Critical amino acid changes in VP2 variable domain are associated with typical and atypical antigenicity in very virulent infectious bursal disease viruses
Critical amino acid changes in VP2 variable domain are associated with typical and atypical antigenicity in very virulent infectious bursal disease viruses
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DOI：
10.1007/s007050050404
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发表时间：
1998-01-01
影响因子：
2.7
通讯作者：
Rivallan, G
中科院分区：
文献类型：
--
作者：
Eterradossi, N;Arnauld, C;Rivallan, G
经典的血清1型传染性法氏囊病病毒（IBDV），但不是非常强的（vv）分离株，与中和单克隆抗体（NMab）3在病毒中和试验或抗原捕获ELISA反应。另外两个NMab，6和8，结合经典和大多数vv株，但不典型的94 432和91 168 vv株，分别。通过对编码VP 2主要免疫原性结构域的基因组区域进行测序，研究了此类反应性的基础。在经典、变异、疫苗或vv IBDV毒株中，与NMab 3的阴性反应与氨基酸（aa）位置222-223（亲水峰A）的脯氨酸-甘氨酸对的变化相关，与NMab 6和8的阴性反应与氨基酸位置318至324（亲水峰B）的变化相关。91 168和94 432病毒是在峰B中呈现aa变化的第一批vvIBDV。
Classical serotype 1 infectious bursal disease viruses (IBDV), but not very virulent (vv) isolates, react with neutralizing monoclonal antibody (NMab) 3 in virus neutralization tests or antigen-capture ELISA. Two other NMabs, 6 and 8, bind to both classical and most vv strains, but not to the atypical 94 432 and 91 168 vv strains, respectively. The basis for such reactivities was investigated by sequencing the genome region encoding the VP2 major immunogenic domain. In classical, variant, vaccine or vv IBDV strains, negative reactions with NMab3 were associated with changes in the Proline-Glycine pair at amino-acid (aa) positions 222-223 (hydrophilic peak A), and negative reactions with NMabs 6 and 8 with aa changes from positions 318 to 324 (hydrophilic peak B). The 91 168 and 94 432 viruses are the first vvIBDVs to present aa changes in peak B.