Optimization of a lysis method to isolate periplasmic proteins from Gram-negative bacteria for clinical mass spectrometry.
clinical mass spectrometry
infectious disease
periplasmic protein
sample preparation
top-down proteomics
Journal
Proteomics. Clinical applications
ISSN: 1862-8354
Titre abrégé: Proteomics Clin Appl
Pays: Germany
ID NLM: 101298608
Informations de publication
Date de publication:
11 2021
11 2021
Historique:
revised:
06
08
2021
received:
13
07
2021
accepted:
08
08
2021
pubmed:
10
8
2021
medline:
15
3
2022
entrez:
9
8
2021
Statut:
ppublish
Résumé
Clinical mass spectrometry requires a simple step process for sample preparation. This study aims to optimize the method for isolating periplasmic protein from Gram-negative bacteria and apply to clinical mass spectrometry. The Klebsiella pneumoniae carbapenemase (KPC)-producing E. coli standard cells were used for optimizing the osmotic shock (OS) lysis method. The supernatant from OS lysis was analysed by LC-MS/MS and MALDI-TOF MS. The effectiveness of the OS lysis method for KPC-2-producing Enterobacteriaceae clinical isolates were then confirmed by MALDI-TOF MS. The optimized OS lysis using KPC-2 producing E. coli standard cells showed a high yield of KPC-2 protein and enriches periplasmic proteins. Compared with other lysis methods, the detection sensitivity of KPC-2 protein significantly increased in MALDI-TOF MS analysis. Nineteen clinical isolates were validated by MALDI-TOF MS using the OS method, which also showed higher detection sensitivity compared to other lysis method (e.g., 1.5% n-octyl-β-D-glucopyranoside) (p < 0.001). This study provides a straightforward, rapid, affordable, and detergent-free method for the analysis of periplasmic proteins from Enterobacteriaceae clinical isolates. This approach may contribute to MS-based clinical diagnostics.
Identifiants
pubmed: 34370896
doi: 10.1002/prca.202100044
doi:
Substances chimiques
Periplasmic Proteins
0
Sodium Chloride
451W47IQ8X
beta-lactamase KPC-2
EC 3.5.2.-
beta-Lactamases
EC 3.5.2.6
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2100044Informations de copyright
© 2021 Wiley-VCH GmbH.
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