Backbone NMR assignment of the yeast expressed Fab fragment of the NISTmAb reference antibody

被引:4
|
作者
Solomon, Tsega L. L. [1 ,2 ]
Chao, Kinlin [1 ,2 ]
Gingras, Genevieve [3 ]
Aubin, Yves [3 ]
O'Dell, William B. B. [1 ,2 ]
Marino, John P. P. [1 ,2 ]
Brinson, Robert G. G. [1 ,2 ]
机构
[1] Natl Inst Stand & Technol, Inst Biosci & Biotechnol Res, Rockville, MD 20850 USA
[2] Univ Maryland, Rockville, MD 20850 USA
[3] Hlth Canada, Ctr Oncol Radiopharmaceut & Res, Biol & Radiotherapeut Drugs Directorate, 251 Sir Frederick Banting Driveway, Ottawa, ON K1A 0K9, Canada
关键词
Backbone assignments; Fab domain; NISTmAb; Biologics; C-13; DYNAMICS; H-1;
D O I
10.1007/s12104-023-10123-9
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The monoclonal antibody (mAb) protein class has become a primary therapeutic platform for the production of new life saving drug products. MAbs are comprised of two domains: the antigen-binding fragment (Fab) and crystallizable fragment (Fc). Despite the success in the clinic, NMR assignments of the complete Fab domain have been elusive, in part due to problems in production of properly folded, triply-labeled H-2,C-13,N-15 Fab domain. Here, we report the successful recombinant expression of a triply-labeled Fab domain, derived from the standard IgG1 kappa known as NISTmAb, in yeast. Using the H-2,C-13,N-15 Fab domain, we assigned 94% of the H-1, C-13, and N-15 backbone atoms.
引用
收藏
页码:75 / 81
页数:7
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