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14 results on '"Feitsma, Louris"'

4. Structural insights into collagen binding by platelet receptor glycoprotein VI

Author

Feitsma, Louris J, Brondijk, Harma C, Jarvis, Gavin E, Hagemans, Dominique, Bihan, Dominique, Jerah, Natasia, Versteeg, Marian, Farndale, Richard W, Huizinga, Eric G, Feitsma, Louris J [0000-0002-8403-1108], Brondijk, Harma C [0000-0002-0234-673X], Bihan, Dominique [0000-0002-4837-3389], Farndale, Richard W [0000-0001-6130-8808], Huizinga, Eric G [0000-0001-6928-8426], and Apollo - University of Cambridge Repository

Subjects
Blood Platelets, Binding Sites, Animals, Thrombosis, Collagen, Platelet Membrane Glycoproteins, Peptides, Platelet Activation, Protein Binding
Abstract

Glycoprotein VI (GPVI) mediates collagen-induced platelet activation after vascular damage and is an important contributor to the onset of thrombosis, heart attack, and stroke. Animal models of thrombosis have identified GPVI as a promising target for antithrombotic therapy. Although for many years the crystal structure of GPVI has been known, the essential details of its interaction with collagen have remained elusive. Here, we present crystal structures of the GPVI ectodomain bound to triple-helical collagen peptides, which reveal a collagen-binding site across the β-sheet of the D1 domain. Mutagenesis and binding studies confirm the observed binding site and identify Trp76, Arg38, and Glu40 as essential residues for binding to fibrillar collagens and collagen-related peptides (CRPs). GPVI binds a site on collagen comprising two collagen chains with the core formed by the sequence motif OGPOGP. Potent GPVI-binding peptides from Toolkit-III all contain OGPOGP; weaker binding peptides frequently contain a partial motif varying at either terminus. Alanine-scanning of peptide III-30 also identified two AGPOGP motifs that contribute to GPVI binding, but steric hindrance between GPVI molecules restricts the maximum binding capacity. We further show that no cooperative interactions could occur between two GPVI monomers binding to a stretch of (GPO)5 and that binding of ≥2 GPVI molecules to a fibril-embedded helix requires non-overlapping OGPOGP motifs. Our structure confirms the previously suggested similarity in collagen binding between GPVI and leukocyte-associated immunoglobulin-like receptor 1 (LAIR-1) but also indicates significant differences that may be exploited for the development of receptor-specific therapeutics.

Published
2022

7. Betacoronavirus Adaptation to Humans Involved Progressive Loss of Hemagglutinin-Esterase Lectin Activity

Author

dI&I I&I-1, LS Virologie, Bakkers, Mark J G, Lang, Yifei, Feitsma, Louris J, Hulswit, Ruben J G, de Poot, Stefanie A H, van Vliet, Arno L W, Margine, Irina, de Groot-Mijnes, Jolanda D F, van Kuppeveld, Frank J M, Langereis, Martijn A, Huizinga, Eric G, de Groot, Raoul J, dI&I I&I-1, LS Virologie, Bakkers, Mark J G, Lang, Yifei, Feitsma, Louris J, Hulswit, Ruben J G, de Poot, Stefanie A H, van Vliet, Arno L W, Margine, Irina, de Groot-Mijnes, Jolanda D F, van Kuppeveld, Frank J M, Langereis, Martijn A, Huizinga, Eric G, and de Groot, Raoul J

Published
2017

8. Betacoronavirus Adaptation to Humans Involved Progressive Loss of Hemagglutinin-Esterase Lectin Activity

Author

Bakkers, Mark J.G., primary, Lang, Yifei, additional, Feitsma, Louris J., additional, Hulswit, Ruben J.G., additional, de Poot, Stefanie A.H., additional, van Vliet, Arno L.W., additional, Margine, Irina, additional, de Groot-Mijnes, Jolanda D.F., additional, van Kuppeveld, Frank J.M., additional, Langereis, Martijn A., additional, Huizinga, Eric G., additional, and de Groot, Raoul J., additional

Published
2017
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9. Coronavirus receptor switch explained from the stereochemistry of protein-carbohydrate interactions and a single mutation

Author

Bakkers, Mark J G, Zeng, Qinghong, Feitsma, Louris J, Hulswit, Ruben J G, Li, Zeshi, Westerbeke, Aniek, van Kuppeveld, Frank J M, Boons, Geert-Jan, Langereis, Martijn A, Huizinga, Eric G, de Groot, Raoul J, Bakkers, Mark J G, Zeng, Qinghong, Feitsma, Louris J, Hulswit, Ruben J G, Li, Zeshi, Westerbeke, Aniek, van Kuppeveld, Frank J M, Boons, Geert-Jan, Langereis, Martijn A, Huizinga, Eric G, and de Groot, Raoul J

