Speziale P, Raucci G, Visai L, Switalski L M, Timpl R, Höök M
J Bacteriol. 1986 Jul;167(1):77-81. doi: 10.1128/jb.167.1.77-81.1986.
Collagen binds to a receptor protein present on the surfaces of Staphylococcus aureus cells. Binding of 125I-labeled type II collagen to its bacterial receptor is reversible, and Scatchard plot analysis indicates the presence of one class of receptor that occurs on an average of 3 X 10(4) copies per cell and binds type II collagen with a Kd of 10(-7) M. Studies on the specificity of collagen cell binding indicate that the receptor does not recognize noncollagenous proteins but binds all of the different collagen types tested (types I to VI). Furthermore, isolated collagen alpha chains and peptides generated by cyanogen bromide cleavage of type I collagen alpha chains are recognized by the receptor as indicated by the ability of these polypeptides to inhibit binding of 125I-labeled type II collagen to staphylococcal cells. Synthetic collagen analogs were tested as inhibitors of type II collagen binding to bacterial cells. The peptides (Pro-Gly-Pro)n, (Pro-Pro-Gly)10, and (Pro-OH-Pro-Gly)10 were recognized by the receptor, whereas the peptides (Pro-Ala-Gly)n and polyproline showed no inhibitory activity.
胶原蛋白与金黄色葡萄球菌细胞表面存在的一种受体蛋白结合。125I标记的II型胶原蛋白与其细菌受体的结合是可逆的,Scatchard图分析表明存在一类受体,平均每个细胞有3×10⁴个拷贝,与II型胶原蛋白结合的解离常数为10⁻⁷M。对胶原蛋白细胞结合特异性的研究表明,该受体不识别非胶原蛋白,但能结合所有测试的不同类型胶原蛋白(I至VI型)。此外,如这些多肽抑制125I标记的II型胶原蛋白与葡萄球菌细胞结合的能力所示,分离的胶原蛋白α链和由I型胶原蛋白α链经溴化氰裂解产生的肽被该受体识别。测试了合成胶原蛋白类似物作为II型胶原蛋白与细菌细胞结合的抑制剂。肽(Pro-Gly-Pro)n、(Pro-Pro-Gly)10和(Pro-OH-Pro-Gly)10被该受体识别,而肽(Pro-Ala-Gly)n和聚脯氨酸则无抑制活性。