PEPTIDE MIMICS OF GROUP B STREPTOCOCCAL CARBOHYDRATE ANTIGENS

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。利用噬菌体展示文库，筛选出与高度保护性的单抗S9结合的多肽，该单抗与B组链球菌的III型衣壳多糖结合。证明了这种多肽作为抗原性模拟物的能力，并在免疫后诱导抗III型抗体。二级噬菌体文库允许选择改进的模拟物。核磁共振研究表明，该多肽在溶液中是游离的，并与抗体结合。与CCRC的合作研究旨在进一步研究这种模仿的结构基础。同时与CPS和多肽结合的抗体正在制造中。一旦它们被提纯，它们将被结晶，无论有没有碳水化合物或多肽抗原，并用于X射线衍射分析。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Using phage display libraries, peptides were selected that bind to the highly protective monoclonal antibody S9, which binds to the type III capsular polysaccharide of group B streptococcus. The ability of this peptide to be an antigenic mimic and to elicit anti-type III antibodies upon immunization was demonstrated. A secondary phage library allowed the selection of improved mimics. NMR studies have been performed showing the peptide both free in solution and bound by the antibody. Collaborative research with the CCRC aims to further study the structural basis for this mimicry. Fabs of antibodies that bind to both the CPS and peptide are being made. Once they are purified, they will be crystallized, either with or without carbohydrate or peptide antigen, and used for X-ray diffraction analyses.