Evidence map›Paper›PMID 30502324›Full record

ArticleJournal of immunological methods2019

Production of a recombinant monoclonal antibody to Herpes Simplex Virus glycoprotein D for immunoaffinity purification of tagged proteins.

Sara M O'Rourke, Bin Yu, Javier F Morales, Chelsea M Didinger, David L Alexander, Christopher Vollmers, Phillip W Berman

Open access · greenAbstract read
In one paragraph

Article in Journal of immunological methods, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 31% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

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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

7 authors at 1 institution in 1 country.

Sara M O'RourkeDepartment of Biomolecular Engineering, The University of California at Santa Cruz, Santa Cruz, CA, USA.
Bin YuDepartment of Biomolecular Engineering, The University of California at Santa Cruz, Santa Cruz, CA, USA; Askgene Pharma, Inc., Camarillo, CA 93021, USA.
Javier F MoralesDepartment of Biomolecular Engineering, The University of California at Santa Cruz, Santa Cruz, CA, USA; Eureka Therapeutics, Emeryville, CA 94608, USA.
Chelsea M DidingerDepartment of Biomolecular Engineering, The University of California at Santa Cruz, Santa Cruz, CA, USA.
David L AlexanderDepartment of Biomolecular Engineering, The University of California at Santa Cruz, Santa Cruz, CA, USA.
Christopher VollmersDepartment of Biomolecular Engineering, The University of California at Santa Cruz, Santa Cruz, CA, USA.
Phillip W BermanDepartment of Biomolecular Engineering, The University of California at Santa Cruz, Santa Cruz, CA, USA. Electronic address: pwb@soe.ucsc.edu.
University of California, Santa Cruz · US

Funding

Re-engineering gp120 to include glycan-dependent epitopesR01AI113893 · NIAID · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI BERMAN, PHILLIP WAYNE · 2014 to 2017
$4.2M
HIV Variation in Injection Drug Users: Mapping Broadly Neutralizing AntibodiesR01DA026801 · NIDA · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI BERMAN, PHILLIP WAYNE · 2009 to 2013
$3.2M
Refocusing the Immune Response to the HIV Envelope GlycoproteinR01AI089378 · NIAID · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI BERMAN, PHILLIP WAYNE · 2010 to 2013
$3.1M
NIAID NIH HHS R01 AI089378NIAID NIH HHS R01 AI113893NIDA NIH HHS R01 DA026801
6 · The paper itself

Abstract

We have developed a stable Chinese Hamster Ovary (CHO) cell line for the production of a recombinant monoclonal antibody (mAb) to a short protein sequence derived from the N-terminus of human herpes simplex virus type 1 glycoprotein D (HSV-1 gD). The antibody (designated r34.1) provides a useful tool for the immunoaffinity purification of HSV-1 gD tagged proteins, and provides a generic purification system by which various proteins and peptides can be purified. Recombinant 34.1 was assembled using cDNA derived from a HSV-1 gD specific murine hybridoma engineered to encode a full-length IgG molecule. Antibody expression cassettes were transfected into CHO-S cells, and a stable cell-line expressing up to 500 mg/L of antibody, isolated. Affinity purified r34.1 exhibited nanomolar affinity for its cognate ligand, and is stable throughout multiple cycles of immunoaffinity purification involving ligand binding at neutral pH, followed by acid elution. The HSV-1 gD tag expression and purification strategy has been used to enhance the secretion and purification of several vaccine immunogens including HIV envelope protein rgp120s, but the protocol has potential for generic application.

Indexed as

AnimalsAntibodies, Monoclonal, Murine-DerivedAntibodies, ViralCHO CellsCricetulusHerpesvirus 1, HumanHumansMiceRecombinant ProteinsViral Envelope ProteinsAntibodies, Monoclonal, Murine-DerivedAntibodies, Viralglycoprotein D, Human herpesvirus 1Recombinant ProteinsViral Envelope ProteinsAntibodiesCHO cellsHIV-1 vaccineImmunoaffinity chromatography

Identifiers

PMID30502324
PMCPMC7501881
OpenAlexW2902967814

What OpenQuestion holds

Textmetadata
LicenceTDM
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.