Invariant surface glycoprotein 65 of Trypanosoma brucei is a complement C3 receptor

Autor: Macleod, Olivia JS, Cook, Alexander D, Webb, Helena, Crow, Mandy, Burns, Roisin, Redpath, Maria, Seisenberger, Stefanie, Trevor, Camilla E, Peacock, Lori, Schwede, Angela, Kimblin, Nicola, Francisco, Amanda F, Pepperl, Julia, Rust, Steve, Voorheis, Paul, Gibson, Wendy, Taylor, Martin C, Higgins, Matthew K, Carrington, Mark

African trypanosomes are extracellular pathogens of mammals and are exposed to the adaptive and innate immune systems. Trypanosomes evade the adaptive immune response through antigenic variation, but little is known about how they interact with compo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3da2c8aeeec59f755860b44df5185f4
https://researchonline.lshtm.ac.uk/id/eprint/4667328/7/Macleod_etal_2022_Invariant-surface-glycoprotein-65-of.pdf

Invariant surface glycoprotein 65 of Trypanosoma brucei is a complement C3 receptor.

Autor: Macleod OJS; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Cook AD; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.; Kavli Institute for Nanoscience Discovery, Dorothy Crowfoot Hodgkin Building, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK., Webb H; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Crow M; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Burns R; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Redpath M; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Seisenberger S; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Trevor CE; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Peacock L; Bristol Veterinary School and School of Biological Sciences, University of Bristol, Bristol, UK., Schwede A; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Kimblin N; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Francisco AF; Faculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, London, WC1E 7HT, UK., Pepperl J; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Rust S; Antibody Discovery and Protein Engineering, Biopharmaceuticals R&D, AstraZeneca, Cambridge, UK., Voorheis P; School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin, Ireland., Gibson W; Bristol Veterinary School and School of Biological Sciences, University of Bristol, Bristol, UK., Taylor MC; Faculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, London, WC1E 7HT, UK., Higgins MK; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. matthew.higgins@bioch.ox.ac.uk.; Kavli Institute for Nanoscience Discovery, Dorothy Crowfoot Hodgkin Building, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. matthew.higgins@bioch.ox.ac.uk., Carrington M; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK. mc115@cam.ac.uk.

Publikováno v: Nature communications [Nat Commun] 2022 Aug 29; Vol. 13 (1), pp. 5085. Date of Electronic Publication: 2022 Aug 29.