IDENTIFICATION OF MONOCLONAL ANTIBODY-BINDING DOMAINS WITHIN ANTIGEN-P1 OF STREPTOCOCCUS-MUTANS AND CROSS-REACTIVITY WITH RELATED SURFACE-ANTIGENS OF ORAL STREPTOCOCCI
IDENTIFICATION OF MONOCLONAL ANTIBODY-BINDING DOMAINS WITHIN ANTIGEN-P1 OF STREPTOCOCCUS-MUTANS AND CROSS-REACTIVITY WITH RELATED SURFACE-ANTIGENS OF ORAL STREPTOCOCCI
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DOI：
10.1128/iai.59.12.4425-4435.1991
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发表时间：
1991-12-01
影响因子：
3.1
通讯作者：
BLEIWEIS, AS
中科院分区：
文献类型：
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作者：
BRADY, LJ;PIACENTINI, DA;BLEIWEIS, AS
11个单克隆抗体（MAbs）特异性P1，变形链球菌血清型C的主要蛋白表面抗原，其特征在于通过Western印迹（免疫印迹）分析和放射免疫分析，使用全细菌细胞。 通过使用全长和截短的P1多肽确定MAbs的近似结合结构域。 通过放射免疫测定法测定了完整细菌表面上这些结合位点的可及性。 单克隆抗体与沙门氏菌相关蛋白的交叉反应能力。变形链球菌血清型e和f、S. sanguis和S.还报道了sobrinus血清型G。
Eleven monoclonal antibodies (MAbs) specific for P1, the major protein surface antigen of Streptococcus mutans serotype c, were characterized by Western blot (immunoblot) analysis and by radioimmunoassay using whole bacterial cells. The approximate binding domains of the MAbs were determined by using full-length and truncated P1 polypeptides. The accessibility of these binding sites on the surfaces of intact bacteria was determined by radioimmunoassay. The ability of each MAb to cross-react with related proteins from strains of S. mutans serotypes e and f, S. sanguis, and S. sobrinus serotype g is also reported.