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B族链球菌群特异性多糖上的α-L-(1----2)-三鼠李糖吡喃糖苷表位。

The alpha-L-(1----2)-trirhamnopyranoside epitope on the group-specific polysaccharide of group B streptococci.

作者信息

Michon F, Chalifour R, Feldman R, Wessels M, Kasper D L, Gamian A, Pozsgay V, Jennings H J

机构信息

Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario.

出版信息

Infect Immun. 1991 May;59(5):1690-6. doi: 10.1128/iai.59.5.1690-1696.1991.

Abstract

A number of epitope specificities associated with the group antigen (group B polysaccharide) of group B streptococci have been identified in a polyclonal antiserum induced in rabbits by a nonencapsulated variant strain of group B streptococci. This was achieved by using a series of oligosaccharide inhibitors, obtained by both synthetic and degradative procedures, to inhibit the binding of the group B polysaccharide to the polyclonal antiserum. While the dominant epitope expressed in the antiserum was alpha-L-Rhap(1----2)alpha-L-Rhap(1----2)alpha-L-Rhap, specificities associated with alpha-L-Rhap and alpha-L-Rhap(1----3)alpha-D-Galp(1----3)beta-D-Glcp-NAc(1----4)alp ha-L-Rhap were also identified. The dominant expression of the former epitope is consistent with its terminal location on the group antigen and also with highly branched multiantennary structure of this antigen. Antibodies specific for the alpha-L-trirhamnopyranoside epitope were purified by affinity chromatography, using the synthetic trisaccharide glucitol as the hapten. Oligosaccharide inhibition studies indicate that the specificity of these antibodies is identical to that of a murine monoclonal antibody induced by the same nonencapsulated strain of group B streptococci.

摘要

通过用B族链球菌的非荚膜变异株诱导兔产生的多克隆抗血清,已鉴定出一些与B族链球菌群抗原(B族多糖)相关的表位特异性。这是通过使用一系列通过合成和降解程序获得的寡糖抑制剂来抑制B族多糖与多克隆抗血清的结合来实现的。虽然抗血清中表达的主要表位是α-L-Rhap(1→2)α-L-Rhap(1→2)α-L-Rhap,但也鉴定出了与α-L-Rhap和α-L-Rhap(1→3)α-D-Galp(1→3)β-D-Glcp-NAc(1→4)α-L-Rhap相关的特异性。前一种表位的主要表达与其在群抗原上的末端位置一致,也与其该抗原的高度分支多天线结构一致。使用合成三糖葡糖醇作为半抗原,通过亲和色谱法纯化了对α-L-三鼠李吡喃糖苷表位特异的抗体。寡糖抑制研究表明,这些抗体的特异性与由同一B族链球菌非荚膜菌株诱导的鼠单克隆抗体的特异性相同。

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