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Applied and Environmental Microbiology, October 2004, p. 5825-5832, Vol. 70, No. 10
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.10.5825-5832.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Identification of Lactococcus lactis Genes Required for Bacteriophage Adsorption

Kitt Dupont,1,2 Thomas Janzen,3 Finn Kvist Vogensen,1,2 Jytte Josephsen,1,2 and Birgitte Stuer-Lauridsen3*

Department of Food Science,1 Centre for Advanced Food Studies, The Royal Veterinary and Agricultural University, Frederiksberg,2 Applied Biotechnology, Chr. Hansen A/S, Hørsholm, Denmark3

Received 28 February 2004/ Accepted 18 June 2004

The aim of this work was to identify genes in Lactococcus lactis subsp. lactis IL1403 and Lactococcus lactis subsp. cremoris Wg2 important for adsorption of the 936-species phages bIL170 and {phi}645, respectively. Random insertional mutagenesis of the two L. lactis strains was carried out with the vector pGh9:ISS1, and integrants that were resistant to phage infection and showed reduced phage adsorption were selected. In L. lactis IL1403 integration was obtained in the ycaG and rgpE genes, whereas in L. lactis Wg2 integration was obtained in two genes homologous to ycbC and ycbB of L. lactis IL1403. rgpE and ycbB encode putative glycosyltransferases, whereas ycaG and ycbC encode putative membrane-spanning proteins with unknown functions. Interestingly, ycaG, rgpE, ycbC, and ycbB are all part of the same operon in L. lactis IL1403. This operon is probably involved in biosynthesis and transport of cell wall polysaccharides (WPS). Binding and infection studies showed that {phi}645 binds to and infects L. lactis Wg2, L. lactis IL1403, and L. lactis IL1403 strains with pGh9:ISS1 integration in ycaG and rgpE, whereas bIL170 binds to and infects only L. lactis IL1403 and cannot infect Wg2. These results indicate that {phi}645 binds to a WPS structure present in both L. lactis IL1403 and L. lactis Wg2, whereas bIL170 binds to another WPS structure not present in L. lactis Wg2. Binding of bIL170 and {phi}645 to different WPS structures was supported by alignment of the receptor-binding proteins of bIL170 and {phi}645 that showed no homology in the C-terminal part.

* Corresponding author. Mailing address: Applied Biotechnology, Chr. Hansen A/S, Bøge Allé 10-12, DK-2970 Hørsholm, Denmark. Phone: 45 45 74 84 08. Fax: 45 45 74 89 94. E-mail: Birgitte.Stuer-Lauridsen{at}dk.chr-hansen.com.

Applied and Environmental Microbiology, October 2004, p. 5825-5832, Vol. 70, No. 10
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.10.5825-5832.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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Copyright © 2004 by the American Society for Microbiology. All rights reserved.