Gallina A, Rossi F, Mariani M, Bonelli F, Achilli G, Cattaneo E, Milanesi G
Istituto di Genetica Biochimica ed Evoluzionistica, Consiglio Nazionale delle Ricerche, Pavia, Italy.
J Med Virol. 1990 Nov;32(3):164-70. doi: 10.1002/jmv.1890320307.
Antigenicity in mice of a recombinant polypeptide including the complete amino acid sequence of mature human immunodeficiency virus type 1 p24 protein was studied by induction of monoclonal antibodies (MAbs). A panel of nine recloned hybridomas secreting MAbs with anti-p24 reactivity was isolated and further characterized. Competitive inhibition experiments suggested that the MAbs could be grouped into four epitopic classes corresponding to at least two distinct determinants. Analysis of reactivity to recombinant p24 deletion variants indicated that all the recognized epitopes are localized within a carboxy-terminal domain (amino acids 168-208) which should be largely exposed in recombinant as well as authentic antigen. Lack of response to N-terminal and central portions of p24 suggests that the antigenicity of those regions in the natural polypeptide is strongly conformation-dependent.
通过诱导单克隆抗体（MAb）研究了包含成熟人类免疫缺陷病毒1型p24蛋白完整氨基酸序列的重组多肽在小鼠体内的抗原性。分离出一组九个经再次克隆的分泌具有抗p24反应性单克隆抗体的杂交瘤，并对其进行了进一步鉴定。竞争性抑制实验表明，这些单克隆抗体可分为四个表位类别，对应于至少两个不同的决定簇。对重组p24缺失变体的反应性分析表明，所有识别的表位均位于羧基末端结构域（氨基酸168 - 208）内，该结构域在重组抗原以及天然抗原中应大部分暴露。对p24 N端和中间部分无反应表明，天然多肽中这些区域的抗原性强烈依赖于构象。
