Molecular Interaction between LTAs and L. delbrueckii Phages Depends on D4 Alanyl and alfa-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 HIC-purified LTAs from different phage resistant and sensitive strains of L. delbrueckii subsp. lactis. NMR analyses revealed variation in the degree of α-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 α-glucose-specific lectin inhibited the LL-H phage inactivation. The overall level of decoration or the specific spatial combination of α-glucosyl substituted, D-alanyl substituted and nonsubstituted glycerol residues may also affect phage adsorption.
RÄISÄNEN Liisa;
DRAING C.;
PFITZENMAIER Markus;
SCHUBERT Karin;
JAAKONSAARI Tiina;
VON AULOCK Sonja;
HARTUNG Thomas;
ALATOSSAVA Tapani;
2007-10-10
AMER SOC MICROBIOLOGY
JRC38179
0021-9193,
https://publications.jrc.ec.europa.eu/repository/handle/JRC38179,
10.1128/JB.00078-07,
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