Influence of lectins, hexoses, and neuraminidase on the association of purified elementary bodies of Chlamydia trachomatis UW-31 with HeLa cells
Influence of lectins, hexoses, and neuraminidase on the association of purified elementary bodies of Chlamydia trachomatis UW-31 with HeLa cells
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凝集素、己糖和神经氨酸酶对沙眼衣原体 UW-31 纯化原体与 HeLa 细胞结合的影响
作者：
S. Bose;G. B. Smith;R. Paul
利用高纯度的沙眼衣原体UW-31(K型)的基本体，我们发现HeLa 229单层培养物在用凝集素麦胚凝集素处理后结合更多的32P标记的衣原体。另一方面，当在聚阳离子存在的情况下检测衣原体结合时，凝集素竞争性地抑制。用N-乙酰神经氨酸(NeuNAc)或N-乙酰氨基葡萄糖(GlcNAc)预先孵育的小麦胚凝集素可消除麦胚凝集素的这两种作用。HeLa细胞短暂暴露于神经氨酸酶后，无论是否存在多聚阳离子，其结合基本体的能力都会消失。此外，在5℃而不是37℃，NeuNAc、GlcNAc和N-乙酰半乳糖胺仅在没有聚阳离子DEAE-葡聚糖的情况下抑制衣原体结合。结果表明，质膜上的NeuNAc残基是沙眼衣原体的主要受体，但不是唯一的受体。
Using highly purified elementary bodies of Chlamydia trachomatis UW-31 (serotype K), we found that HeLa 229 monolayer cultures bound more 32P-labeled chlamydiae after pretreatment with the lectin wheat germ agglutinin. The lectin, on the other hand, inhibited competitively when chlamydial association was assayed in the presence of polycations. The two effects of wheat germ agglutinin were abolished when N-acetylneuraminic acid (NeuNAc)- or N-acetylglucosamine (GlcNAc)-preincubated wheat germ agglutinin was used. Brief exposure of HeLa cells to neuraminidase abolished the ability to bind the elementary bodies, whether or not polycations were present. Furthermore, at 5 degrees C but not at 37 degrees C, NeuNAc, GlcNAc and N-acetylgalactosamine inhibited chlamydial association only in the absence of the polycation DEAE-dextran. The results suggest that NeuNAc residues on the plasma membrane are the principal, but not the only, receptors for this strain of C. trachomatis.
影响因子：
6.4
作者：
BEACHEY, EH
通讯作者：
BEACHEY, EH