Vasi J, Svensson J, Frick I M, Müller H P
Department of Microbiology, SLU, Uppsala, Sweden.
Infect Immun. 1999 Jan;67(1):413-6. doi: 10.1128/IAI.67.1.413-416.1999.
Protein MIG, from Streptococcus dysgalactiae, binds alpha2-macroglobulin and immunoglobulin G (IgG). MIG-derived fusion proteins with one to five IgG-binding repeats differed up to 72,000- fold in avidity for goat IgG, indicating a considerable cooperativity of the repeats. Significant sequence variation in the IgG-binding repeats was recognized. Protein MIG interacted with goat IgG1 via both the Fc and Fab parts.
来自停乳链球菌的蛋白质MIG可结合α2-巨球蛋白和免疫球蛋白G(IgG)。具有1至5个IgG结合重复序列的MIG衍生融合蛋白对山羊IgG的亲和力差异高达72000倍,表明这些重复序列具有相当大的协同性。已识别出IgG结合重复序列中的显著序列变异。蛋白质MIG通过Fc和Fab部分与山羊IgG1相互作用。