Getzoff E D, Parge H E, McRee D E, Tainer J A
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.
Rev Infect Dis. 1988 Jul-Aug;10 Suppl 2:S296-9. doi: 10.1093/cid/10.supplement_2.s296.
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-alpha-helix bundle fold in proteins such as the coat protein subunit of tobacco mosaic virus and myohemerythrin. Therefore, the monomeric protein myohemeythrin was used to identify structural correlations for antigenic determinants on 4-alpha-helix bundle proteins such as pilin.
菌毛——在许多传染性革兰氏阴性菌细胞表面发现的丝状蛋白质结构——通常是介导与宿主上皮细胞黏附的毒力因子。菌毛是淋球菌的主要表面抗原，由数千个重复的相同蛋白质亚基（菌毛蛋白）特异性结合形成。对菌毛蛋白和菌毛纤维的结构研究，通过提供菌毛抗原表面的信息，包括鉴定定位于三维结构单个区域的序列距离较远的抗原区域，可能有助于基于肽的疫苗的合理设计。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，单体蛋白肌红蛋白被用于确定4-α-螺旋束蛋白（如菌毛蛋白）上抗原决定簇的结构相关性。
