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Applied and Environmental Microbiology, October 2003, p. 5802-5811, Vol. 69, No. 10
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.10.5802-5811.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10

Irena Pastar,1 Ivana Tonic,1 Natasa Golic,1 Milan Kojic,1 Richard van Kranenburg,2,3,{dagger} Michiel Kleerebezem,2,3 Ljubisa Topisirovic,1 and Goran Jovanovic1*

Institute of Molecular Genetics and Genetic Engineering, 11001 Belgrade, Serbia and Montenegro,1 Wageningen Centre for Food Sciences, 6700 AN Wageningen,2 NIZO Food Research, 6710 BA Ede, The Netherlands3

Received 2 April 2003/ Accepted 14 July 2003

A novel proteinase, PrtR, produced by the human vaginal isolate Lactobacillus rhamnosus strain BGT10 was identified and genetically characterized. The prtR gene and flanking regions were cloned and sequenced. The deduced amino acid sequence of PrtR shares characteristics that are common for other cell envelope proteinases (CEPs) characterized to date, but in contrast to the other cell surface subtilisin-like serine proteinases, it has a smaller and somewhat different B domain and lacks the helix domain, and the anchor domain has a rare sorting signal sequence. Furthermore, PrtR lacks the insert domain, which otherwise is situated inside the catalytic serine protease domain of all CEPs, and has a different cell wall spacer (W) domain similar to that of the cell surface antigen I and II polypeptides expressed by oral and vaginal streptococci. Moreover, the PrtR W domain exhibits significant sequence homology to the consensus sequence that has been shown to be the hallmark of human intestinal mucin protein. According to its {alpha}S1- and ß-casein cleavage efficacy, PrtR is an efficient proteinase at pH 6.5 and is distributed throughout all L. rhamnosus strains tested. Proteinase extracts of the BGT10 strain obtained with Ca2+-free buffer at pH 6.5 were proteolytically active. The prtR promoter-like sequence was determined, and the minimal promoter region was defined by use of prtR-gusA operon fusions. The prtR expression is Casitone dependent, emphasizing that nitrogen depletion elevates its transcription. This is in correlation with the catalytic activity of the PrtR proteinase.

* Corresponding author. Mailing address: Institute of Molecular Genetics and Genetic Engineering, Vojvode Stepe 444A, P.O. Box 446, 11001 Belgrade, Serbia and Montenegro. Phone: 381 11 397-5960. Fax: 381 11 397-5808. E-mail: LAB6{at}eunet.yu.

{dagger} Present address: Purac Biochem, Gorinchem, The Netherlands.

Applied and Environmental Microbiology, October 2003, p. 5802-5811, Vol. 69, No. 10
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.10.5802-5811.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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