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,
| Name | Country | City | Type |
|---|
This document is only visible at the Commission level.
You are not authorized to publish or distribute it outside the European Commission.
This is a public document. You can share this publication.
Datasets
| ID | Title | Public URL |
|---|
Dataset collections
| ID | Acronym | Title | Public URL |
|---|
Scripts / source codes
| Description | Public URL |
|---|
Additional supporting files
| File name | Description | File type |
|---|