Chauvaux S, Matuschek M, Beguin P
Unité de Physiologie Cellulaire, Département des Biotechnologies, Institut Pasteur, 75724 Paris Cedex 15, France.
J Bacteriol. 1999 Apr;181(8):2455-8. doi: 10.1128/JB.181.8.2455-2458.1999.
Binding parameters were determined for the SLH (S-layer homologous) domains from the Clostridium thermocellum outer layer protein OlpB, from the C. thermocellum S-layer protein SlpA, and from the Bacillus anthracis S-layer proteins EA1 and Sap, using cell walls from C. thermocellum and B. anthracis. Each SLH domain bound to C. thermocellum and B. anthracis cell walls with a different KD, ranging between 7.1 x 10(-7) and 1.8 x 10(-8) M. Cell wall binding sites for SLH domains displayed different binding specificities in C. thermocellum and B. anthracis. SLH-binding sites were not detected in cell walls of Bacillus subtilis. Cell walls of C. thermocellum lost their affinity for SLH domains after treatment with 48% hydrofluoric acid but not after treatment with formamide or dilute acid. A soluble component, extracted from C. thermocellum cells by sodium dodecyl sulfate treatment, bound the SLH domains from C. thermocellum but not those from B. anthracis proteins. A corresponding component was not found in B. anthracis.
利用嗜热栖热菌和炭疽芽孢杆菌的细胞壁,测定了来自嗜热栖热菌外层蛋白OlpB、嗜热栖热菌S层蛋白SlpA以及炭疽芽孢杆菌S层蛋白EA1和Sap的S层同源(SLH)结构域的结合参数。每个SLH结构域与嗜热栖热菌和炭疽芽孢杆菌细胞壁结合时具有不同的解离常数(KD),范围在7.1×10⁻⁷至1.8×10⁻⁸ M之间。SLH结构域的细胞壁结合位点在嗜热栖热菌和炭疽芽孢杆菌中表现出不同的结合特异性。在枯草芽孢杆菌的细胞壁中未检测到SLH结合位点。嗜热栖热菌的细胞壁在用48%氢氟酸处理后失去了对SLH结构域的亲和力,但在用甲酰胺或稀酸处理后没有。通过十二烷基硫酸钠处理从嗜热栖热菌细胞中提取的一种可溶性成分,能结合嗜热栖热菌的SLH结构域,但不能结合炭疽芽孢杆菌蛋白的SLH结构域。在炭疽芽孢杆菌中未发现相应成分。