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人CD56+自然杀伤细胞和淋巴因子激活的杀伤细胞对人巨细胞病毒感染靶细胞的MHC非限制性识别的结构特异性

Structural specificity of MHC-unrestricted recognition of HCMV-infected target cells by human CD56+NK and LAK cells.

作者信息

Steinmassl M, Anderer F A

机构信息

Friedrich-Miescher-Laboratorium der Max-Planck-Gesellschaft, Tuebingen, Germany.

出版信息

Scand J Immunol. 1994 Dec;40(6):665-8. doi: 10.1111/j.1365-3083.1994.tb03521.x.

DOI:10.1111/j.1365-3083.1994.tb03521.x
PMID:7527935
Abstract

Structural specificity of binding and cytolysis of HCMV-infected human foreskin fibroblasts (HFF) by human NK and LAK cells was studied in inhibition assays. A sample of 60%-deacetylated alpha-D mannose penta-acetate was used as inhibitor that was previously shown to specifically inhibit binding and cytolysis of tumour target cells by human NK and LAK cells. We found now that cytolysis of HCMV-infected HFF was inhibited in a dose-dependent manner showing complete inhibition at concentrations above 640 nmoles/ml mannose acetate. This effect on cytolysis was based on inhibition of conjugate formation between virus-infected cells and CD56+NK and LAK cells. In the presence of mannose acetate (640 nmoles/ml) conjugate formation of virus-infected cells was suppressed down to the level of uninfected cells. The latter showed residual conjugate formation on the basis of adhesive interactions with chemospecifity other than for mannose acetate, which were not capable of triggering cytolytic reactions. Coculturing of target cells with LAK cells appeared to induce expression of additional mannose acetate-specific target sites yielding increases of conjugate formation and cytolysis.

摘要

在抑制试验中研究了人自然杀伤细胞(NK)和淋巴因子激活的杀伤细胞(LAK)对人巨细胞病毒(HCMV)感染的人包皮成纤维细胞(HFF)的结合和细胞溶解的结构特异性。使用60%脱乙酰化的α-D甘露糖五乙酸酯作为抑制剂,该抑制剂先前已被证明能特异性抑制人NK和LAK细胞对肿瘤靶细胞的结合和细胞溶解。我们现在发现,HCMV感染的HFF的细胞溶解以剂量依赖的方式受到抑制,在高于640纳摩尔/毫升甘露糖乙酸酯的浓度下表现出完全抑制。这种对细胞溶解的作用是基于抑制病毒感染细胞与CD56+NK和LAK细胞之间的共轭物形成。在存在甘露糖乙酸酯(640纳摩尔/毫升)的情况下,病毒感染细胞的共轭物形成被抑制到未感染细胞的水平。后者基于与除甘露糖乙酸酯以外的化学特异性的粘附相互作用显示出残留的共轭物形成,而这些相互作用不能触发细胞溶解反应。靶细胞与LAK细胞共培养似乎诱导了额外的甘露糖乙酸酯特异性靶位点的表达,导致共轭物形成和细胞溶解增加。

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