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通过疏水基与蛋白酶体结合的肽在没有佐剂的情况下会变得具有高度免疫原性。

Peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants.

作者信息

Lowell G H, Smith L F, Seid R C, Zollinger W D

机构信息

Department of Bacterial Diseases, Walter Reed Army Institute of Research, Washington, DC 20307.

出版信息

J Exp Med. 1988 Feb 1;167(2):658-63. doi: 10.1084/jem.167.2.658.

Abstract

Addition of either a lauroyl or a pentapeptide (FLLAV) hydrophobic foot to the NH2 terminus of a small, synthetic peptide allowed the peptide to hydrophobically complex to meningococcal outer membrane protein proteosomes by simple dialysis. Both conventional and LPS-hyporesponsive mice immunized with these complexes without any adjuvants developed high-titered and persistent anti-peptide IgG. Since proteosomes have been safely given to many people and since important antigenic determinants are generally hydrophilic, this system should be widely applicable to the development of peptide vaccines for human use.

摘要

在一种小的合成肽的NH2末端添加月桂酰或五肽(FLLAV)疏水基团,可使该肽通过简单透析与脑膜炎球菌外膜蛋白蛋白酶体发生疏水结合。用这些复合物免疫的传统小鼠和LPS低反应性小鼠在没有任何佐剂的情况下均产生了高滴度且持久的抗肽IgG。由于蛋白酶体已安全地给予许多人,且重要的抗原决定簇通常是亲水的,因此该系统应广泛应用于人类肽疫苗的开发。

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