Kostyushov V V
Department of Pharmacology, Odessa State Medical University.
Bull Exp Biol Med. 2000 Dec;130(12):1147-9.
The effects of HIV antigen glycoproteins gp160, gp41, and gp36 on thiol-dependent specific (affinity) binding of serum IgM, IgG, and IgA with the corresponding antigens were determined by the formation of signal thiol-containing analytes (free nonprotein SH groups). Free nonprotein SH groups were not found in the reaction mixture, which indicated that HIV antigen glycoproteins blocked this process. The results suggest that the thiol-selective mechanism underlies in vitro conjugation of HIV antigen glycoproteins gp160, gp41, and gp36 with serum immunoglobulins. Previous studies showed that this mechanism of conjugation with immunoglobulins is not characteristic of other lymphotropic viruses (e.g., hepatitis B virus).
通过形成含硫醇信号分析物(游离非蛋白SH基团),测定了HIV抗原糖蛋白gp160、gp41和gp36对血清IgM、IgG和IgA与相应抗原的硫醇依赖性特异性(亲和性)结合的影响。反应混合物中未发现游离非蛋白SH基团,这表明HIV抗原糖蛋白阻断了这一过程。结果表明,硫醇选择性机制是HIV抗原糖蛋白gp160、gp41和gp36与血清免疫球蛋白在体外结合的基础。先前的研究表明,这种与免疫球蛋白结合的机制并非其他嗜淋巴细胞病毒(如乙型肝炎病毒)所特有。