Understanding the structure and antigenicity of gonococcal pili.

Understanding the structure and antigenicity of gonococcal pili.
复制标题

了解淋球菌菌毛的结构和抗原性。

DOI:
10.1093/cid/10.supplement_2.s296
复制
发表时间:
1988
期刊:
Reviews of infectious diseases
影响因子:
--
通讯作者:
Tainer,JA
Tainer,JA
中科院分区:
--
文献类型:
--
作者:
Getzoff,ED;Parge,HE;McRee,DE;Tainer,JA

文献摘要

被引文献

相似文献

皮利-在许多感染性革兰氏阴性菌的细胞表面上发现的丝状蛋白质结构-通常是介导对宿主上皮细胞粘附的毒力因子。菌毛是淋球菌的主要表面抗原,由数千个重复相同的蛋白质亚基(菌毛蛋白)特异性结合而成。菌毛蛋白和菌毛纤维的结构研究可以通过提供关于皮利抗原表面的信息来帮助基于肽的疫苗的合理设计,所述信息包括鉴定定位于三维结构的单个区域的序列远距离抗原区域。初步结果表明,菌毛蛋白亚基与烟草花叶病毒外壳蛋白亚基和肌红蛋白等蛋白质中的4-α-螺旋束折叠结构相似。因此,使用单体蛋白肌红蛋白来鉴定4-α-螺旋束蛋白(如菌毛蛋白)上抗原决定簇的结构相关性。
Pili - filamentous protein structures found on the cell surface of many infectious gram-negative bacteria - often are virulence factors that mediate adherence to host epithelial cells. The pilus, a major surface antigen of the gonococcus, is formed by the specific association of thousands of repeating identical protein subunits (pilin). Structural studies of the pilin protein and the pilus fiber may aid the rational design of a peptide-based vaccine by providing information on the antigenic surface of pili that includes the identification of sequence-distant antigenic regions that are localized to single areas of the three-dimensional structure. Preliminary results suggest that the pilin subunit has structural similarity to the 4-α-helix bundle fold in proteins such as the coat protein subunit of tobacco mosaic virus and myohemerythrin. Therefore, the monomeric protein myohemerythrin was used to identify structural correlations for antigenic determinants on 4-α-helix bundle proteins such as pilin.