主要目的：比较肌内注射CBL8851注射液与破伤风人免疫球蛋白在中国成年志愿者中的中和抗体活性，为后续疗效确证性试验选择最佳使用剂量。次要目的：（1）比较肌内注射CBL8851注射液与破伤风人免疫球蛋白在中国成年志愿者中的安全性；（2）评价肌内注射CBL8851注射液在中国成年志愿者中的免疫原性特征。

开始日期-

申办/合作机构

长春百克生物科技股份公司

CTR20241199 / Recruiting临床1期

多中心、随机、盲法、对照评价全人源抗破伤风毒素单克隆抗体A82/B86注射液组合制剂的安全性、耐受性、药动学、药效学和免疫原性的I/II期临床试验

Ia（单独给药阶段）主要目的：评价单次肌内注射不同剂量CBL8851注射液在中国健康成年志愿者中的安全性、耐受性。次要目的：（1）评价单次肌内注射不同剂量CBL8851注射液在中国健康成年志愿者中的药代动力学特征；（2）评价单次肌内注射不同剂量CBL8851注射液在中国健康成年志愿者中的药效学特征；（3）评价单次肌内注射不同剂量CBL8851注射液在中国健康成年志愿者中的免疫原性特征。 Ib（药物相互作用阶段）主要目的：评价肌内注射CBL8851注射液联合吸附破伤风疫苗在中国健康成年志愿者中的安全性、耐受性。次要目的：（1）评价肌内注射CBL8851注射液联合吸附破伤风疫苗在中国健康成年志愿者中的药效学特征，评估药物相互作用；（2）评价肌内注射CBL8851注射液联合吸附破伤风疫苗在中国健康成年志愿者中的药代动力学特征；（3）评价肌内注射CBL8851注射液联合吸附破伤风疫苗在中国健康成年志愿者中的免疫原性特征。

开始日期2024-04-30

申办/合作机构

长春百克生物科技股份公司

NCT06360250 / Not yet recruiting早期临床1期

Multicenter, Randomized, Blinded, Controlled Phase I / Clinical Trial Evaluating the Safety, Tolerability, Pharmacokinetics, Pharmacodynamics, and Immunogenicity of the Fully Human Anti-tetanus Toxin Monoclonal Antibody A82 / B86 Injection Combination

To evaluate the safety, tolerability, pharmacokinetics, pharmacodynamics, and immunogenicity of the full human anti-tetanus toxin monoclonal antibody A82 / B86 injection combination formulation

开始日期2024-04-10

申办/合作机构

长春百克生物科技股份公司

100 项与全人源抗破伤风毒素单克隆抗体A82/B86(百克生物) 相关的临床结果

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100 项与全人源抗破伤风毒素单克隆抗体A82/B86(百克生物) 相关的转化医学

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100 项与全人源抗破伤风毒素单克隆抗体A82/B86(百克生物) 相关的专利（医药）

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项与全人源抗破伤风毒素单克隆抗体A82/B86(百克生物) 相关的文献（医药）

2018-06-01·Vaccine3区 · 医学

Cooperative binding of anti-tetanus toxin monoclonal antibodies: Implications for designing an efficient biclonal preparation to prevent tetanus toxin intoxication

3区 · 医学

Article

作者: Stojanovic, Marijana ; Filipovic, Ana ; Miljkovic, Radmila ; Lukic, Ivana ; Marinkovic, Emilija ; Inic-Kanada, Aleksandra

Oligoclonal combinations of several monoclonal antibodies (MAbs) are being considered for the treatment of various infectious pathologies. These combinations are less sensitive to antigen structural changes than individual MAbs; at the same time, their characteristics can be more efficiently controlled than those of polyclonal antibodies. The main goal of this study was to evaluate the binding characteristics of six biclonal equimolar preparations (BEP) of tetanus toxin (TeNT)-specific MAbs and to investigate how the MAb combination influences the BEPs' protective capacity. We show that a combination of TeNT-specific MAbs, which not only bind TeNT but also exert positive cooperative effects, results in a BEP with superior binding characteristics and protective capacity, when compared with the individual component MAbs. Furthermore, we show that a MAb with only partial protective capacity but positive effects on the binding of the other BEP component can be used as a valuable constituent of the BEP.

