N -acetyl galactosamine is part of the receptor in insect gut epithelia that recognizes an insecticidal protein from Bacillus thuringiensis
1991; Royal Society; Volume: 245; Issue: 1312 Linguagem: Inglês
10.1098/rspb.1991.0084
ISSN1471-2954
AutoresBarbara H. Knowles, Peter J. Knight, David J. Ellar,
Tópico(s)Entomopathogenic Microorganisms in Pest Control
ResumoRestricted accessMoreSectionsView PDF ToolsAdd to favoritesDownload CitationsTrack Citations ShareShare onFacebookTwitterLinked InRedditEmail Cite this article Knowles Barbara H. , Knight Peter J. K. and Ellar David J. 1991N-acetyl galactosamine is part of the receptor in insect gut epithelia that recognizes an insecticidal protein from Bacillus thuringiensisProc. R. Soc. Lond. B.24531–35http://doi.org/10.1098/rspb.1991.0084SectionRestricted accessArticleN-acetyl galactosamine is part of the receptor in insect gut epithelia that recognizes an insecticidal protein from Bacillus thuringiensis Barbara H. Knowles Google Scholar Find this author on PubMed Search for more papers by this author , Peter J. K. Knight Google Scholar Find this author on PubMed Search for more papers by this author and David J. Ellar Google Scholar Find this author on PubMed Search for more papers by this author Barbara H. Knowles Google Scholar Find this author on PubMed , Peter J. K. Knight Google Scholar Find this author on PubMed and David J. Ellar Google Scholar Find this author on PubMed Published:22 July 1991https://doi.org/10.1098/rspb.1991.0084AbstractProteins synthesized by the bacterium Bacillus thuringiensis are potent insecticides. When ingested by susceptible larvae they rapidly lyse epithelial cells lining the midgut. In vitro the toxins lyse certain insect cell lines and show saturable, high-affinity binding to brush-border membrane vesicles (bbmvs) prepared from insect midguts. We observed that the sugar V-acetyl galactosamine (GalNAc) specifically decreased the cytolytic activity of a CrylA (c) toxin towards Choristoneura fumiferana CF1 cells, completely abolished toxin binding to Manduca sexta bbmvs, partially inhibited binding to Heliothis virescens bbmvs and had no apparent effect on binding to Pieris brassicae bbmvs. In ligand blotting experiments the toxin bound proteins of 120 kDa in M . sexta, 125 kDa in P. brassicae and numerous proteins in H. zea. Toxin binding to these proteins was specifically inhibited by GalNAc. The toxin binding proteins of M . sexta and H. zea also bound the lectin soybean agglutinin. Taken together these findings suggest that V-acetyl galactosamine might be a component of a CrylA (c) toxin receptor of CF1 cells and of at least two of the insects tested.FootnotesThis text was harvested from a scanned image of the original document using optical character recognition (OCR) software. As such, it may contain errors. Please contact the Royal Society if you find an error you would like to see corrected. Mathematical notations produced through Infty OCR. Previous ArticleNext Article VIEW FULL TEXT DOWNLOAD PDF FiguresRelatedReferencesDetailsCited by Mishra R, Arora A, Jiménez J, dos Santos Tavares C, Banerjee R, Panneerselvam S and Bonning B (2022) Bacteria-derived pesticidal proteins active against hemipteran pests, Journal of Invertebrate Pathology, 10.1016/j.jip.2022.107834, 195, (107834), Online publication date: 1-Nov-2022. Alam I, Batool K, Idris A, Tan W, Guan X and Zhang L (2022) Role of Lectin in the Response of Aedes aegypti Against Bt Toxin, Frontiers in Immunology, 10.3389/fimmu.2022.898198, 13 Pohare M, Wagh S and Udayasuriyan V (2021) Bacillus thuringiensis as Potential Biocontrol Agent for Sustainable Agriculture Current Trends in Microbial Biotechnology for Sustainable Agriculture, 10.1007/978-981-15-6949-4_18, (439-468), . 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This Issue22 July 1991Volume 245Issue 1312 Article InformationDOI:https://doi.org/10.1098/rspb.1991.0084PubMed:1658805Published by:Royal SocietyPrint ISSN:0962-8452Online ISSN:1471-2954History: Manuscript received21/03/1991Manuscript accepted26/04/1991Published online01/01/1997Published in print22/07/1991 License:Scanned images copyright © 2017, Royal Society Citations and impact Large datasets are available through Proceedings B's partnership with Dryad
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