ArticleThe Journal of biological chemistry2008
A fused lobes gene encodes the processing beta-N-acetylglucosaminidase in Sf9 cells.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.
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Who cites it
31 citing papers in PubMed, 1 synthesis or guideline pooled it, 73 citations in OpenAlex.
- Pooled it
- Isomeric diversity of GlcNAc(ManScientific reports · 2026Article
- N-Glycoengineering of insect cells for tri-antennary N-glycan biosynthesis.Scientific reports · 2026Article
- Engineering the mossFrontiers in plant science · 2025Article
- Identification and validation of protective glycoproteins inFrontiers in immunology · 2025Article
- Bioinformatic, Enzymatic, and Structural Characterization ofBiochemistry · 2024Article
- The role of glycoconjugates as receptors for insecticidal proteins.FEMS microbiology reviews · 2023Review
- Glycobiotechnology of the Insect Cell-Baculovirus Expression System Technology.Advances in biochemical engineering/biotechnology · 2021Article
- Point mutations that inactivate MGAT4D-L, an inhibitor of MGAT1 and complexThe Journal of biological chemistry · 2020Article
- 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
- N-Glycan Modification of a Recombinant Protein via Coexpression of Human Glycosyltransferases in Silkworm Pupae.Scientific reports · 2017Article
- The underestimated N-glycomes of lepidopteran species.Biochimica et biophysica acta. General subjects · 2017Article
- Humanizing glycosylation pathways in eukaryotic expression systems.World journal of microbiology & biotechnology · 2017Review
- Targeted glycoengineering extends the protein N-glycosylation pathway in the silkworm silk gland.Insect biochemistry and molecular biology · 2015Article
- Enzymatic properties and subtle differences in the substrate specificity of phylogenetically distinct invertebrate N-glycan processing hexosaminidases.Glycobiology · 2015Article
- Engineering β1,4-galactosyltransferase I to reduce secretion and enhance N-glycan elongation in insect cells.Journal of biotechnology · 2015Article
- A new insect cell glycoengineering approach provides baculovirus-inducible glycogene expression and increases human-type glycosylation efficiency.Journal of biotechnology · 2014Article
- Mutations in four glycosyl hydrolases reveal a highly coordinated pathway for rhodopsin biosynthesis and N-glycan trimming in Drosophila melanogaster.PLoS genetics · 2014Article
- A novel baculovirus vector for the production of nonfucosylated recombinant glycoproteins in insect cells.Glycobiology · 2014Article
- Impact of a human CMP-sialic acid transporter on recombinant glycoprotein sialylation in glycoengineered insect cells.Glycobiology · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Manalpha6(Manalpha3)Manbeta4GlcNAcbeta4GlcNAc-R is the core structure of the major processed protein N-glycans produced by insect cells. Ultimately, this paucimannose type structure is produced by an unusual beta-N-acetylglucosaminidase, which removes the terminal N-acetylglucosamine residue from the upstream intermediate, Manalpha6(GlcNAcbeta2Manalpha3)Manbeta4GlcNAcbeta4GlcNAc-R. Because the N-glycan processing pathways leading to the production of this intermediate are probably identical in insects and higher eukaryotes, the presence or absence of this specific, processing beta-N-acetylglucosaminidase is a key factor distinguishing the processing pathways in these two different types of organisms. Recent studies have shown that the fused lobes (fdl) gene encodes the specific, processing beta-N-acetylglucosaminidase of Drosophila melanogaster. However, there are conflicting reports on the identity of the gene encoding this enzyme in the lepidopteran insect, Spodoptera frugiperda. One has suggested that a gene alternatively designated SfGlcNAcase-3 or SfHex encodes this function, whereas another has suggested that this gene encodes a broad-spectrum beta-N-acetylglucosaminidase that functions in glycan and chitin degradation. In this study we resolved this conflict by molecularly cloning an S. frugiperda fdl ortholog (Sf-fdl) and demonstrating that it encodes a product with the substrate specificity expected of the processing beta-N-acetylglucosaminidase. Moreover, we showed that the endogenous levels of specific, processing beta-N-acetylglucosaminidase activity were significantly reduced in S. frugiperda cells engineered to express a double-stranded RNA derived from the Sf-fdl gene. These results indicate that Sf-fdl encodes the specific, processing beta-N-acetylglucosaminidase of S. frugiperda and validate our previous suggestion that the broad-spectrum beta-N-acetylglucosaminidase encoded by the SfGlcNAcase-3/SfHex gene is more likely to be involved in N-glycan and/or chitin degradation.
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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.