2017-01-17·Human Antibodies

Construction of human anti-tetanus single-chain variable fragment applying SYMPLEX technology

Article

作者: Bazaz, Masoumeh ; Nejad, Hamideh Rouhani ; Esmati, Laya ; Mehrabadi, Jalil Fallah

BACKGROUNDHuman monoclonal antibodies are important molecules in clinical research. Current Limitations of mAb technologies namely instability of immortalized B-cell line and probability of forming unusual VH-VL pairs in phage-display method led to mAbs technology based on single plasma cell called ``SYMPLEX''.OBJECTIVEIn this method, cognate VH and VL fragments generated from individual antibody genes exactly the same as natural ones.METHODSPBMCs of whole blood of an immunized candidate was used as a resource of rearranged Ab genes. Then flow-cytometric screening was performed to isolate VH and VL from PBMCs. Various VH and VLκ were amplified by six pairs of primers. Overlap Extension PCR was accomplished to link VH and Vκ regions. ScFv inserted into T-vector and its sequence was determined and eventually analyzed by using blast analysis tools.RESULTSElectrophoresis results indicated that VH and VL fragments were separately amplified by PCR with a length of about 400bp and linked through OE-PCR. Hence, ScFv, which was approximately 800bp in size, was constructed then sequencing and BLASTn results of the ScFv fragment consequently proved the accuracy.CONCLUSIONResults showed 88% similarity to available sequences in mentioned databank. ScFv was ultimately inserted into expression vector for producing recombinant human anti-tetanus mAb.

2014-02-01·Human Vaccines & Immunotherapeutics3区 · 医学

Comparativein vitroandin vivoassessment of toxin neutralization by anti-tetanus toxin monoclonal antibodies

3区 · 医学

Article

作者: Rabbani, Hodjatallah ; Jeddi-Tehrani, Mahmood ; Khosravi-Eghbal, Roya ; Yousefi, Mehdi ; Shokri, Fazel ; Reza Mahmoudi, Ahmad

Tetanus is caused by the tetanus neurotoxin (TeNT), a 150 kDa single polypeptide molecule which is cleaved into an active two-chain molecule composed of a 50 kDa N-terminal light (L) and a 100 kDa C-terminal heavy (H) chains. Recently, extensive effort has focused on characterization of TeNT binding receptors and toxin neutralization by monoclonal antibodies (mAbs). Toxin binding inhibition and neutralization is routinely assessed either in vitro by the ganglioside GT1b binding inhibition assay or in vivo using an animal model. These two assay systems have never been compared. In the present study, we report characterization of eleven mAbs against different parts of TeNT. The toxin inhibitory and neutralization activity of the mAbs was assessed in vitro and in vivo respectively. Our data demonstrated that seven mAbs bind to fragment C of the heavy chain, two mAbs react with the light chain, one mAb recognizes both chains and one mAb reacts with neither light chain nor fragment C. Six fragment C specific mAbs were able to inhibit TeNT binding to GT1b ganglioside in vitro but three failed to neutralize the toxin in vivo. One in vitro inhibitory mAb (1F3E3) was found to synergize with the in vivo neutralizing mAbs to reduce toxin lethal activity in vivo. Sequencing of the immunoglobulin heavy and light chain variable region genes revealed that the three in vivo neutralizing mAbs were derived from a common origin. Altogether, our data suggests that fragment C specific mAbs contribute to toxin neutralization in both systems, though some of the GT1b binding inhibitory mAbs may not be able to neutralize TeNT in vivo.

100 项与全人源抗破伤风毒素单克隆抗体A82/B86(百克生物) 相关的药物交易

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