论文部分内容阅读
目的：对重组杆状病毒表达的经多种信号序列修饰的天然和变异百日咳毒素（ＰＴ）Ｓ１亚单位（ｒＳ１）的生物学及免疫学特性作出评价。方法：应用生物化学和免疫学技术与方法对这些ｒＳ１的酶活性、分泌性和免疫原性等做了系统鉴定。结果：ｒＳ１变异子无可检出的酶活性；所有ｒＳ１均不能由细胞分泌，可从细胞膜组分中大量检出，但不能从可溶性胞浆蛋白组分或细胞培养上清中检出；ｒＳ１分子内部含有３个疏水性区域；ｒＳ１虽不能与Ｂ寡聚体结合形成ＰＴ全毒素，但均能诱导抗ＰＴ免疫应答。结论：这些ｒＳ１极可能以膜蛋白形式存在，其非分泌性与分子内部的疏水性区域有关；所有ｒＳ１均保持其免疫原性。
OBJECTIVE: To evaluate the biological and immunological properties of recombinant and recombinant pertussis toxin (PT) S1 subunit (rS1) expressed by recombinant baculovirus using various signal sequences. Methods: The biochemical and immunological techniques and methods were used to systematically identify the enzyme activities, secretion and immunogenicity of these rS1. Results: rS1 had no detectable enzyme activity. All rS1 were not secreted by cells and could be detected abundantly in cell membrane fraction but not in soluble cytosolic fractions or cell culture supernatant. RS1 There are three hydrophobic regions in the molecule. Although rS1 can not bind to B oligomer to form PT holotoxin, it can induce anti-PT immune response. CONCLUSIONS: These rS1s are likely to be present as membrane proteins, and their non-secreted nature is related to the hydrophobic region within the molecule; all rS1s remain immunogenic.