Evidence map›Paper›PMID 30402825›Full record

ArticleThe AAPS journal2018

Approaches to Resolve False Reporting in Neutralizing Antibody Assays Caused by Reagent Leaching from Affinity Capture Elution Solid Phase.

Yuhong Xiang, John Kamerud, Jean Donley, Katrina Olson, Teresa Caiazzo, Dave Yeung, Chuenlei Parng, Boris Gorovits

Abstract read
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In one paragraph

Article in The AAPS journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 40% of its field
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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. 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 at 2 institutions in 1 country.

Yuhong XiangPfizer Worldwide Research & Development, Biomedicine Design, 1 Burtt Rd., Andover, Massachusetts, 01810, USA.
John KamerudPfizer Worldwide Research & Development, Biomedicine Design, 1 Burtt Rd., Andover, Massachusetts, 01810, USA.
Jean DonleyPfizer Worldwide Research & Development, Biomedicine Design, 1 Burtt Rd., Andover, Massachusetts, 01810, USA.
Katrina OlsonPfizer Worldwide Research & Development, Biomedicine Design, 1 Burtt Rd., Andover, Massachusetts, 01810, USA.
Teresa CaiazzoPfizer Worldwide Research & Development, Biomedicine Design, 1 Burtt Rd., Andover, Massachusetts, 01810, USA.
Dave YeungTakeda Pharmaceutical Company Limited, Cambridge, Massachusetts, USA.
Chuenlei ParngPfizer Worldwide Research & Development, Biomedicine Design, 1 Burtt Rd., Andover, Massachusetts, 01810, USA.
Boris GorovitsPfizer Worldwide Research & Development, Biomedicine Design, 1 Burtt Rd., Andover, Massachusetts, 01810, USA. Boris.Gorovits@pfizer.com.
Pfizer (United States) · USTakeda (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insufficient drug tolerance presents a major challenge in the development of neutralizing antibody (NAb) assays for biotherapeutics. Sample pre-treatment using solid-phase extraction with acid dissociation (SPEAD) is widely reported to improve drug tolerance. In this paper, a case study is presented in which SPEAD was used in conjunction with a competitive ligand binding NAb assay format. A significant degree of biotin-drug conjugate leaching was observed resulting in the reporting of both false positive and false negative results in NAb assay. Mitigation steps have been evaluated to address drug/biotin-drug conjugate leaching. These steps included assessment of the streptavidin-coated plate in conjunction with biotin-drug conjugates at various biotin molar challenge ratios (MCR). In addition, an alternative method based on covalent capture of the drug on an aldehyde-activated plate was assessed. Both approaches were compared for the degree of drug/biotin-drug conjugate leaching during the second elution step of the SPEAD procedure. Moreover, the impact of various conditions on the assay performance was assessed, including elution pH, sample incubation time, and biotin MCR. For the covalent drug capture method, capture conditions were evaluated. Optimized conditions in both streptavidin capture and covalent capture methods enabled a significant reduction of drug/biotin-drug conjugate leaching. A streptavidin high binding capacity approach using biotin-drug conjugate with a MCR of 50:1 was chosen as the optimal method yielding a NAb assay with a fit for purpose sensitivity (153 ng/mL) and a drug tolerance of up to 50 μg/mL with 500 ng/mL PC.

Indexed as

Antibodies, Monoclonal, HumanizedAntibodies, NeutralizingBiological ProductsBiotinChemistry, PharmaceuticalChromatography, AffinityDrug ToleranceFalse Negative ReactionsFalse Positive ReactionsHumansIndicators and ReagentsNeutralization TestsSolid Phase ExtractionStreptavidinSuccinimidesAntibodies, Monoclonal, HumanizedAntibodies, NeutralizingBiological ProductsBiotinIndicators and ReagentsStreptavidinSuccinimidessulfo-N-hydroxysuccinimide-biotinACEanti-drug antibodybiotin-drug conjugate/drug leachingdrug toleranceimmunogenicityneutralizing antibodysample pre-treatmentSPEAD

Identifiers

PMID30402825
OpenAlexW2899795005

What OpenQuestion holds

Textmetadata
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.