Plagemann P G, Harty J T, Even C
Department of Microbiology, University of Minnesota Medical School, Minneapolis.
Arch Virol. 1992;123(1-2):89-100. doi: 10.1007/BF01317140.
Neutralization of the infectivity of [3H]uridine-labeled lactate dehydrogenase-elevating virus (LDV) by polyclonal mouse or rabbit antibodies to the envelope glycoprotein of LDV, VP-3, or by neutralizing monoclonal antibodies (mAb) that recognize a different epitope on VP-3 than the polyclonal antibodies correlated with an increase in the sedimentation rate of LDV from 230 S to greater than or equal to 270 S. Incubation of LDV with normal mouse plasma or non-neutralizing mAbs to LDV VP-3 had no effect on its sedimentation rate. Similarly, incubation of a neutralization escape variant of LDV with the mAb used in its selection had no effect on its sedimentation rate, whereas neutralization of this variant by polyclonal mouse or rabbit anti-VP3 antibodies increased the sedimentation rate. Neutralization of LDV infectivity was only observed at high antibody/virion ratios and often was followed by loss of the viral RNA. The results suggest that neutralization of LDV infectivity results from binding of multiple antibody molecules that recognize specific epitopes on the viral envelope glycoprotein and ultimately leads to disintegration of the virions.
用针对乳酸脱氢酶升高病毒（LDV）包膜糖蛋白VP - 3的多克隆小鼠或兔抗体，或用识别VP - 3上与多克隆抗体不同表位的中和单克隆抗体（mAb）中和[3H]尿苷标记的LDV的感染性，与LDV沉降速率从230 S增加到大于或等于270 S相关。将LDV与正常小鼠血浆或针对LDV VP - 3的非中和mAb孵育对其沉降速率没有影响。同样，将LDV的中和逃逸变体与用于筛选它的mAb孵育对其沉降速率没有影响，而用多克隆小鼠或兔抗VP3抗体中和该变体则增加了沉降速率。仅在高抗体/病毒粒子比率下观察到LDV感染性的中和，并且通常随后病毒RNA丢失。结果表明，LDV感染性的中和是由于识别病毒包膜糖蛋白上特定表位的多个抗体分子的结合，最终导致病毒粒子解体。
