Evidence map›Paper›PMID 27610742›Full record

ArticlemAbs

Precise quantification of mixtures of bispecific IgG produced in single host cells by liquid chromatography-Orbitrap high-resolution mass spectrometry.

Yiyuan Yin, Guanghui Han, Jianhui Zhou, Michael Dillon, Luke McCarty, Lou Gavino, Diego Ellerman, Christoph Spiess, Wendy Sandoval, Paul J Carter

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Generation of Bispecific Antibodies Using FAST-Ig™.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. High-throughput antibody screening from complex matrices using intact protein electrospray mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Article
  10. Engineering IgG-Like Bispecific Antibodies-An Overview.Antibodies (Basel, Switzerland) · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Yiyuan Yina Antibody Engineering Department , Genentech, Inc. , South San Francisco , CA , USA.
Guanghui Hanb Proteomics and Biologics Resources Department , Genentech, Inc. , South San Francisco , CA , USA.
Jianhui Zhoua Antibody Engineering Department , Genentech, Inc. , South San Francisco , CA , USA.
Michael Dillona Antibody Engineering Department , Genentech, Inc. , South San Francisco , CA , USA.
Luke McCartyc Protein Chemistry and Structural Biology Department , Genentech, Inc. , South San Francisco , CA , USA.
Lou Gavinod Chromatography and Mass Spectrometry Division, Thermo Fisher Scientific , San Jose , CA , USA.
Diego Ellermanc Protein Chemistry and Structural Biology Department , Genentech, Inc. , South San Francisco , CA , USA.
Christoph Spiessa Antibody Engineering Department , Genentech, Inc. , South San Francisco , CA , USA.
Wendy Sandovalb Proteomics and Biologics Resources Department , Genentech, Inc. , South San Francisco , CA , USA.
Paul J Cartera Antibody Engineering Department , Genentech, Inc. , South San Francisco , CA , USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bispecific IgG are heterotetramers comprising 2 pairs of heavy and light chains. Co-expression of the 4 component chains in a single host cell typically yields the desired bispecific IgG plus up to 9 additional incorrect chain pairings. Several protein engineering strategies have been reported to facilitate the heterodimerization of antibody heavy chains or cognate pairing of antibody heavy and light chains. These technologies have been used to direct the efficient assembly of bispecific IgG in single host cells and minimize unwanted chain pairings. When purifying bispecific IgGs, the identification and quantification of low levels of closely related IgG contaminants are substantial analytical challenges. Here we have developed a robust high-throughput method for quantitative analysis of bispecific IgG preparations using novel online liquid chromatography in conjunction with an extended mass range Orbitrap-based high-resolution mass spectrometer. A mathematical method was developed to estimate the yields of the 2 isobaric species, namely the desired bispecific IgG and the light chain-scrambled IgG. The analytical methods described herein are anticipated to be broadly applicable to the development of bispecific IgG as drugs and potentially to other complex next-generation biotherapeutics.

Indexed as

Models, TheoreticalAntibodies, BispecificChromatography, High Pressure LiquidChromatography, LiquidHigh-Throughput Screening AssaysHumansImmunoglobulin GMass SpectrometryProtein EngineeringAntibodies, BispecificImmunoglobulin GBispecific antibodybispecific IgG quantificationDNA ratioshigh-resolution mass spectrometrysingle host expression

Identifiers

PMID27610742
PMCPMC5098441

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.