Efficient loading of identical viral peptide onto class II molecules by antigenized immunoglobulin and influenza virus.
Efficient loading of identical viral peptide onto class II molecules by antigenized immunoglobulin and influenza virus.
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DOI：
10.1084/jem.178.5.1795
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发表时间：
1993-11-01
影响因子：
15.3
通讯作者：
Zaghouani, H
中科院分区：
文献类型：
--
作者：
Brumeanu, T D;Swiggard, W J;Steinman, R M;Bona, C A;Zaghouani, H
几个先前的报道已经鉴定了与呈递细胞上的主要组织相容性复合体（MHC）II类分子天然相关的肽。我们已经研究了从外源性来源的肽到MHC II类分子的递送。该肽来源于流感病毒血凝素（HA）并激活CD 4 + T细胞杂交瘤。在抗原呈递的功能测定中，该表位在流感病毒或嵌合免疫球蛋白（IG）分子（Ig-HA）的情况下有效地递送至T细胞，其中肽已取代重链的CDR 3环。我们发现，相同的11-mer肽可以从小鼠MHC II类抗原中分离出来，无论肽的外源性来源是游离HA肽、Ig-HA嵌合体还是紫外线灭活的PR 8流感病毒。Ig-HA嵌合体被证明是通过外源途径给II类分子充电的最有效载体。鉴于这一事实，自我免疫球蛋白代表天然的长寿载体，我们认为，抗原化的免疫球蛋白有相当大的潜力，肽传递到MHC分子在原位。
Several prior reports have identified peptides that are naturally associated with major histocompatibility complex (MHC) class II molecules on presenting cells. We have examined the delivery of a peptide from exogenous sources to MHC class II molecules. The peptide derives from the influenza virus hemagglutinin (HA) and activates a CD4+ T cell hybridoma. In functional assays of antigen presentation, this epitope is delivered effectively to T cells either in the context of influenza virus or chimeric immunoglobulin (Ig) molecules (Ig-HA) in which the peptide has replaced the CDR3 loop of the heavy chain. We find that the identical 11-mer peptide can be isolated from mouse MHC class II antigens whether the exogenous source of peptide is free HA peptide, the Ig-HA chimera, or ultraviolet-inactivated PR8 influenza virus. The Ig-HA chimera proves to be the most efficient vehicle for charging class II molecules via the exogenous route. Given the fact that self Igs represent natural long-lived carriers, we suggest that antigenized Igs have considerable potential for peptide delivery to MHC molecules in situ.