Molecular interaction between lipoteichoic acids and Lactobacillus delbrueckii phages depends on D-alanyl and alpha-glucose substitution of poly(glycerophosphate) backbones.
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 LTAs purified by hydrophobic interaction chromatography from different phage-resistant and -sensitive strains of Lactobacillus delbrueckii subsp. lactis. Nuclear magnetic resonance analyses revealed variation in the degree of alpha-glucosyl and D-alanyl substitution of the 1,3-linked poly(glycerophosphate) LTAs between the phage-sensitive and 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 alpha-glucose-specific lectin inhibited the LL-H phage inactivation. The overall level of decoration or the specific spatial combination of alpha-glucosyl-substituted, D-alanyl-substituted, and nonsubstituted glycerol residues may also affect phage adsorption.
Räisänen
Liisa
L
Department of Biology, University of Oulu, P.O. Box 3000, FIN-90014 Oulu, Finland. liisa.raisanen@oulu.fi
Draing
Christian
C
Pfitzenmaier
Markus
M
Schubert
Karin
K
Jaakonsaari
Tiina
T
von Aulock
Sonja
S
Hartung
Thomas
T
Alatossava
Tapani
T
D001435:Bacteriophages / Q000145:classification / Q000187:drug effects* / Q000254:growth & development / Q000378:metabolism; D005994:Glycerophosphates / Q000737:chemistry / Q000378:metabolism*; D048668:Lactobacillus delbrueckii / Q000821:virology*; D008070:Lipopolysaccharides / Q000737:chemistry / Q000494:pharmacology*; D009682:Magnetic Resonance Spectroscopy; D013682:Teichoic Acids / Q000737:chemistry / Q000494:pharmacology*; D038301:Virus Inactivation / Q000187:drug effects
D005994:Glycerophosphates; D008070:Lipopolysaccharides; D013682:Teichoic Acids; C009900:lipoteichoic acid