Literature DB >> 34687006

Micro-Heterogeneity of Antibody Molecules.

Yusuke Mimura1, Radka Saldova2,3, Yuka Mimura-Kimura4, Pauline M Rudd2,5, Roy Jefferis6.   

Abstract

Therapeutic monoclonal antibodies (mAbs) are mostly of the IgG class and constitute highly efficacious biopharmaceuticals for a wide range of clinical indications. Full-length IgG mAbs are large proteins that are subject to multiple posttranslational modifications (PTMs) during biosynthesis, purification, or storage, resulting in micro-heterogeneity. The production of recombinant mAbs in nonhuman cell lines may result in loss of structural fidelity and the generation of variants having altered stability, biological activities, and/or immunogenic potential. Additionally, even fully human therapeutic mAbs are of unique specificity, by design, and, consequently, of unique structure; therefore, structural elements may be recognized as non-self by individuals within an outbred human population to provoke an anti-therapeutic/anti-drug antibody (ATA/ADA) response. Consequently, regulatory authorities require that the structure of a potential mAb drug product is comprehensively characterized employing state-of-the-art orthogonal analytical technologies; the PTM profile may define a set of critical quality attributes (CQAs) for the drug product that must be maintained, employing quality by design parameters, throughout the lifetime of the drug. Glycosylation of IgG-Fc, at Asn297 on each heavy chain, is an established CQA since its presence and fine structure can have a profound impact on efficacy and safety. The glycoform profile of serum-derived IgG is highly heterogeneous while mAbs produced in mammalian cells in vitro is less heterogeneous and can be "orchestrated" depending on the cell line employed and the culture conditions adopted. Thus, the gross structure and PTM profile of a given mAb, established for the drug substance gaining regulatory approval, have to be maintained for the lifespan of the drug. This review outlines our current understanding of common PTMs detected in mAbs and endogenous IgG and the relationship between a variant's structural attribute and its impact on clinical performance.
© 2021. The Author(s), under exclusive license to Springer Nature Switzerland AG.

Entities:  

Keywords:  Critical quality attributes; Glycoforms; Glycoproteins; Oligosaccharides; Posttranslational modifications; Recombinant antibody therapeutics

Mesh:

Substances:

Year:  2021        PMID: 34687006     DOI: 10.1007/978-3-030-76912-3_1

Source DB:  PubMed          Journal:  Exp Suppl        ISSN: 1664-431X


  106 in total

1.  Analysis of lysine clipping of a humanized Lewis-Y specific IgG antibody and its relation to Fc-mediated effector function.

Authors:  Bernhard Antes; Sabine Amon; Andreas Rizzi; Susi Wiederkum; Manuela Kainer; Oliver Szolar; Markus Fido; Ralf Kircheis; Andreas Nechansky
Journal:  J Chromatogr B Analyt Technol Biomed Life Sci       Date:  2007-01-26       Impact factor: 3.205

2.  The effect of sucrose hydrolysis on the stability of protein therapeutics during accelerated formulation studies.

Authors:  Douglas D Banks; David M Hambly; Joanna L Scavezze; Christine C Siska; Nicole L Stackhouse; Himanshu S Gadgil
Journal:  J Pharm Sci       Date:  2009-12       Impact factor: 3.534

3.  Removal of cysteinylation from an unpaired sulfhydryl in the variable region of a recombinant monoclonal IgG1 antibody improves homogeneity, stability, and biological activity.

Authors:  Douglas D Banks; Himanshu S Gadgil; Gary D Pipes; Pavel V Bondarenko; Vipa Hobbs; Joanna L Scavezze; Jun Kim; Xu-Rong Jiang; Venkat Mukku; Thomas M Dillon
Journal:  J Pharm Sci       Date:  2008-02       Impact factor: 3.534

4.  Recombinant antibody color resulting from advanced glycation end product modifications.

Authors:  Margaret Butko; Hilary Pallat; Armando Cordoba; X Christopher Yu
Journal:  Anal Chem       Date:  2014-09-11       Impact factor: 6.986

Review 5.  Determination of critical quality attributes for monoclonal antibodies using quality by design principles.

Authors:  Nadja Alt; Taylor Y Zhang; Paul Motchnik; Ron Taticek; Valerie Quarmby; Tilman Schlothauer; Hermann Beck; Thomas Emrich; Reed J Harris
Journal:  Biologicals       Date:  2016-07-25       Impact factor: 1.856

Review 6.  Analytical comparability study of recombinant monoclonal antibody therapeutics.

Authors:  Alexandre Ambrogelly; Stephen Gozo; Amit Katiyar; Shara Dellatore; Yune Kune; Ram Bhat; Joanne Sun; Ning Li; Dongdong Wang; Christine Nowak; Alyssa Neill; Gomathinayagam Ponniah; Cory King; Bruce Mason; Alain Beck; Hongcheng Liu
Journal:  MAbs       Date:  2018-03-20       Impact factor: 5.857

7.  Immunological studies on glycated human IgG.

Authors:  Saman Ahmad; Asif Ali
Journal:  Life Sci       Date:  2012-05-23       Impact factor: 5.037

8.  Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I.

Authors:  Adam W Barb; Evan K Brady; James H Prestegard
Journal:  Biochemistry       Date:  2009-10-20       Impact factor: 3.162

9.  Impact of methionine oxidation on the binding of human IgG1 to Fc Rn and Fc gamma receptors.

Authors:  Andrea Bertolotti-Ciarlet; Weirong Wang; Rebecca Lownes; Pavlo Pristatsky; Yulin Fang; Troy McKelvey; Yingzhe Li; Yunsong Li; James Drummond; Thomayant Prueksaritanont; Josef Vlasak
Journal:  Mol Immunol       Date:  2009-03-06       Impact factor: 4.407

10.  Aggregation of biopharmaceuticals in human plasma and human serum: implications for drug research and development.

Authors:  Tudor Arvinte; Caroline Palais; Erin Green-Trexler; Sonia Gregory; Henryk Mach; Chakravarthy Narasimhan; Mohammed Shameem
Journal:  MAbs       Date:  2013-04-09       Impact factor: 5.857

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.