ArticleAMB Express2017
Expressing anti-HIV VRC01 antibody using the murine IgG1 secretion signal in Pichia pastoris.
Article in AMB Express, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- The landscape of antibody production systems: recombinant expression for research, diagnostics and therapy.Frontiers in bioengineering and biotechnology · 2026Review
- Advancing recombinant protein expression in Komagataella phaffii: opportunities and challenges.FEMS yeast research · 2025Review
- Evaluation of reference genes for transcript analyses in Komagataella phaffii (Pichia pastoris).Fungal biology and biotechnology · 2023Article
- Differential role of segments of α-mating factor secretion signal in Pichia pastoris towards granulocyte colony-stimulating factor emerging from a wild type or codon optimized copy of the gene.Microbial cell factories · 2020Article
- NS1 Recombinant Proteins Are Efficiently Produced inDiagnostics (Basel, Switzerland) · 2020Article
- Carbon metabolism influenced for promoters and temperature used in the heterologous protein production using Pichia pastoris yeast.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2018Review
- A systematic analysis of the expression of the anti-HIV VRC01 antibody in Pichia pastoris through signal peptide optimization.Protein expression and purification · 2018Article
- A streamlined cloning workflow minimising the time-to-strain pipeline for Pichia pastoris.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The use of the recombinant expression platform Pichia pastoris to produce pharmaceutically important proteins has been investigated over the past 30 years. Compared to mammalian cultures, expression in P. pastoris is cheaper and faster, potentially leading to decreased costs and process development times. Product yields depend on a number of factors including the secretion signal chosen for expression, which can influence the host cell response to recombinant protein production. VRC01, a broadly neutralising anti-HIV antibody, was expressed in P. pastoris, using the methanol inducible AOX1 promoter for both the heavy and light chains. Titre reached up to 3.05 μg mL
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Registered trials
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.