K
Kees Leenhouts
Researcher at University of Groningen
Publications - 55
Citations - 4198
Kees Leenhouts is an academic researcher from University of Groningen. The author has contributed to research in topics: Lactococcus lactis & Vaccination. The author has an hindex of 33, co-authored 54 publications receiving 3993 citations.
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Journal ArticleDOI
A system to generate chromosomal mutations in Lactococcus lactis which allows fast analysis of targeted genes.
TL;DR: A system for generating chromosomal insertions in lactococci based on the conditional replication of lactococcal pWV01-derived Ori+ RepA- vector pORI19, containing lacZ alpha and the multiple cloning site of pUC19 is described.
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A chloride-inducible acid resistance mechanism in Lactococcus lactis and its regulation
TL;DR: The nucleotide sequence and functional analysis of two genes transcribed from this promoter, gadC and gadB, suggest that these genes encode a glutamate‐dependent acid resistance mechanism of L. lactis that is optimally active under conditions in which it is needed to maintain viability.
Journal ArticleDOI
Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation.
Girbe Buist,Jan Kok,Kees Leenhouts,Magdalena Dabrowska,Gerhardus Venema,Alfred J. Haandrikman +5 more
TL;DR: A gene of Lactococcus lactis subsp.
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Cell Wall Attachment of a Widely Distributed Peptidoglycan Binding Domain Is Hindered by Cell Wall Constituents
Anton Steen,Girbe Buist,Kees Leenhouts,Mohamed El Khattabi,Froukje Grijpstra,Aldert Zomer,Gerard Venema,Oscar P. Kuipers,Jan Kok +8 more
TL;DR: It is proposed that LysM-type repeats bind to peptidoglycan and that binding is hindered by other cell wall constituents, resulting in localized binding of AcmA, and Lipoteichoic acid is a candidate hindering component.
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Nucleotide sequence of the cell wall proteinase gene of Streptococcus cremoris Wg2.
TL;DR: A 6.5-kilobase HindIII fragment that specifies the proteolytic activity of Streptococcus cremoris Wg2 was sequenced entirely and contained regions of extensive homology with serine proteases of the subtilisin family.