ADHERENCE OF MYCOPLASMA-GALLISEPTICUM TO HUMAN ERYTHROCYTES
ADHERENCE OF MYCOPLASMA-GALLISEPTICUM TO HUMAN ERYTHROCYTES
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DOI：
10.1128/iai.21.2.365-372.1978
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发表时间：
1978-01-01
影响因子：
3.1
通讯作者：
BREDT, W
中科院分区：
文献类型：
--
作者：
BANAI, M;KAHANE, I;BREDT, W
致病性支原体粘附并定殖于受感染动物的呼吸道和生殖道的上皮内层。建立了一套适用于支原体粘附定量研究的实验系统。该系统由人红细胞（RBC）和禽病原体鸡毒支原体组成，其中膜脂质被标记。根据放射性测量确定的附着于RBC的支原体细胞的量随着附着混合物的pH或离子强度的增加而减少。附着遵循一级动力学，并依赖于温度。暴露于RBC后保留在上清液中的支原体细胞群在第二次附着试验期间显示出更差的附着RBC的能力，表明给定群体内细胞之间的结合位点分布不均匀。通过神经氨酸酶从RBC中逐渐去除唾液酸残基，伴随着支原体附着的减少。分离的血型糖蛋白，红细胞膜糖蛋白携带几乎所有的红细胞唾液酸部分，抑制M。鸡败血症附着;去唾液酸血型糖蛋白和唾液酸本身是非常差的附着抑制剂。只有一部分的125 I标记的血型糖蛋白结合支原体可以通过神经氨酸酶或通过交换未标记的血型糖蛋白。血型糖蛋白，代表M.鸡毒支原体可通过其唾液酸部分特异性结合支原体，并且通过其暴露的疏水多肽部分非特异性结合支原体。
Pathogenic mycoplasmas adhere to and colonize the epithelial lining of the respiratory and genital tracts of infected animals. An experimental system suitable for the quantitative study of mycoplasma adherence was developed. The system consists of human erythrocytes (RBC) and the avian pathogen Mycoplasma gallisepticum, in which membrane lipids were labeled. The amount of mycoplasma cells attached to the RBC, which was determined according to radioactivity measurements, decreased on increasing the pH or ionic strength of the attachment mixture. Attachment followed 1st-order kinetics and depended on temperature. The mycoplasma cell population remaining in the supernatant fluid after exposure to RBC showed a much poorer ability to attach to RBC during a 2nd attachment test, indicating an unequal distribution of binding sites among cells within a given population. The gradual removal of sialic acid residues from the RBC by neuraminidase was accompanied by a decrease in mycoplasma attachment. Isolated glycophorin, the RBC membrane glycoprotein carrying almost all the sialic acid moieties of the RBC, inhibited M. gallisepticum attachment; asialoglycophorin and sialic acid itself were very poor inhibitors of attachment. Only part of the 125I-labeled glycophorin bound to mycoplasmas could be removed by neuraminidase or by exchange with unlabeled glycophorin. Glycophorin, representing the isolated major RBC receptor for M. gallisepticum, may bind to the mycoplasmas specifically, through its sialic acid moieties, and nonspecifically, through its exposed hydrophobic polypeptide moiety.