Zhang J P, Stephens R S
Department of Biomedical and Environmental Health Sciences, University of California, Berkeley 94720.
Cell. 1992 May 29;69(5):861-9. doi: 10.1016/0092-8674(92)90296-o.
A novel trimolecular mechanism of microbial attachment to mammalian host cells was characterized for the obligate intracellular pathogen Chlamydia trachomatis. Using purified glycosaminoglycans (GAGs) and specific GAG lyases, we demonstrated that a heparan sulfate-like GAG present on the surface of chlamydia organisms is required for attachment to host cells. These observations were supported by inhibition of attachment following binding of heparan sulfate receptor analogs to chlamydiae and by demonstrating that chlamydiae synthesize a unique heparan sulfate-like GAG. Furthermore, exogenous heparan sulfate, as an adhesin analog, restored attachment and infectivity to organisms that had lost these attributes following treatment with heparan sulfate lyase. These data suggest that a GAG adhesin ligand mediates attachment by bridging mutual GAG receptors on the host cell surface and on the chlamydial outer membrane surface.
针对专性胞内病原体沙眼衣原体，我们鉴定了一种新型的微生物附着于哺乳动物宿主细胞的三分子机制。通过使用纯化的糖胺聚糖（GAGs）和特定的GAG裂解酶，我们证明沙眼衣原体表面存在的一种硫酸乙酰肝素样GAG是附着于宿主细胞所必需的。硫酸乙酰肝素受体类似物与衣原体结合后对附着的抑制作用，以及证明衣原体合成独特的硫酸乙酰肝素样GAG，均支持了这些观察结果。此外，作为黏附素类似物的外源性硫酸乙酰肝素，恢复了经硫酸乙酰肝素裂解酶处理后丧失这些特性的生物体的附着和感染性。这些数据表明，一种GAG黏附素配体通过桥接宿主细胞表面和衣原体外膜表面的共同GAG受体来介导附着。
