Tang X L, Tregear G W, White D O, Jackson D C
Department of Microbiology, University of Melbourne, Parkville, Australia.
J Virol. 1988 Dec;62(12):4745-51. doi: 10.1128/JVI.62.12.4745-4751.1988.
Synthetic peptides of increasing length and corresponding in sequence to the C-terminal end of the HA1 molecule of influenza virus were constructed and examined for their immunogenic and antigenic properties. Peptides containing at least the four C-terminal amino acids, when coupled to keyhole limpet hemocyanin, were capable of eliciting antibody in BALB/c mice that bound to the 24-residue parent peptide H3 HA1 (305 to 328). In the absence of a carrier, the C-terminal decapeptide was the shortest peptide capable of eliciting antibody. The specificity of this antibody was indistinguishable from that of a monoclonal antibody to the parent peptide which recognizes an epitope encompassed by the C-terminal seven residues. All peptides containing at least the C-terminal four residues were able to inhibit completely the binding of this monoclonal antibody to the parent peptide. Taken together, these results indicate that (i) the tetrapeptide is capable of eliciting specific antibody when coupled to a carrier, (ii) this tetrapeptide possesses all of the antigenic information necessary to occupy the paratope of a monoclonal antibody elicited by the longer parent peptide, and (iii) the decapeptide contains all of the information necessary to elicit a specific immune response and therefore carries an epitope recognized by T cells as well as one recognized by B cells.
构建了长度递增且序列与流感病毒HA1分子C末端相对应的合成肽，并检测了它们的免疫原性和抗原性。当与钥孔血蓝蛋白偶联时，含有至少四个C末端氨基酸的肽能够在BALB/c小鼠中引发与24个残基的亲本肽H3 HA1（305至328）结合的抗体。在没有载体的情况下，C末端十肽是能够引发抗体的最短肽。该抗体的特异性与识别由C末端七个残基组成的表位的亲本肽单克隆抗体的特异性无法区分。所有含有至少C末端四个残基的肽都能够完全抑制该单克隆抗体与亲本肽的结合。综上所述，这些结果表明：（i）四肽与载体偶联时能够引发特异性抗体；（ii）该四肽具有占据由较长亲本肽引发的单克隆抗体互补位所需的所有抗原信息；（iii）十肽包含引发特异性免疫反应所需的所有信息，因此携带一个被T细胞识别的表位以及一个被B细胞识别的表位。
