使用表面等离子体共振测定一组IgG和Fab对完整包膜（甲型流感）病毒粒子的亲和力。
Determination of affinities of a panel of IgGs and Fabs for whole enveloped (influenza A) virions using surface plasmon resonance.
作者信息
Schofield D J, Dimmock N J
机构信息
Department of Biological Sciences, University of Warwick, Coventry, UK.
出版信息
J Virol Methods. 1996 Oct;62(1):33-42. doi: 10.1016/0166-0934(96)02086-1.
Abstract
The affinity of a panel of neutralizing monoclonal IgGs and their Fab fragments has been measured for the first time with an enveloped type A influenza virus, by surface plasmon resonance (SPR) and the BIAlite instrument. Equilibrium constants could be calculated for four of the five mAbs tested. These were in the nanomolar range. The ranking order was very similar to that obtained with an affinity ELISA, (an equilibrium system) but as others have found, affinities were 2-10-fold lower as measured by SPR (a flow system). No data were obtained with mAb HC58 although it had one of the highest affinities using an ELISA format, and was 28-fold higher than another mAb (HC10) which gave good data by SPR. This may relate to the orientation of its binding on the virion surface. The Kdissoc. of the Fabs was only 3-10-fold higher compared to their IgGs. Fab from the lowest affinity IgG (HC10) could not be measured, possibly because it fell below the threshold for detection.
摘要
首次使用表面等离子体共振（SPR）和BIAlite仪器，测定了一组中和性单克隆IgG及其Fab片段与包膜A型流感病毒的亲和力。对于所测试的五种单克隆抗体中的四种，可以计算出平衡常数。这些常数处于纳摩尔范围内。排名顺序与通过亲和力ELISA（一种平衡系统）获得的顺序非常相似，但正如其他人所发现的，通过SPR（一种流动系统）测量的亲和力低2至10倍。尽管单克隆抗体HC58在ELISA检测中具有最高的亲和力之一，且比通过SPR获得良好数据的另一种单克隆抗体（HC10）高28倍，但未获得其相关数据。这可能与其在病毒粒子表面的结合方向有关。与它们的IgG相比，Fab的解离常数仅高3至10倍。来自最低亲和力IgG（HC10）的Fab无法测量，可能是因为它低于检测阈值。
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