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Michiel Kleerebezem

Researcher at Wageningen University and Research Centre

Publications -  311
Citations -  38778

Michiel Kleerebezem is an academic researcher from Wageningen University and Research Centre. The author has contributed to research in topics: Lactococcus lactis & Lactobacillus plantarum. The author has an hindex of 93, co-authored 301 publications receiving 33750 citations. Previous affiliations of Michiel Kleerebezem include Netherlands Bioinformatics Centre.

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Correlation of Lactobacillus rhamnosus Genotypes and Carbohydrate Utilization Signatures Determined by Phenotype Profiling

TL;DR: From the analysis, candidate genes were identified that correlate with l-sorbose and α-methyl-d-glucoside utilization, and the proposed function of these genes could be confirmed by heterologous expression in a strain lacking the genes.
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The Major Autolysin Acm2 from Lactobacillus plantarum Undergoes Cytoplasmic O-Glycosylation

TL;DR: High-resolution liquid chromatography-tandem mass spectrometry was used to study the possible occurrence of glycans on peptides generated from lactobacillary surface proteins by protease treatment and yielded five glycopeptides in various glycoforms, suggesting that Acm2 is O-glycosylated.
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Two Homologous Agr-Like Quorum-Sensing Systems Cooperatively Control Adherence, Cell Morphology, and Cell Viability Properties in Lactobacillus plantarum WCFS1

TL;DR: Microarray analysis suggested that the same cell wall polysaccharide synthesis genes, stress response-related genes, and cell wall protein-encoding genes were affected in the DeltalamA and DeltalusR mutants, indicating the cooperative effect of LamA and LamR.
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O-Glycosylation as a Novel Control Mechanism of Peptidoglycan Hydrolase Activity

TL;DR: This work presents the first functional evidence that glycosylation controls the activity of a bacterial enzyme, and proposes a model in which access of the Acm2 catalytic domain to its substrate may be hindered by the AST domain where O-glycosylated changes its conformation and/or mediates interdomain interactions.