ArticleThe Journal of biological chemistry2011
Baculovirus envelope protein ODV-E66 is a novel chondroitinase with distinct substrate specificity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 45 citations in OpenAlex.
- Engineering Chondroitinase-Free Baculovirus-Insect Cell Expression System for Efficient Synthesis of Chondroitin Sulphates.Microbial biotechnology · 2026Article
- Article
- A novel and diverse family of filamentous DNA viruses associated with parasitic wasps.Virus evolution · 2024Article
- Effects of Mixed Baculovirus Infections in Biological Control: A Comprehensive Historical and Technical Analysis.Viruses · 2023Review
- Substrate specificity of Chondroitinase ABC I based on analyses of biochemical reactions and crystal structures in complex with disaccharides.Glycobiology · 2021Article
- MdBVe46 is an envelope protein that is required for virion formation by Microplitis demolitor bracovirus.The Journal of general virology · 2021Article
- Mosaic genome evolution and phylogenetics of Chrysodeixis includens nucleopolyhedrovirus (ChinNPV) and virulence of seven new isolates from the Brazilian states of Minas Gerais and Mato Grosso.Archives of virology · 2021Article
- Enzymatic Synthesis of Chondroitin Sulfate E to Attenuate Bacteria Lipopolysaccharide-Induced Organ Damage.ACS central science · 2020Article
- Research and Application of Chondroitin Sulfate/Dermatan Sulfate-Degrading Enzymes.Frontiers in cell and developmental biology · 2020Review
- Cross-talking between baculoviruses and host insects towards a successful infection.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019Article
- Prion-like Domains in Eukaryotic Viruses.Scientific reports · 2018Article
- Article
- Enzymatic Synthesis of Homogeneous Chondroitin Sulfate Oligosaccharides.Angewandte Chemie (International ed. in English) · 2017Article
- Genome Sequencing of the Behavior Manipulating Virus LbFV Reveals a Possible New Virus Family.Genome biology and evolution · 2016Article
- Genome Sequencing and Analysis of Catopsilia pomona nucleopolyhedrovirus: A Distinct Species in Group I Alphabaculovirus.PloS one · 2016Article
- Proteomic Analysis of Mamestra Brassicae Nucleopolyhedrovirus Progeny Virions from Two Different Hosts.PloS one · 2016Article
- Chondroitin Lyase from a Marine Arthrobacter sp. MAT3885 for the Production of Chondroitin Sulfate Disaccharides.Marine biotechnology (New York, N.Y.) · 2015Article
- Reaching the melting point: Degradative enzymes and protease inhibitors involved in baculovirus infection and dissemination.Virology · 2015Review
- Autographa californica Nucleopolyhedrovirus Ac76: a dimeric type II integral membrane protein that contains an inner nuclear membrane-sorting motif.Journal of virology · 2014Article
- The baculovirus core gene ac83 is required for nucleocapsid assembly and per os infectivity of Autographa californica nucleopolyhedrovirus.Journal of virology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chondroitin sulfate is a linear polysaccharide of alternating D-glucuronic acid and N-acetyl-D-galactosamine residues with sulfate groups at various positions of the sugars. It interacts with and regulates cytokine and growth factor signal transduction, thus influencing development, organ morphogenesis, inflammation, and infection. We found chondroitinase activity in medium conditioned by baculovirus-infected insect cells and identified a novel chondroitinase. Sequence analysis revealed that the enzyme was a truncated form of occlusion-derived virus envelope protein 66 (ODV-E66) of Autographa californica nucleopolyhedrovirus. The enzyme was a novel chondroitin lyase with distinct substrate specificity. The enzyme was active over a wide range of pH (pH 4-9) and temperature (30-60 °C) and was unaffected by divalent metal ions. The ODV-E66 truncated protein digested chondroitin most efficiently followed by chondroitin 6-sulfate. It degraded hyaluronan to a minimal extent but did not degrade dermatan sulfate, heparin, and N-acetylheparosan. Further analysis using chemo-enzymatically synthesized substrates revealed that the enzyme specifically acted on glucuronate residues in non-sulfated and chondroitin 6-sulfate structures but not in chondroitin 4-sulfate structures. These results suggest that this chondroitinase is useful for detailed structural and compositional analysis of chondroitin sulfate, preparation of specific chondroitin oligosaccharides, and study of baculovirus infection mechanism.
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