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Your search keyword '"Hendrickx, Rodinde"' showing total 10 results
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10 results on '"Hendrickx, Rodinde"'

1. Plant cells-based biological matrix composites

Author

Roumeli, Eleftheria, Bonanomi, Luca, Hendrickx, Rodinde, Rinaldi, Katherine, and Daraio, Chiara

Subjects
Physics - Applied Physics, Condensed Matter - Materials Science
Abstract

The global increase in materials consumption calls for innovative materials, with tailored performance and multi-functionality, that are environmentally sustainable. Composites from renewable resources offer solutions to fulfil these demands but have so far been dominated by hybrid petrochemicals-based matrixes reinforced by natural fillers. Here, we present biological matrix composites with properties comparable to wood and commercial polymers. The biocomposites are obtained from cultured, undifferentiated plant cells, dehydrated and compressed under controlled conditions, forming a lamellar microstructure. Their stiffness and strength surpass that of commercial plastics of similar density, like polystyrene, and low-density polyethylene, while being entirely biodegradable. The properties can be further tuned varying the fabrication process. For example, filler particles can be integrated during fabrication, to vary the mechanical response or introduce new functionalities.

Published
2019

7. The RGD-binding integrins αvβ6 and αvβ8 are receptors for mouse adenovirus-1 and -3 infection

Author

Bieri, Manuela, Hendrickx, Rodinde, Bauer, Michael, Yu, Bin, Jetzer, Tania, Dreier, Birgit, Mittl, Peer R E, Sobek, Jens, Plückthun, Andreas, Greber, Urs F, Hemmi, Silvio, University of Zurich, and Neumann, Donna

Subjects
Integrins, Physiology, Cell Lines, Adenoviridae Infections, Biochemistry, Mice, Spectrum Analysis Techniques, Immune Physiology, Medicine and Health Sciences, Flow cytometry, Biology (General), 0303 health sciences, Immune System Proteins, 030302 biochemistry & molecular biology, Cell staining, Recombinant Proteins, 10124 Institute of Molecular Life Sciences, Extracellular Matrix, 3. Good health, Spectrophotometry, Receptors, Virus, Cytophotometry, Biological Cultures, Cellular Structures and Organelles, Antibodies, Cell binding, Cell binding assay, B16 cells, Binding analysis, Research Article, Cell Physiology, QH301-705.5, Immunology, Research and Analysis Methods, Microbiology, Adenoviridae, 03 medical and health sciences, Antigens, Neoplasm, Virology, Cell Adhesion, 10019 Department of Biochemistry, Genetics, Animals, Humans, Molecular Biology, Chemical Characterization, 030304 developmental biology, Biology and Life Sciences, Proteins, Cell Biology, RC581-607, 570 Life sciences, biology, Parasitology, Immunologic diseases. Allergy
Abstract

Mammalian adenoviruses (AdVs) comprise more than ~350 types including over 100 human (HAdVs) and just three mouse AdVs (MAdVs). While most HAdVs initiate infection by high affinity/avidity binding of their fiber knob (FK) protein to either coxsackievirus AdV receptor (CAR), CD46 or desmoglein (DSG)-2, MAdV-1 (M1) infection requires arginine-glycine-aspartate (RGD) binding integrins. To identify the receptors mediating MAdV infection we generated five novel reporter viruses for MAdV-1/-2/-3 (M1, M2, M3) transducing permissive murine (m) CMT-93 cells, but not B16 mouse melanoma cells expressing mCAR, human (h) CD46 or hDSG-2. Recombinant M1 or M3 FKs cross-blocked M1 and M3 but not M2 infections. Profiling of murine and human cells expressing RGD-binding integrins suggested that αvβ6 and αvβ8 heterodimers are associated with M1 and M3 infections. Ectopic expression of mβ6 in B16 cells strongly enhanced M1 and M3 binding, infection, and progeny production comparable with mαvβ6-positive CMT-93 cells, whereas mβ8 expressing cells were more permissive to M1 than M3. Anti-integrin antibodies potently blocked M1 and M3 binding and infection of CMT-93 cells and hαvβ8-positive M000216 cells. Soluble integrin αvβ6, and synthetic peptides containing the RGDLXXL sequence derived from FK-M1, FK-M3 and foot and mouth disease virus coat protein strongly interfered with M1/M3 infections, in agreement with high affinity interactions of FK-M1/FK-M3 with αvβ6/αvβ8, determined by surface plasmon resonance measurements. Molecular docking simulations of ternary complexes revealed a bent conformation of RGDLXXL-containing FK-M3 peptides on the subunit interface of αvβ6/β8, where the distal leucine residue dips into a hydrophobic pocket of β6/8, the arginine residue ionically engages αv aspartate215, and the aspartate residue coordinates a divalent cation in αvβ6/β8. Together, the RGDLXXL-bearing FKs are part of an essential mechanism for M1/M3 infection engaging murine and human αvβ6/8 integrins. These integrins are highly conserved in other mammals, and may favour cross-species virus transmission., PLoS Pathogens, 17 (12), ISSN:1553-7374, ISSN:1553-7366

