Severinsson L, Martens I, Peterson P A
J Immunol. 1986 Aug 1;137(3):1003-9.
The glycoprotein E19, encoded in early region 3 of adenovirus-2, forms complexes with major histocompatibility complex class I antigens. As a result of the complex formation, the intracellular transport of the class I antigens is abrogated, and adenovirus-infected cells display gradually diminishing quantities of cell surface-expressed class I molecules. To assess whether the E19 protein interacts equally well with different class I antigens, the associations between the viral protein and HLA-A2 and HLA-B7 antigens have been estimated. By infecting transfected HeLa cells expressing various amounts of HLA-A2 and HLA-B7 molecules, respectively, with various infectious doses of adenovirus-2, experimental conditions could be established that allowed quantitative estimates of the interactions to be determined. It was found that HLA-A2 molecules and the E19 protein interacts with a binding constant that is more than twice as high as that for HLA-B7 antigens and the viral protein. It is suggested that the pathogenicity of the virus may be dependent on the HLA-type of the infected individual.
腺病毒2型早期区域3编码的糖蛋白E19与主要组织相容性复合体I类抗原形成复合物。复合物形成后，I类抗原的细胞内转运被阻断，腺病毒感染的细胞表面表达的I类分子数量逐渐减少。为了评估E19蛋白与不同I类抗原的相互作用是否同样良好，已对病毒蛋白与HLA - A2和HLA - B7抗原之间的关联进行了评估。通过分别用不同感染剂量的腺病毒2感染表达不同数量HLA - A2和HLA - B7分子的转染HeLa细胞，可以建立实验条件来定量确定相互作用。结果发现，HLA - A2分子与E19蛋白相互作用的结合常数比HLA - B7抗原与病毒蛋白相互作用的结合常数高出两倍多。提示病毒的致病性可能取决于被感染个体的HLA类型。
