Surface parasitism by Mycoplasma pneumoniae of respiratory epithelium.
Surface parasitism by Mycoplasma pneumoniae of respiratory epithelium.
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DOI：
10.1084/jem.145.5.1328
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发表时间：
1977-05-01
影响因子：
15.3
通讯作者：
Baseman, J B
中科院分区：
文献类型：
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作者：
Hu, P C;Collier, A M;Baseman, J B
试图鉴定允许呼吸道上皮表面寄生的强毒肺炎支原体微生物上的附着因子。对M.具有蛋白酶的肺炎支原体单层防止支原体附着于敏感宿主细胞而不降低微生物的活力。完整支原体暴露于蛋白酶之前和之后的支原体蛋白的凝胶电泳分析显示，在酶处理的制剂中没有一个主要的蛋白质种类（P1），而除P2外的其他蛋白质条带几乎不受影响。P1的缺失与酶处理的支原体未能附着在气管外植体上相关。支原体单层蛋白酶处理后的P1再生与支原体的再附着能力直接相关。肺炎。红霉素抑制P1再合成，从而防止支原体恢复附着活性。乳过氧化物酶催化的完整M. pneumoniae生物体进一步证实了P1是一种外膜蛋白，并表明其表面组分是宿主和寄生虫之间成功的膜-膜相互作用所必需的。
Identification of the attachment factor on virulent Mycoplasma pneumoniae organisms which permits surface parasitism of respiratory epithelium was attempted. Brief pretreatment of M. pneumoniae monolayers with protease prevented mycoplasma attachment ot sensitive host cells without reducing viability of the microorganisms. Gel electrophoretic analysis of mycoplasma proteins before and after exposure of intact mycoplasmas to protease revealed the absence of a major protein species (P1) in enzyme-treated preparations while other protein bands with the exception of P2 were virtually unaffected. The absence of P1 correlated with the failure of enzyme-treated mycoplasmas to attach to tracheal explants. P1 regeneration after protease treatment of mycoplasma monolayers was directly associated with reattachment capabilities in M. pneumoniae. Erythromycin inhibited P1 resynthesis, thus preventing resumed attachment activity by mycoplasmas. Lactoperoxidase-catalyzed iodination of intact M. pneumoniae organisms further confirmed that P1 was an external membrane protein and suggested that his surface component was required for the successful membrane-membrane interaction between host and parasite.