Buxton T B, Rissing J P, Horner J A, Plowman K M, Scott D F, Sprinkle T J, Best G K
Veterans Administration Medical Center, Augusta, GA 30910.
Microb Pathog. 1990 Jun;8(6):441-8. doi: 10.1016/0882-4010(90)90031-k.
We contrasted the collagen-binding potential of the experimental osteomyelitis pathogen, Staphylococcus aureus strain SMH, to several other strains. These included Cowan 1 (binder), Wood 46 (non-binder) and six capsular variants. These measurements were made using an 125I-collagen binding assay. Formalin-killed S. aureus SMH strongly bound commercial type I iodinated collagen (dissociation constant, Kd = 2 x 10(-9) M). The extent of binding was similar to Cowan 1. Binding was saturable and not inhibited by 100 mM solutions of D-glucose, D-galactose, D-mannose, methyl-alpha-L-fucopyranoside, L-hydroxyproline or L-glycine. D-lactose gave moderate inhibition of binding to collagen, and L-fucose was strongly inhibitory. Trypsinized SMH did not bind collagen. None of four Ruthenium-red-staining staphylococci (encapsulated) avidly bound type I collagen. The encapsulated Smith strain, for example, did not bind to collagen but its capsule-negative variant, Smith compact, showed extensive binding. Three of five non-encapsulated S. aureus were strong collagen binders. These data suggest that the prototype bone pathogen binds to the major protein component of bone's extracellular matrix. Collagen-binding is promoted by protein adhesin(s), not capsule. The latter, in fact, appeared to interfere with this interaction. Binding was inhibited by solutions containing the simple monosaccharide, L-fucose.
我们将实验性骨髓炎病原体金黄色葡萄球菌菌株SMH与其他几种菌株的胶原结合潜力进行了对比。这些菌株包括考恩1株（结合菌）、伍德46株（非结合菌）以及六个荚膜变种。这些测量是使用125I - 胶原结合试验进行的。经福尔马林灭活的金黄色葡萄球菌SMH能强烈结合商业用I型碘化胶原（解离常数，Kd = 2×10(-9) M）。结合程度与考恩1株相似。结合具有饱和性，且不受100 mM的D - 葡萄糖、D - 半乳糖、D - 甘露糖、甲基 - α - L - 岩藻糖苷、L - 羟脯氨酸或L - 甘氨酸溶液的抑制。D - 乳糖对与胶原的结合有中等程度的抑制作用，而L - 岩藻糖具有强烈的抑制作用。经胰蛋白酶处理的SMH不与胶原结合。四种经钌红染色的葡萄球菌（有荚膜）均未强烈结合I型胶原。例如，有荚膜的史密斯菌株不与胶原结合，但其无荚膜变种史密斯紧密型却表现出广泛的结合。五株无荚膜的金黄色葡萄球菌中有三株是强胶原结合菌。这些数据表明，这种典型的骨病原体与骨细胞外基质的主要蛋白质成分结合。胶原结合是由蛋白质黏附素促进的，而非荚膜。事实上，后者似乎会干扰这种相互作用。含有简单单糖L - 岩藻糖的溶液会抑制结合。
