Synthetic peptides of envelope proteins of two different strains of simian AIDS retrovirus (SRV-1 and SRV-2) represent unique antigenic determinants for serum neutralizing antibodies.
Synthetic peptides of envelope proteins of two different strains of simian AIDS retrovirus (SRV-1 and SRV-2) represent unique antigenic determinants for serum neutralizing antibodies.
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两种不同的猿猴艾滋病逆转录病毒株（SRV-1 和 SRV-2）的包膜蛋白的合成肽代表了血清中和抗体的独特抗原决定簇。
DOI：
10.1016/0161-5890(90)90098-k
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发表时间：
1990
影响因子：
3.6
通讯作者：
Benjamini,E
中科院分区：
文献类型：
--
作者：
Werner,LL;Malley,A;Torres,JV;Leung,CY;Kwang,HS;Benjamini,E
猴D型逆转录病毒（SRV）至少有三种不同的血清型，它们表现出广泛的血清学交叉反应性，但在血清中和抗体水平上不存在交叉反应性。比较了SRV-1和SRV-2包膜蛋白的氨基酸序列分析和疏水性图，以鉴定各自中和抗体可能针对的独特潜在抗原决定簇。合成代表SRV-1的残基147-162和SRV-2的残基96-102的肽，并评估其免疫反应性。分别使用SRV-1 147-162肽和SRV-2肽96-102证明了对针对SRV-1和SRV-2的毒株特异性血清（恒河猴）中和抗体的游离肽抑制。这些肽对血清中和活性的抑制也是菌株特异性的，未显示交叉抑制。与蛋白质载体缀合并与Sepharose珠交联的SRV-1147 -162特异性吸附来自SRV-1免疫恒河猴血清的中和抗体。从免疫吸附剂上洗脱的抗体具有中和SRV-1的活性，但对SRV-2的感染性没有影响。肽SRV-1147 -162也表现出与中和SRV-1的感染性的小鼠单克隆抗体特异性结合的能力。用重组的SRV-1包膜蛋白或用完整的灭活的SRV-1免疫的小鼠产生结合SRV-1147 -162缀合物的抗体，但不结合蛋白载体本身。针对SRV-I 147-162缀合物的小鼠抗体表现出与天然SRV-I和重组SRV-I包膜蛋白的特异性结合。这些发现提供了强有力的证据，证明SRV-1 147-162和SRV-2 96-102构成至少两个独特的抗原决定簇或其部分，其参与菌株特异性中和抗体应答。此外，研究结果表明，猴产生的SRV-1中和抗体和小鼠产生的至少一定数量的中和抗体识别SRV-1的相同表位。
There are at least three distinct serotypes of simian type D retrovirus (SRV) which exhibit extensive serological cross-reactivity, but no cross-reactivity exists at the level of serum neutralizing antibodies. Amino acid sequence analysis and hydrophobicity plots of SRV-1 and SRV-2 envelope proteins were compared in order to identify unique potential antigenic determinants to which respective neutralizing antibodies may be directed. Peptides representing residues 147–162 of SRV-1 and 96–102 of SRV-2 were synthesized and assessed for their immunoreactivity. Free peptide inhibition of strain-specific serum (rhesus) neutralizing antibodies to SRV-1 and SRV-2 was demonstrated using the SRV-1 147–162 peptide and the SRV-2 peptide, 96–102, respectively. Inhibition of serum neutralizing activity by these peptides was also strain-specific, showing no cross-inhibition. SRV-1 147–162 conjugated to a protein carrier and cross-linked to Sepharose beads specifically adsorbed neutralizing antibodies from SRV-1 immune rhesus sera. The antibodies eluted from the immunoadsorbent possessed SRV-1 neutralizing activity, but showed no effect on the infectivity of SRV-2. Peptide SRV-1 147–162 also exhibited the capacity to bind specifically with a mouse monoclonal antibody which neutralizes the infectivity of SRV-1.Mice immunized with a recombinant SRV-1 envelope protein or with whole, inactivated SRV-1 produced antibodies which bound the SRV-1 147–162 conjugate, but not the protein carrier itself. Mouse antibodies to the SRV-1 147–162 conjugate exhibited specific binding with both natlve SRV-1 and with recombinant SRV-1 envelope protein. These findings provide strong evidence that SRV-1 147–162 and SRV-2 96–102 constitute at least two unique antigenic determinants, or parts thereof, which participate in the strain-specific neutralizing antibody response. Moreover, the findings indicate that the SRV-1 neutralizing antibodies produced by monkeys and at least a certain population of neutralizing antibodies produced by mice recognize the same epitope of SRV-1.