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http://dx.doi.org/10.5478/MSL.2014.5.4.110

Evaluation of MALDI Biotyping for Rapid Subspecies Identification of Carbapenemase-Producing Bacteria via Protein Profiling  

Somboro, Anou M. (Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal)
Tiwari, Dileep (Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal)
Shobo, Adeola (Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal)
Bester, Linda A. (Biomedical Resource Unit, Westville campus, University of KwaZulu Natal)
Kruger, Hendrik G. (Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal)
Govender, Thavendran (Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal)
Essack, Sabiha Y. (Antimicrobial Research Unit, School of Health Sciences, University of KwaZulu-Natal)
Publication Information
Mass Spectrometry Letters / v.5, no.4, 2014 , pp. 110-114 More about this Journal
Abstract
The method of direct mass spectrometry profiling is reliable and reproducible for the rapid identification of clinical isolates of bacteria and fungi. This is the first study evaluating the approach of MALDI-TOF mass spectrometry profiling for rapid identification of carbapenemase-resistant enterobacteriaceae (CRE). Proof of concept was achieved by the discrimination of CRE using MALDI Biotyper MS based on the protein. This profiling appears promising by the visual observation of consistent unique peaks, albeit low intensity, that could be picked up from the mean spectra (MSP) method. The Biotyper MSP creation and identification methods needed to be optimized to provide significantly improved differences in scores to allow for subspecies identification with and without carbapenemases. These spectra were subjected to visual peak picking and in all cases; there were pertinent differences in the presence or absence of potential biomarker peaks to differentiate isolates. We also evaluated this method for potential discrimination between different carbapenemases bacteria, utilizing the same strategy. Based on our data and pending further investigation in other CREs, MALDI-TOF MS has potential as a diagnostic tool for the rapid identification of even closely related carbapenemases but would require a paradigm shift in which Biotyper suppliers enable more flexible software control of mass spectral profiling methods.
Keywords
MALDI-TOF MS; Carbapenemase; Enterobacteriaceae;
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