Wang Jing, Zhang Anding, Li Ran, Jin Meilin
State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China.
Sheng Wu Gong Cheng Xue Bao. 2009 Apr;25(4):509-13.
Streptococcus suis (S. suis) IgG-binding protein (SPG) was present in all S. suis strains examined. It showed binding activities with IgG from various host species. Little was known about the biological role of this protein, but it was commonly believed that it acted as virulence factor. In this study, the genes encoding SPG were amplified respectively from the total DNA of the S. suis serotype 1/2, 1, 2 and 9 with PCR and expressed in Escherichia coli BL21 by plasmid pET28a as vector. The recombinant proteins were first purified with affinity chromatography (Ni-NTA), and further purified by sephadexG-200 gel chromatography. The recombinant SPG proteins were identified to have binding activities with IgG of different host species, and for human and porcine IgG they showed better binding activities. But the SPG from different serotypes of S. suis showed no great differences in their binding activities with IgG from the same host species.
猪链球菌(S. suis)IgG结合蛋白(SPG)存在于所有检测的猪链球菌菌株中。它与来自不同宿主物种的IgG具有结合活性。关于该蛋白的生物学作用知之甚少,但普遍认为它作为一种毒力因子发挥作用。在本研究中,通过PCR分别从猪链球菌1/2型、1型、2型和9型的总DNA中扩增出编码SPG的基因,并以质粒pET28a作为载体在大肠杆菌BL21中表达。重组蛋白首先用亲和层析(Ni-NTA)纯化,然后通过sephadexG-200凝胶层析进一步纯化。重组SPG蛋白被鉴定与不同宿主物种的IgG具有结合活性,并且对于人和猪的IgG,它们表现出更好的结合活性。但是来自不同血清型猪链球菌的SPG在与相同宿主物种IgG的结合活性上没有很大差异。