CD46 short consensus repeats III and IV enhance measles virus binding but impair soluble hemagglutinin binding
نویسندگان
چکیده
منابع مشابه
Distinct kinetics for binding of the CD46 and SLAM receptors to overlapping sites in the measles virus hemagglutinin protein.
Measles virus (MV) is a human pathogen using two distinct cell surface receptors for entry into host cells. We present here a comparative analysis for binding of the MV receptors CD46 and SLAM to the measles virus hemagglutinin protein (MVH, Edmonston strain). Soluble monomeric and dimeric MVH variants were prepared in mammalian cells and their conformation assessed using a panel of monoclonal ...
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The pH-independent fusion of membranes induced by measles virus (MV) requires, in addition to the fusion-competent protein F, hemagglutinin (H), and on the target membrane, the virus receptor CD46. We constructed hybrid receptors composed of different numbers and combinations of the four CD46 short consensus repeat (SCR) domains, followed by immunoglobulin-like domains of another cell surface p...
متن کاملEvidence for distinct complement regulatory and measles virus binding sites on CD46 SCR2.
Human CD46, or membrane cofactor protein, is a regulator of complement activation and is used as a cellular receptor by measles virus. Using a series of 13 single point mutants, the region of short consensus repeat (SCR) 2 domain involved in the regulation of complement activation was mapped to residues E84, N94, Y98, E102, E103, I104 and E108. Molecular modelling localized all residues, with t...
متن کاملCrystal structure of two CD46 domains reveals an extended measles virus-binding surface.
Measles virus is a paramyxovirus which, like other members of the family such as respiratory syncytial virus, is a major cause of morbidity and mortality worldwide. The cell surface receptor for measles virus in humans is CD46, a complement cofactor. We report here the crystal structure at 3.1 A resolution of the measles virus-binding fragment of CD46. The structure reveals the architecture and...
متن کاملThe receptor-binding site of the measles virus hemagglutinin protein itself constitutes a conserved neutralizing epitope.
Here, we provide direct evidence that the receptor-binding site of measles virus (MV) hemagglutinin protein itself forms an effective conserved neutralizing epitope (CNE). Several receptor-interacting residues constitute the CNE. Thus, viral escape from neutralization has to be associated with loss of receptor-binding activity. Since interactions with both the signaling lymphocyte activation mo...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 1997
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.71.5.4157-4160.1997