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J. Bacteriol. doi:10.1128/JB.00078-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Molecular Interaction between LTAs and L. delbrueckii Phages Depends on d-Alanyl and -Glucose Substitution of Poly(glycerophosphate) Backbones

Department of Biology, University of Oulu, P.O. Box 3000, FIN-90014 Oulu, Finland; Department of Biochemical Pharmacology, University of Konstanz, D-78457 Konstanz, Germany; Institute for Organic Chemistry, Philipps-Universität Marburg, D-35043 Marburg, Germany; Department Biologie I, Bereich Mikrobiologie der Universität München, D-80638 Munich, Germany; Biotechnology Laboratory, REDEC of Kajaani, University of Oulu, FIN-88600 Sotkamo, Finland; European Centre for the Validation of Alternative Methods, IHCP, JRC, 21020 Ispra, Italy; Department of Food Technology, University of Helsinki, P.O. Box 66, FIN-00014 Helsinki, Finland

^* To whom correspondence should be addressed. Email: liisa.raisanen{at}oulu.fi.

	Abstract

Lipoteichoic acids (LTAs) have been shown to act as bacterial counterparts to the receptor binding proteins of LL-H, LL-H host range mutant LL-H-a21 and JCL1032. Here we have used HIC-purified LTAs from different phage resistant and sensitive strains of L. delbrueckii subsp. lactis. NMR analyses revealed variation in the degree of -glucosyl and D-alanyl substitution of the 1,3-linked poly(glycerophosphate) LTAs between the phage sensitive and the phage resistant strains. Inactivation of phages was less effective if there was a high level of D-alanine residues in the LTA backbones. Prior incubation of the LTAs with -glucose-specific lectin inhibited the LL-H phage inactivation. The overall level of decoration or the specific spatial combination of -glucosyl substituted, D-alanyl substituted and nonsubstituted glycerol residues may also affect phage adsorption.

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