Solubilization and partial properties of receptor substance for bacteriophage alpha 2 induced from Clostridium botulinum type A 190L.
Bacteriophage alpha 2, one of the two inducible phages from Clostridium botulinum type A 190L, had a latent period of 55 min and an average burst size of 75 in C. botulinum type A Hall used as the host bacterium. The phage particles were adsorbed on the cell walls extracted with hot trichloroacetic acid (TCA-walls). The receptor substance for the phage was solubilized from the TCA-walls with Achromopeptidase and fractionated by gel filtration on Sephadex G-150. The fraction having the highest level of receptor activity for the phage contained large amounts of muramic acid and glucosamine. Both authentic muramic acid and glucosamine significantly inactivated the phage, whereas glucose, galactose, L-and D-alanine, diaminopimeric acid, or D-glutamic acid did not exhibit similar activity. There results strongly suggest that the receptor site for phage alpha 2 is closely associated with glycan moieties of the cell wall peptidoglycan.
D001435:Bacteriophages / Q000032:analysis* / Q000302:isolation & purification / Q000648:ultrastructure; D002473:Cell Wall / Q000032:analysis*; D002850:Chromatography, Gel; D003014:Clostridium botulinum / Q000032:analysis*; D010450:Endopeptidases; D005944:Glucosamine / Q000032:analysis; D008854:Microscopy, Electron; D009112:Muramic Acids / Q000032:analysis; D011991:Receptors, Virus / Q000032:analysis*; D012697:Serine Endopeptidases; D014238:Trichloroacetic Acid
D009112:Muramic Acids; D011991:Receptors, Virus; D014238:Trichloroacetic Acid; D010450:Endopeptidases; D012697:Serine Endopeptidases; C036813:lysyl endopeptidase; D005944:Glucosamine