Campbell A P, Sheth H, Hodges R S, Sykes B D
Protein Engineering Network of Centers of Excellence, University of Alberta, Edmonton, Canada.
Int J Pept Protein Res. 1996 Dec;48(6):539-52. doi: 10.1111/j.1399-3011.1996.tb00873.x.
The solution structure of the peptide antigen from the receptor binding domain of Pseudomonas aeruginosa strain P1 has been determined using two-dimensional 1H NMR techniques. Ensembles of solution conformations for the trans form of this 23-residue disulfide bridged peptide have been generated using a simulated annealing procedure in conjunction with distance and torsion angle restraints derived from NMR data. Comparison of the NMR-derived solution structures of the P1 peptide with those previously determined for the 17-residue PAK, PAO and KB7 strain peptides [McInnes, C., et al. (1993) Biochemistry 32, 13432-13440; Campbell, A.P., et al. (1995) Biochemistry 34, 16255-16268] reveals the common structural motif of a beta-turn, which may be the necessary structural requirement for recognition of a common cell surface receptor and a common cross-reactive antibody to which all four strains bind. The importance of this conserved beta-turn in the PAK, PAO, KB7 and P1 peptides is discussed with regard to the design of a synthetic peptide vaccine effective against multiple strains of Pseudomonas aeruginosa infections.
利用二维1H NMR技术确定了铜绿假单胞菌P1菌株受体结合域肽抗原的溶液结构。结合从NMR数据得出的距离和扭转角限制，通过模拟退火程序生成了这种23个残基的二硫键桥连肽反式构象的溶液构象集合。将P1肽的NMR衍生溶液结构与先前为17个残基的PAK、PAO和KB7菌株肽所确定的结构进行比较[McInnes, C., 等人 (1993) Biochemistry 32, 13432 - 13440; Campbell, A.P., 等人 (1995) Biochemistry 34, 16255 - 16268]，揭示了β-转角的共同结构基序，这可能是识别所有四种菌株都能结合的共同细胞表面受体和共同交叉反应抗体的必要结构要求。关于设计一种有效对抗多种铜绿假单胞菌感染菌株的合成肽疫苗，讨论了PAK、PAO、KB7和P1肽中这种保守β-转角的重要性。