Published
2021

10. The RGD-binding integrins αvβ6 and αvβ8 are receptors for mouse adenovirus-1 and -3 infection.

Author

Bieri M, Hendrickx R, Bauer M, Yu B, Jetzer T, Dreier B, Mittl PRE, Sobek J, Plückthun A, Greber UF, and Hemmi S

Subjects
Animals, Humans, Mice, Adenoviridae metabolism, Adenoviridae Infections metabolism, Antigens, Neoplasm metabolism, Integrins metabolism, Receptors, Virus metabolism
Abstract

Mammalian adenoviruses (AdVs) comprise more than ~350 types including over 100 human (HAdVs) and just three mouse AdVs (MAdVs). While most HAdVs initiate infection by high affinity/avidity binding of their fiber knob (FK) protein to either coxsackievirus AdV receptor (CAR), CD46 or desmoglein (DSG)-2, MAdV-1 (M1) infection requires arginine-glycine-aspartate (RGD) binding integrins. To identify the receptors mediating MAdV infection we generated five novel reporter viruses for MAdV-1/-2/-3 (M1, M2, M3) transducing permissive murine (m) CMT-93 cells, but not B16 mouse melanoma cells expressing mCAR, human (h) CD46 or hDSG-2. Recombinant M1 or M3 FKs cross-blocked M1 and M3 but not M2 infections. Profiling of murine and human cells expressing RGD-binding integrins suggested that αvβ6 and αvβ8 heterodimers are associated with M1 and M3 infections. Ectopic expression of mβ6 in B16 cells strongly enhanced M1 and M3 binding, infection, and progeny production comparable with mαvβ6-positive CMT-93 cells, whereas mβ8 expressing cells were more permissive to M1 than M3. Anti-integrin antibodies potently blocked M1 and M3 binding and infection of CMT-93 cells and hαvβ8-positive M000216 cells. Soluble integrin αvβ6, and synthetic peptides containing the RGDLXXL sequence derived from FK-M1, FK-M3 and foot and mouth disease virus coat protein strongly interfered with M1/M3 infections, in agreement with high affinity interactions of FK-M1/FK-M3 with αvβ6/αvβ8, determined by surface plasmon resonance measurements. Molecular docking simulations of ternary complexes revealed a bent conformation of RGDLXXL-containing FK-M3 peptides on the subunit interface of αvβ6/β8, where the distal leucine residue dips into a hydrophobic pocket of β6/8, the arginine residue ionically engages αv aspartate215, and the aspartate residue coordinates a divalent cation in αvβ6/β8. Together, the RGDLXXL-bearing FKs are part of an essential mechanism for M1/M3 infection engaging murine and human αvβ6/8 integrins. These integrins are highly conserved in other mammals, and may favour cross-species virus transmission., Competing Interests: The authors have declared that no competing interests exist

Published
2021
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