Characterization of receptor sites for bacteriophages PL-1,J-1 and MLC-A using two strains of Lactobacillus casei.

CAPRA MARÍA LUJÁN; QUIBERONI ANDREA DEL LUJAN; REINHEIMER JORGE ALBERTO

Contemporary trends in bacteriophage research

Nova Science Publishers

Lugar: New York; Año: 2009; p. 391 - 406

Receptor sites and adsorption process of two collection phages and the first Argentinean indigenous Lactobacillus paracasei bacteriophage (MLC-A), on purified cell walls were characterized. To identify the nature of receptors, thermal, enzymatic and chemical treatments were performed on L. casei purified cell walls. Differences found between adsorption onwhole or fragments of cells indicated that cell wall fragments were efficient for phage adsorption, but its receptors were not as complete as in whole cell. Adsorption of phages was not influenced by sodium dodecyl sulphate and proteinase K treatments, but decreased when cell walls were previously incubated with mutanolysin or trichloroacetic acid, suggesting that receptors were carbohydrates in nature. L-rhamnose was implicated as a receptor component for the collection phages on L. casei ATCC 393 and also as a major component for phage MLC-A on L. casei ATCC 27139. In the latter case, L-ribose seemed to play an important role in adsorption process. This study suggested possible existence of an equilibrium state between phage adsorption to and its release from cell walls, questioning the integrity of receptor sites on cell walls.