Bacteriophage receptors of Lactococcus lactis subsp. 'diacetylactis' F7/2 and Lactococcus lactis subsp. cremoris Wg2-1.
Bacteriophage P008 revealed irreversible and uniform adsorption to cell walls of L. lactis subsp. 'diacetylactis' F7/2, whereas phage P127 adsorbed reversibly to a limited number of receptor sites on cell walls of L. lactis subsp. cremoris Wg2-1. Neither extraction of lipids, cell wall- and membrane-teichoic acids nor enzymatic degradation of proteins altered the binding efficiencies of both cell wall fractions. However, phage binding was inhibited, when cell walls were subjected to lysozyme, metaperiodate, or acid treatments. This reflects that a carbohydrate component embedded in the peptidoglycan matrix is part of the phage receptors of strains F7/2 and Wg2-1.
Schäfer
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A
Institute of Microbiology, Federal Dairy Research Center, Kiel, F.R.G.
Geis
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A
Neve
H
H
Teuber
M
M
D000327:Adsorption; D000372:Agglutination Tests; D001435:Bacteriophages / Q000648:ultrastructure; D002473:Cell Wall; D002855:Chromatography, Thin Layer; D013294:Lactococcus lactis / Q000032:analysis* / Q000648:ultrastructure; D037102:Lectins; D011991:Receptors, Virus / Q000032:analysis*; D012995:Solubility
D037102:Lectins; D011991:Receptors, Virus