and MALDI-TOF MS analysis. MALDI-TOF/TOF MS analysis was then performed to verify the corrospondence of proteins between SDS-PAGE and MALDI-TOF MS. The results indicated that the mass spectrum of ca. 35,000-m/z, 37,000-m/z and 38,000-m/z peaks of E. coli ATCC 25922 corresponded to OmpA, OmpC and OmpF with molecular weight of approximately ca. 38 kDa, 40 kDa and 41 kDa in SDS-PAGE gel, respectively. The band of OmpC and OmpF porins were unable to be distinguished by SDS-PAGE, whereas it was easy to be differentiated by MALDI-TOF MS. As for K. pneumoniae isolates, the mass spectrum of ca. 36,000-m/z and 38,600-m/z peaks was observed corresponding to OmpA and OmpK36 with molecular weight of approximately ca. 40 kDa and 42 kDa in SDS-PAGE gel, respectively. Porin OmpK35 was not observed in the current SDS-PAGE, while a 37,000-m/z peak was found in K. pneumoniae ATCC 13883 and carbapenem-susceptible strains by MALDI-TOF MS which was presumed to be the characteristic peak of the OmpK35 porin. Compared with SDS-PAGE, MALDI-TOF MS is able to rapidly identify the porin-deficient strains within half an hour with better sensitivity, less cost, and is easier to operate and has less interference.
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