Evidence map›Paper›PMID 39964430›Full record

ArticleAnalytical and bioanalytical chemistry2025

Studying host cell protein based on 2D nano-LC-MS/MS: comparison between the removal and the reservation of the main antibody components.

Xinling Cui, Lei Li, Ming Li, Wantao Ying, Jinlan Cheng, Ling Lin, Wei Mi, Zhishang Hu

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Analytical and bioanalytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
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

8 authors.

Xinling Cui *Division of Chemical Metrology and Analytical Science, National Institute of Metrology, Beijing, 100029, China.
Lei Li *Central Laboratory, Capital Medical University, Beijing, 100069, China.
Ming LiDivision of Chemical Metrology and Analytical Science, National Institute of Metrology, Beijing, 100029, China.
Wantao YingState Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Proteome Research Center, Beijing Institute of Lifeomics, Beijing, 102206, China.
Jinlan ChengDivision of Chemical Metrology and Analytical Science, National Institute of Metrology, Beijing, 100029, China.
Ling LinDepartment of Bioengineering, Beijing Technology and Business University, Beijing, 100048, China. linling@btbu.edu.cn.
Wei MiDivision of Chemical Metrology and Analytical Science, National Institute of Metrology, Beijing, 100029, China. miwei@nim.ac.cn.
Zhishang HuDivision of Chemical Metrology and Analytical Science, National Institute of Metrology, Beijing, 100029, China. huz@nim.ac.cn.

Funding

Advanced Talents of Beijing Technology and Business University 19008021179Beijing Nova Program 20220484055National Key R&D Program of China 2021YFF0600702National Key Research and Development Program of China 2022YFD2101502National Natural Science Foundation of China 82073816Scientific Fund Project of the National Institute of Metrology of China AKYZD2114-1
6 · The paper itself

Abstract

Host cell proteins (HCPs) are process-related impurities that are generated by the host organism, and are typically present at low levels in therapeutic monoclonal antibody (mAb) and other recombinant biopharmaceutical products. Firstly, a high-pH-low-pH "two-dimensional" reversed-phase nano-LC-MS/MS label-free quantification (2D nano-LC-MS/MS LFQ) method with a robust stability (CV% < 20%) was developed. Subsequently, this study developed economical hexamer ligand (HWRGWV) magnetic beads (HLMB), which aim to improve the sensitivity and reliability of HCP detection and has an IgG antibody-binding capacity similar to that of Protein A. In turn, the HCP study based on 2D nano-LC-MS/MS, a comparison between the removal and the reservation of the main antibody components was developed, and the qualitative and quantitative results were compared among HLMB/Protein A depletion and other two pretreatment processes. Results of this study indicated that after using HLMB/ProA material for antibody primary component removal, the content of HCPs in the elution buffer (associated or co-purified with the antibody) was significantly higher than that in the flow-through. In total, 22 kinds of HCPs were co-identified in HLMB eluent and ProA eluent, in which most of the HCPs exhibited weak alkalinity, while the sensitivity of HCPs identified with a low molecular weight (ranging from 13 to 21 kDa) was as low as 0.1 ppm. Together, this study established an economical and effective approach to comprehensively evaluate HCPs in antibodies, while also globally presenting the impact of major antibody components on the qualitative and quantitative analyses of HCPs.

Indexed as

Antibodies, MonoclonalProteinsTandem Mass SpectrometryAnimalsCHO CellsChromatography, LiquidCricetulusImmunoglobulin GNanotechnologyAntibodies, MonoclonalImmunoglobulin GProteinsHexamer ligand magnetism beads (HLMB)Host cell proteinsMAb removalMAb retainingProA magnetism beads

Identifiers

PMID39964430

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Registered trials

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