K. Sparbier

Publications (5)2.86 Total impact

• Article: MALDI-TOF MS based functional assay for the rapid detection of resistance against beta-lactam antibiotics

  K. Sparbier, S. Schubert, U. Weller, C. Boogen, M. Kostrzewa
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  ABSTRACT: Resistance against ss-lactam antibiotics is a growing challenge for managing severe bacterial infections. The rapid and cost efficient determination of ss-lactam resistance is an important prerequisite for the choice of an adequate antibiotic therapy. ss-lactam resistance is mainly based on the expression/overexpression of ss-lactamases destroying the central ss-lactam ring of these drugs by hydrolysis. Hydrolysis corresponds to a mass shift of plus 18 Da which can be easily detected by MALDI-TOF mass spectrometry. Therefore, a MALDI-TOF MS based assay was set up to investigate different enterobacteria for resistance against different ss-lactam antibiotics: Ampicillin, Piperacillin, Cefotaxime, Ceftazidime, Ertapenem, Imipenem and Meropenem. ss-lactamases are enzymes comprising a high turn over rate. Therefore, hydrolysis can already be detected by MALDI-TOF MS after a few hours of incubation of the bacteria to be tested with the respective antibiotic. The comparison of the MS-derived data with the dat
  J Clin Microbiol. 12/2011;
• Article: Rapid detection of Salmonella sp. by means of a combination of selective enrichment broth and MALDI-TOF MS.

  K Sparbier, U Weller, C Boogen, M Kostrzewa
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  ABSTRACT: The identification of Salmonella sp. in stool samples usually takes 2 days when employing routine procedures. Fast approaches are necessary in order to shorten the analysis time. The aim of this work was the development of a rapid procedure for the detection of Salmonella sp. from clinical stool samples. Spiked stool samples were cultured in selective selenite enrichment broth. Identifications were directly performed from the liquid broth by the MALDI Biotyper. After the evaluation of this method, the same procedure was applied to clinical samples. Coevally, the samples were streaked on Hektoen agar and single colonies were analyzed by the MALDI Biotyper. For comparison, the liquid broth was plated according to the standard laboratory procedure. A total of 4,847 samples were analyzed for Salmonella sp. In total, 108 Salmonella sp.-positive samples were identified; 66 of these were identified after the streaking of stool samples on Hektoen agar and subsequent MALDI Biotyper analysis of Salmonella sp. suspicious colonies. These and a further 34 samples were detected as Salmonella sp.-positive directly from the selenite enrichment broth on day one. Eight Salmonella sp.-positive samples were not detected before plating of the selenite broth and subsequent MALDI Biotyper analysis on day two. The combination of MALDI Biotyper analysis and selective selenite enrichment broth identification delivers positive results for the majority of the samples already after one day.
  European Journal of Clinical Microbiology 08/2011; 31(5):767-73. · 2.86 Impact Factor
• Article: P41-M Automated LC-MALDI Analysis of Glycopeptides from Glycoprotein Digests Using DHB as Matrix

  A. Resemann, A. Asperger, K. Sparbier, K. Seemann, T. Eichhorn, C. Hunzinger, G. Stein, L. Vorwerg, D. Suckau
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  ABSTRACT: 2,5-Dihydroxybenzoic acid (DHB) is the matrix of choice for carbohydrate and glycopeptide analysis, but due to the inhomogeneous surface morphology of samples prepared with DHB, it is typically incompatible with automated measurements.
• Article: P183-T Analysis of Glycoproteins in Human Serum by Means of Glyco-Specific Magnetic Bead Separation and LC-MALDI with Automated Glycopeptide Detection

  K. Sparbier, A. Asperger, A. Resemann, I. Kessler, S. Koch, T Wenzel, G. Shi, G. Stein, L. Vorwerg, D. Suckau, M Kostrzewa
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  ABSTRACT: Comprehensive proteomic analyses require efficient and selective pre-fractionation to facilitate analysis of post-translationally modified peptides and proteins and automated analysis procedures for the detection, identification, and structural characterization of the corresponding peptide modification.
• Article: P11-M Comprehensive and Reliable Proteome Analysis Using Bioinformatic Strategies for Automated Result Validation

  M. Macht, C. Albers, K. Sparbier, A. Asperger, J. Glandorf, H. Thiele
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  ABSTRACT: Proteomic analyses typically produce massive amounts of mass spectrometric data, which are analyzed in an automated way by database search engines for retrieval of peptide sequences and subsequent inference on the corresponding protein sequences. However, this process turned out to be error prone, producing false positives and multiple hits for the same proteins for various reasons.