Interaction of wheat-germ agglutinin with bacterial cells and cell-wall polymers.
Interaction of wheat-germ agglutinin with bacterial cells and cell-wall polymers.
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小麦胚芽凝集素与细菌细胞和细胞壁聚合物的相互作用。
DOI：
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发表时间：
1975
期刊：
影响因子：
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通讯作者：
D. Mirelman
中科院分区：
文献类型：
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作者：
R. Lotan;N. Sharon;D. Mirelman
发现小麦胚芽凝集素可凝集大肠杆菌 PAT 84、藤黄微球菌、金黄色葡萄球菌 H 和金黄色葡萄球菌 52A5 的细胞，但不凝集金黄色葡萄球菌 52A2 的细胞。麦芽凝集素与藤黄微球菌分泌的可溶性线性肽聚糖以及金黄色葡萄球菌 H 的磷壁酸的相互作用通过琼脂凝胶扩散、定量沉淀和对胰蛋白酶处理的兔红细胞血凝的抑制来证明。无法证明磷壁酸与来自缺乏 A-乙酰基-D-葡萄糖胺残基的噬菌体抗性突变体（金黄色葡萄球菌 52A2）的磷壁酸有相互作用。所有相互作用均被低浓度的壳三糖（GlcNAcbeta1 导致 4GlcNAcbeta1 导致 4GlcNAc）和细菌细胞壁四糖（GlcNAcbeta1 导致 4MurNAcbeta1 导致 4GlcNAcbeta1 导致 4MurNAc）特异性抑制。血凝抑制实验表明，金黄色葡萄球菌 H 的线性肽聚糖和磷壁酸对麦芽凝集素的抑制作用比 N-乙酰基-D-葡萄糖胺强数千倍。比较不同糖类通过麦芽凝集素抑制血凝和聚合物沉淀的效率，强烈表明次级非特异性相互作用有助于凝集素与聚合物的结合。
Wheat germ agglutinin was found to agglutinate cells of Escherichia coli PAT 84, Micrococcus luteus, Staphylococcus aureus H, and of S. aureus 52A5, but not cells of S. aureus 52A2. Interaction of wheat germ agglutinin with a soluble linear peptidoglycan secreted by Micrococcus luteus and with the teichoic acid of S. aureus H was demonstrated by agar gel diffusion, quantitative precipitation and inhibition of hemagglutination of trypsinized rabbit erythrocytes. No interaction could be demonstrated with the teichoic acid from a phage-resistant mutant (S. aureus 52A2) which lacks A-acetyl-D-glucosamine residues. All interactions were specifically inhibited by low concentrations of chitotriose (GlcNAcbeta1 leads to 4GlcNAcbeta1 leads to 4GlcNAc) and the bacterial cell wall tetrasaccharide, GlcNAcbeta1 leads to 4MurNAcbeta1 leads to 4GlcNAcbeta1 leads to 4MurNAc. Hemagglutination-inhibition experiments showed that the linear peptidoglycan and the teichoic acid of S. aureus H were several thousand times more potent inhibitors of wheat germ agglutinin than was N-acetyl-D-glucosamine. Comparison of the efficiency of different saccharides in inhibition of hemagglutination and precipitation of polymers by wheat germ agglutinin, strongly suggests that secondary, non-specific interactions contribute to the binding of the lectin to the polymers.