Abstract
Hydrolysis of the cell wall of Bacillus subtilis 168 by autolysins or lysozyme resulted in the exposure of glucosylated teichoic acid molecules as evidenced by increased precipitation of [14C] concanavalin A. The number of concanavalin A-reactive sites increased significantly after only limited enzymatic digestion of the walls. Quantitative analyses of [14C] concanavalin A-treated wall or wall hydrolysate complexes indicate that approximately one-half of the teichoic acid molecules are surface-exposed, whereas the remainder are probably embedded within the peptidoglycan matrix. Treatment of the cell walls with sodium dodecyl sulfate or Triton X-100 did not result in new concanavalin A-reactive sites. Partial autolysis diminished the ability of the cell walls to adsorb bacteriophage phi25. Fluorescein-labeled concanavalin A bound intensely over the entire surface of growing B. subtilis 168 cells, suggesting that teichoic acid molecules are located on the total solvent-exposed surface area of the bacteria.
MeSH Terms
Adsorption
Bacillus subtilis/ultrastructure
Binding Sites
Cell Fractionation
Cell Wall/metabolism,microbiology,ultrastructure
Chemical Precipitation
Coliphages
Concanavalin A/metabolism
DNA Viruses
Enzymes/metabolism
Fluoresceins
Hydrolysis
Microscopy, Fluorescence
Muramidase/metabolism
Polyethylene Glycols/pharmacology
Sodium Dodecyl Sulfate/pharmacology
Teichoic Acids/isolation & purification,metabolism
Chemicals
Enzymes
Fluoresceins
Teichoic Acids
Concanavalin A
Sodium Dodecyl Sulfate
Polyethylene Glycols
Muramidase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Doyle R J
McDannel M L
Helman J R
Streips U N
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24 references, click to expand
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