中华皮肤科杂志
中華皮膚科雜誌
중화피부과잡지
Chinese Journal of Dermatology
2012年
10期
731-734
,共4页
刘沐桑%松下修三%柴田润二%刘维达
劉沐桑%鬆下脩三%柴田潤二%劉維達
류목상%송하수삼%시전윤이%류유체
HIV-1%突变%中和抗体
HIV-1%突變%中和抗體
HIV-1%돌변%중화항체
HIV-1%Mutation%Neutralizing antibody
目的 探讨HIV-1病毒包膜蛋白gp120的V2区突变对其他结构域的中和抗体识别的影响.方法 使用假病毒构建系统包装野生型和V2区突变型的HIV-1假病毒,分别测试抗CD4结合位点中和抗体和CD4诱导的中和抗体对两种病毒的中和作用.使用双抗体夹心ELISA法测试CD4结合位点中和抗体和CD4诱导的中和抗体对gp120野生型和突变型蛋白的亲合力.结果 CD4结合位点中和抗体和CD4诱导的中和抗体均无法中和野生株JR-FL WT假病毒,但2种中和抗体对V2突变株的中和活性显著提高,在低浓度下即可中和该病毒.野生株和突变株gp120单体与抗CD4结合位点中和抗体的结合力无明显差异,而gp120单体与CD4诱导的中和抗体的结合实验ELISA曲线却明显分离,CD4诱导的中和抗体与突变型JR-FL L175P gp120的结合强度均明显高于它们与野生型JR-FLWT gp120的结合强度.结论 HIV-1 V2区突变可影响中和抗体的抗病毒效果.
目的 探討HIV-1病毒包膜蛋白gp120的V2區突變對其他結構域的中和抗體識彆的影響.方法 使用假病毒構建繫統包裝野生型和V2區突變型的HIV-1假病毒,分彆測試抗CD4結閤位點中和抗體和CD4誘導的中和抗體對兩種病毒的中和作用.使用雙抗體夾心ELISA法測試CD4結閤位點中和抗體和CD4誘導的中和抗體對gp120野生型和突變型蛋白的親閤力.結果 CD4結閤位點中和抗體和CD4誘導的中和抗體均無法中和野生株JR-FL WT假病毒,但2種中和抗體對V2突變株的中和活性顯著提高,在低濃度下即可中和該病毒.野生株和突變株gp120單體與抗CD4結閤位點中和抗體的結閤力無明顯差異,而gp120單體與CD4誘導的中和抗體的結閤實驗ELISA麯線卻明顯分離,CD4誘導的中和抗體與突變型JR-FL L175P gp120的結閤彊度均明顯高于它們與野生型JR-FLWT gp120的結閤彊度.結論 HIV-1 V2區突變可影響中和抗體的抗病毒效果.
목적 탐토HIV-1병독포막단백gp120적V2구돌변대기타결구역적중화항체식별적영향.방법 사용가병독구건계통포장야생형화V2구돌변형적HIV-1가병독,분별측시항CD4결합위점중화항체화CD4유도적중화항체대량충병독적중화작용.사용쌍항체협심ELISA법측시CD4결합위점중화항체화CD4유도적중화항체대gp120야생형화돌변형단백적친합력.결과 CD4결합위점중화항체화CD4유도적중화항체균무법중화야생주JR-FL WT가병독,단2충중화항체대V2돌변주적중화활성현저제고,재저농도하즉가중화해병독.야생주화돌변주gp120단체여항CD4결합위점중화항체적결합력무명현차이,이gp120단체여CD4유도적중화항체적결합실험ELISA곡선각명현분리,CD4유도적중화항체여돌변형JR-FL L175P gp120적결합강도균명현고우타문여야생형JR-FLWT gp120적결합강도.결론 HIV-1 V2구돌변가영향중화항체적항병독효과.
Objective To investigate the impact of mutations in the V2 domain of HIV-1 envelop glycoprotein (gp) 120 gene on the recognition of neutralizing antibodies (NAbs) specific to the other domains of gp120.Methods HIV-1 pseudoviruses (JR-FL) containing wild type or V2-mutant gp120 monomers were constructed,and the neutralization of CD4-binding site-specific and CD4-induced NAbs to the HIV-1 pseudoviruses was observed.Enzyme linked immunosorbent assay (ELISA) was performed to evaluate the binding affinity of CD4-binding site-specific and CD4-induced NAbs to wild type or V2-mutant gp120.Results Neither CD4-binding site-specific nor CD4-induced NAbs could neutralize the wild type JR-FL pseudoviruses,but both of them could neutralize pseudoviruses containg the gp120 V2 mutant at a low concentration.There was no significant difference in the binding affinity to CD4-binding site-specific NAbs between the wild type and mutant gp120,while the ELISA binding curves of wild type and mutant gp120 against CD4-induced NAbs were separate,and the affinity of CD4-induced NAbs to the mutant gp120 (L175P) was notably higher than that to the wild type gp120.Conclusion The mutations in the V2 domain of HIV-1 gp120 may affect the antiviral activity of NAbs.
