摘要
It is desirable to develop potent rabies virus neutralizing human monoclonal antibodies(McAbs) to replace human or equine polyclonal immunoglobulin in the rabies virus postexposure treatment.Using BIAcore2000,affinity constants of McAbs with rabies virus glycoprotein(G protein) were determined taking human immunoglobulin as control,and affinity constants were calculated using BIAevaluation software.The affinity of McAb SOJB with rabies virus G protein was higher than that of SO57.Competition binding analyses ran on BIAcore2000 revealed that SO57 and SOJB competed for binding to rabies virus G protein,suggesting that epitopes recognized by SO57 and SOJB overlapped.Furthermore,the neutralizing potency of SO57 was significantly greater than that of SOJB as RFFIT showed.So it is desirable to develop SO57 firstly for rabies virus postexposure treatment.
It is desirable to develop potent rabies virus neutralizing human monoclonal antibodies(McAbs) to replace human or equine polyclonal immunoglobulin in the rabies virus postexposure treatment. Using BIA-core2000, affinity constants of MeAbs with rabies virus glyeoprotein(G protein) were determined taking human immunoglobulin as control, and affinity constants were calculated using BIAevaluation software. The affinity of MeAb SOJB with rabies virus G protein was higher than that of SO57. Competition binding analyses ran on BI-Acore2000 revealed that SO57 and SOJB competed for binding to rabies virus G protein, suggesting that epitopes recognized by SO57 and SOJB overlapped. Furthermore, the neutralizing potency of SO57 was significantly greater than that of SOJB as RFFIT showed. So it is desirable to develop SO57 firstly for rabies virus postexposure treatment.
出处
《病毒学报》
CAS
CSCD
北大核心
2006年第3期230-232,共3页
Chinese Journal of Virology
关键词
BIA
SO57
SOJB
G蛋白
亲和常数
竞争结合反应
Biomolecular Interaction Analysis(BIA)
G protein
affinity constant
competition binding