ArticleInsect biochemistry and molecular biology2015
Targeted glycoengineering extends the protein N-glycosylation pathway in the silkworm silk gland.
Article in Insect biochemistry and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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.
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.
Who cites it
11 citing papers in PubMed, 35 citations in OpenAlex.
- N-Glycoengineering of insect cells for tri-antennary N-glycan biosynthesis.Scientific reports · 2026Article
- Robust and Reproducible Monoclonal Antibody Production Using a Transgenic Silkworm System.International journal of molecular sciences · 2025Article
- Applications of recombinant type III collagen in tissue engineering.Biomedical engineering online · 2025Review
- Modifying Naturally Occurring, Nonmammalian-Sourced Biopolymers for Biomedical Applications.ACS biomaterials science & engineering · 2024Review
- Insights into the quality of recombinant proteins produced by two different Bombyx mori expression systems.Scientific reports · 2022Article
- Let's talk about sexes: sex-related N-glycosylation in ecologically important invertebrates.Glycoconjugate journal · 2020Review
- Isomeric Separation and Recognition of Anionic and Zwitterionic N-glycans from Royal Jelly Glycoproteins.Molecular & cellular proteomics : MCP · 2018Article
- CRISPR-Cas9 vectors for genome editing and host engineering in the baculovirus-insect cell system.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Increasing the yield of middle silk gland expression system through transgenic knock-down of endogenous sericin-1.Molecular genetics and genomics : MGG · 2017Article
- N-Glycan Modification of a Recombinant Protein via Coexpression of Human Glycosyltransferases in Silkworm Pupae.Scientific reports · 2017Article
- Protein N-glycosylation and N-glycan trimming are required for postembryonic development of the pest beetle Tribolium castaneum.Scientific reports · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The silkworm silk glands are powerful secretory organs that can produce and secrete proteins at high levels. As such, it has been suggested that the biosynthetic and secretory power of the silk gland can be harnessed to produce and secrete recombinant proteins in tight or loose association with silk fibers. However, the utility of the silkworm platform is constrained by the fact that it has a relatively primitive protein N-glycosylation pathway, which produces relatively simple insect-type, rather than mammalian-type N-glycans. In this study, we demonstrate for the first time that the silk gland protein N-glycosylation pathway can be glycoengineered. We accomplished this by using a dual piggyBac vector encoding two distinct mammalian glycosyltransferases under the transcriptional control of a posterior silk gland (PSG)-specific promoter. Both mammalian transgenes were expressed and each mammalian N-glycan processing activity was induced in transformed silkworm PSGs. In addition, the transgenic animals produced endogenous glycoproteins containing significant proportions of mammalian-type, terminally galactosylated N-glycans, while the parental animals produced none. This demonstration of the ability to glycoengineer the silkworm extends its potential utility as a recombinant protein production platform.
Indexed as
Identifiers
What OpenQuestion holds
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.