Doyle R J, McDannel M L, Helman J R, Streips U N
J Bacteriol. 1975 Apr;122(1):152-8. doi: 10.1128/jb.122.1.152-158.1975.
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.
自溶素或溶菌酶对枯草芽孢杆菌168细胞壁的水解导致糖基化磷壁酸分子的暴露，这可通过[14C]伴刀豆球蛋白A沉淀增加得到证明。在对细胞壁进行有限的酶消化后，伴刀豆球蛋白A反应位点的数量显著增加。对[14C]伴刀豆球蛋白A处理的细胞壁或细胞壁水解产物复合物的定量分析表明，大约一半的磷壁酸分子暴露于表面，而其余的可能嵌入肽聚糖基质中。用十二烷基硫酸钠或 Triton X-100处理细胞壁不会产生新的伴刀豆球蛋白A反应位点。部分自溶降低了细胞壁吸附噬菌体phi25的能力。荧光素标记的伴刀豆球蛋白A在生长中的枯草芽孢杆菌168细胞的整个表面强烈结合，这表明磷壁酸分子位于细菌的整个溶剂暴露表面积上。
