Distinct Kinetics for Binding of the CD46 and SLAM Receptors to Overlapping Sites in the Measles Virus Hemagglutinin Protein (original) (raw)

Dynamic Interaction of the Measles Virus Hemagglutinin with Its Receptor Signaling Lymphocytic Activation Molecule (SLAM, CD150)

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Mapping of the Primary Binding Site of Measles Virus to Its Receptor CD46

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Selectively Receptor-Blind Measles Viruses: Identification of Residues Necessary for SLAM- or CD46-Induced Fusion and Their Localization on a New Hemagglutinin Structural Model

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Measles Virus Infects both Polarized Epithelial and Immune Cells by Using Distinctive Receptor-Binding Sites on Its Hemagglutinin

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Functional and structural interactions between measles virus hemagglutinin and CD46

Edward Berger

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Functional and structural interaction between measles virus hemagglutinin and CD46

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The Receptor-Binding Site of the Measles Virus Hemagglutinin Protein Itself Constitutes a Conserved Neutralizing Epitope

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Cell Entry by Measles Virus: Long Hybrid Receptors Uncouple Binding from Membrane Fusion

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CD46 short consensus repeats III and IV enhance measles virus binding but impair soluble hemagglutinin binding

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Measles virus spread by cell-cell contacts: uncoupling of contact-mediated receptor (CD46) downregulation from virus uptake

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Receptor usage and differential downregulation of CD46 by measles virus wild-type and vaccine strains

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Efficient Major Histocompatibility Complex Class II-restricted Presentation of Measles Virus Relies on Hemagglutinin-mediated Targeting to Its Cellular Receptor Human CD46 Expressed by Murine B Cells By Denis Gerlier, Marie-Claude Trescol-Bi6mont

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Interaction of Measles Virus (Hallé Strain) with CD46: Evidence That a Common Binding Site on CD46 Facilitates Both CD46 Downregulation and MV Infection

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Physical association of moesin and CD46 as a receptor complex for measles virus

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CD150 (SLAM) Is a Receptor for Measles Virus but Is Not Involved in Viral Contact-Mediated Proliferation Inhibition

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The Measles Virus Hemagglutinin -Propeller Head 4- 5 Hydrophobic Groove Governs Functional Interactions with Nectin-4 and CD46 but Not Those with the Signaling Lymphocytic Activation Molecule

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CDw150(SLAM) Is a Receptor for a Lymphotropic Strain of Measles Virus and May Account for the Immunosuppressive Properties of This Virus

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Functional fine-mapping and molecular modeling of a conserved loop epitope of the measles virus hemagglutinin protein

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The Measles Virus Hemagglutinin β-Propeller Head β4-β5 Hydrophobic Groove Governs Functional Interactions with Nectin-4 and CD46 but Not Those with the Signaling Lymphocytic Activation Molecule

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Measles virus interacts with human SLAM receptor on dendritic cells to cause immunosuppression

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Antibody cross-reactivity with CD46 and lack of cell surface expression suggest that moesin might not mediate measles virus binding

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Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion protein

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Computational Analysis of the Interaction Energies between Amino Acid Residues of the Measles Virus Hemagglutinin and Its Receptors

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