Immune response to uncoupled peptides of foot-and-mouth disease virus.
Immune response to uncoupled peptides of foot-and-mouth disease virus.
复制标题
对口蹄疫病毒解偶联肽的免疫反应。
作者：
M. Francis;C. Fry;D. Rowlands;J. Bittle;R. Houghten;R. Lerner;F. Brown
口蹄疫病毒（FMDV）VP 1蛋白141-160位氨基酸序列的非偶联合成肽在豚鼠中诱导病毒中和抗体应答。这种反应需要不完全弗氏佐剂（IFA）的主要接种，并依赖于添加的半胱氨酸残基与未封闭的巯基在羧基末端的存在。二次免疫可以在没有佐剂的情况下进行。对150-160至135-160和141-160至141-155的未偶联肽的嵌套组的相对活性的研究表明，氨基酸146-156对于诱导病毒中和抗体是关键的，并且延伸至137-160进一步改善了这种应答。体外增殖研究的结果表明，该肽上的羧基末端残基可以形成T细胞表位。这些观察结果在更广泛的背景下，合成肽疫苗的意义进行了讨论。
Uncoupled synthetic peptide representing the sequence of amino acids 141-160 of foot-and-mouth disease virus (FMDV) protein VP1 induced a virus-neutralizing antibody response in guinea-pigs. This response required incomplete Freund's adjuvant (IFA) for the primary inoculation and was dependent on the presence of an added cysteine residue with an unblocked sulphydryl group at the carboxy-terminus. Secondary immunization could be carried out in the absence of adjuvant. A study of the relative activities of nested sets of uncoupled peptides from 150-160 to 135-160 and 141-160 to 141-155 indicated that amino acids 146-156 were critical for the induction of virus-neutralizing antibodies and that extension to 137-160 further improved this response. Results of in vitro proliferation studies demonstrated that the carboxy-terminal residues on this peptide may form a T-cell epitope. The significance of these observations in the broader context of synthetic peptide vaccines is discussed.