Stephens R S, Koshiyama K, Lewis E, Kubo A
Division of Infectious Diseases, School of Public Health, 235 Earl Warren Hall, University of California, Berkeley, CA 94720, USA.
Mol Microbiol. 2001 May;40(3):691-9. doi: 10.1046/j.1365-2958.2001.02418.x.
As an intracellular pathogen, the mechanism by which Chlamydia invade eukaryotic cells represents a cornerstone to understanding chlamydial biology. The ability of chlamydiae specifically to bind heparan sulphate or heparin and the association of this ability to bind and enter mammalian host cells was approached by searching experimentally for chlamydial outer membrane proteins that bind heparin. The 60 000 molecular weight cysteine-rich outer membrane complex protein, OmcB, bound heparin. The ability of OmcB to bind heparin was supported by mapping the region of the protein with heparin-binding capacity and demonstrating that an OmcB synthetic 20-mer peptide from this region specifically bound heparin. Surface localization of OmcB was shown using monospecific antisera specific to the 20-mer OmcB peptide that bound the surfaces of elementary bodies (EB) and by heparin-binding peptide cross-linking of EB surface proteins.
作为一种细胞内病原体，衣原体侵入真核细胞的机制是理解衣原体生物学的基石。通过实验寻找与肝素结合的衣原体外膜蛋白，探讨了衣原体特异性结合硫酸乙酰肝素或肝素的能力以及这种结合和进入哺乳动物宿主细胞的能力之间的关联。分子量为60000的富含半胱氨酸的外膜复合蛋白OmcB与肝素结合。通过绘制具有肝素结合能力的蛋白质区域，并证明来自该区域的OmcB合成20聚体肽特异性结合肝素，支持了OmcB结合肝素的能力。使用针对结合原体（EB）表面的20聚体OmcB肽的单特异性抗血清以及通过EB表面蛋白的肝素结合肽交联，显示了OmcB的表面定位。
