HUMAN ANTIBODY RESPONSIVENESS AND DENTAL CARIES

主要研究者对人类的研究表明， 口腔细菌的血清抗体沉淀与 龋齿的严重程度和积累的显着差异， 菌斑 一种抗体与一种抗原决定基沉淀， 放线菌大分子另一个是D-丙氨酰酯 来自链球菌和乳酸杆菌的甘油磷壁酸的部分。 抗聚甘油磷酸酯部分的非沉淀性血清抗体 后一种抗原与龋齿严重程度无关。 D-丙氨酰 酯表位在pH 5下稳定，但在生理pH下迅速水解。 本研究的主要具体目的是定量血清和 通过灵敏的酶免疫测定法测定唾液抗体对每个表位的应答 为了检查表位特异性局部和 全身性抗体反应、年龄、龋齿严重程度和牙菌斑积累。 第二个目的是阐明遗传组成在反应中的作用。 发展 血清IgG和分泌型伊加来源于不同的免疫反应模式。 抗原暴露和分别指示全身或局部免疫 应答 在培养物或细胞提取物中的相应抗原 色葡萄变形链球菌GS-4和A. viscosus ATCC 19246将被涂覆威尔斯 微量培养板和血清或唾液样品的抗体含量 测定 在不存在或存在以下物质的情况下结合的抗体的量 适当的半抗原将用碱性磷酸酶共价测定 与对人IgG或分泌链具有特异性的山羊IgG缀合 人类伊加 抑制前后结合的差异将 反映表位特异性抗体结合，并将通过 与适当的强反应性血清进行比较。 的关系 表位特异性抗体与沉淀素反应的结合量 将通过多元判别分析进行检验。 的相互关系 各自抗体含量的相互关系、年龄、龋齿严重程度 暴露在氟化物中的时间长短、牙菌斑积累和牙龈炎将 通过对整个人口进行多元回归分析， 在各种血清和唾液抗体应答组中。 差异 龋病严重程度或HLA-A、B、C和DR特异性表达 分别由抗体应答组进行多重检查 判别分析 研究结果应确定与此相关的新因素。 具有防龋和易感性。

Studies in humans by the principal investigator have shown that precipitating serum antibodies to oral bacteria are associated with significant differences in dental caries severity and accumulation of bacterial plaque. One antibody precipitates with an epitope found on macromolecules from Actinomyces spp. and the other with the D-alanyl ester moeity of glycerol teichoic acids from Streptococci and Lactobacilli. Non-precipitating serum antibodies to the polyglycerol phosphate moeity of the latter antigen are not associated with caries severity. The D-alanyl ester epitope is stable at pH 5, but hydrolyses rapidly at physiologic pH. The major specific aim of this study is to quantitate the serum and salivary antibody response to each epitope by a sensitive enzymoimmunoassay in order to examine the relationships between epitope-specific local and systemic antibody responses, age, caries severity and plaque accumulation. A secondary aim is to elucidate a role for genetic constitution in response development. Serum IgG and secretory IgA originate from different modes of antigen exposure and respectively indicate systemic or local immune responses. The respective antigens, in culture filtrates or cell extracts of S. mutans GS-4 and A. viscosus ATCC 19246, will be coated on wells of microplates and the antibody content of serum or salivary samples determined. The amount of antibody bound in the absence or presence of appropriate haptens will be measured with alkaline phosphatase covalently conjugated to goat IgG specific for either human IgG or the secretory chain of human IgA. The difference in binding before and after inhibition will reflect epitope-specific antibody binding and will be quantified by comparison with an appropriate, strongly reactive serum. The relationship of the epitope-specific antibody binding contents to precipitin responses will be examined by multiple discriminant analysis. The interrelationship of the respective antibody contents to each other, age, caries severity, length of fluoride exposure, plaque accumulation and gingivitis will be examined by multiple regression analysis over the whole population and within various serum and saliva antibody response groups. Differences in caries severity or expression of HLA-A, B, C and DR specificities respectively by antibody response group will be examined by multiple discriminant analysis. The findings should identify new factors associated with caries protection and susceptibility.