Abstract

Hemagglutinin-esterases (HEs) are bimodular envelope proteins of orthomyxoviruses, toroviruses, and coronaviruses with a carbohydrate-binding "lectin" domain appended to a receptor-destroying sialate-O-acetylesterase ("esterase"). In concert, these domains facilitate dynamic virion attachment to cell-surface sialoglycans. Most HEs (type I) target 9-O-acetylated sialic acids (9-O-Ac-Sias), but one group of coronaviruses switched to using 4-O-Ac-Sias instead (type II). This specificity shift required quasisynchronous adaptations in the Sia-binding sites of both lectin and esterase domains. Previously, a partially disordered crystal structure of a type II HE revealed how the shift in lectin ligand specificity was achieved. How the switch in esterase substrate specificity was realized remained unresolved, however. Here, we present a complete structure of a type II HE with a receptor analog in the catalytic site and identify the mutations underlying the 9-O- to 4-O-Ac-Sia substrate switch. We show that (i) common principles pertaining to the stereochemistry of protein-carbohydrate interactions were at the core of the transition in lectin ligand and esterase substrate specificity; (ii) in consequence, the switch in O-Ac-Sia specificity could be readily accomplished via convergent intramolecular coevolution with only modest architectural changes in lectin and esterase domains; and (iii) a single, inconspicuous Ala-to-Ser substitution in the catalytic site was key to the emergence of the type II HEs. Our findings provide fundamental insights into how proteins "see" sugars and how this affects protein and virus evolution.

Published
2016

10. Coronavirus receptor switch explained from the stereochemistry of protein-carbohydrate interactions and a single mutation

Author

dI&I I&I-1, LS Virologie, Sub Crystal and Structural Chemistry, Sub Chemical pharmacology, Sub Algemeen Scheikunde, Medicinal Chemistry and Chemical Biology, Bakkers, Mark J G, Zeng, Qinghong, Feitsma, Louris J, Hulswit, Ruben J G, Li, Zeshi, Westerbeke, Aniek, van Kuppeveld, Frank J M, Boons, Geert-Jan, Langereis, Martijn A, Huizinga, Eric G, de Groot, Raoul J, dI&I I&I-1, LS Virologie, Sub Crystal and Structural Chemistry, Sub Chemical pharmacology, Sub Algemeen Scheikunde, Medicinal Chemistry and Chemical Biology, Bakkers, Mark J G, Zeng, Qinghong, Feitsma, Louris J, Hulswit, Ruben J G, Li, Zeshi, Westerbeke, Aniek, van Kuppeveld, Frank J M, Boons, Geert-Jan, Langereis, Martijn A, Huizinga, Eric G, and de Groot, Raoul J

Published
2016

11. Structural basis for inhibition of TLR2 by staphylococcal superantigen-like protein 3 (SSL3)

Author

Koymans, Kirsten J, Feitsma, Louris J, Brondijk, T Harma C, Aerts, Piet C, Lukkien, Eddie, Lössl, Philip, van Kessel, Kok P M, de Haas, Carla J C, van Strijp, Jos A G, Huizinga, Eric G, Koymans, Kirsten J, Feitsma, Louris J, Brondijk, T Harma C, Aerts, Piet C, Lukkien, Eddie, Lössl, Philip, van Kessel, Kok P M, de Haas, Carla J C, van Strijp, Jos A G, and Huizinga, Eric G

Published
2015

12. Structural basis for inhibition of TLR2 by staphylococcal superantigen-like protein 3 (SSL3)

Author

MMB Research line 1, MMB, Infection & Immunity, Koymans, Kirsten J, Feitsma, Louris J, Brondijk, T Harma C, Aerts, Piet C, Lukkien, Eddie, Lössl, Philip, van Kessel, Kok P M, de Haas, Carla J C, van Strijp, Jos A G, Huizinga, Eric G, MMB Research line 1, MMB, Infection & Immunity, Koymans, Kirsten J, Feitsma, Louris J, Brondijk, T Harma C, Aerts, Piet C, Lukkien, Eddie, Lössl, Philip, van Kessel, Kok P M, de Haas, Carla J C, van Strijp, Jos A G, and Huizinga, Eric G

Published
2015

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