Studies concerning the interaction of measles virus with its cellular receptors.
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Studies concerning the interaction of measles virus with its cellular receptors.

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Published .
Written in English

Book details:

The Physical Object
Pagination215 leaves.
Number of Pages215
ID Numbers
Open LibraryOL19267545M
ISBN 100612457419

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Ideally, a virus receptor would fulfill three main characteristics: (1) a physical interaction between the virus and the receptor should be demonstrated; (2) occupying the virus-binding site of the receptor (e.g., with an antibody directed against the receptor, should inhibit virus infection); and (3) the cellular sensitivity to virus Virus Receptor. Virus receptors may be highly specialized proteins with limited tissue distribution, such as complement receptors, growth factor receptors, or neurotransmitter receptors, or more ubiquitous components of cellular membranes, such as integrins and other intercellular adhesion molecules, glycosaminoglycans, or sialic acid–containing :// Measles virus (MV) belonging to the genus Morbillivirus of the family Paramyxoviridae is a causative agent of measles in humans. Measles is an acute and highly contagious disease that often Current evidence suggests that members of different Paramyxovirinae genera have developed distinct strategies by which the glycoprotein interaction regulates triggering of the F protein –.Based on endoplasmic reticulum (ER) co-retention studies with hPIV3- and PIV5-derived glycoprotein pairs, which demonstrated that an ER-retained glycoprotein mutant is unable to co-retain its unmodified

Kirk U. Knowlton, Hervé Duplain, in Molecular Basis of Cardiovascular Disease (Second Edition), Viral Receptors. To infect a target cell, the virus must attach to a viral receptor or receptor complex. In , a common receptor for coxsackie and adenovirus, the coxsackie adenovirus receptor (CAR), was identified. CAR mediates cell attachment and entry into the :// After the virus enters into cells, various cellular proteins may interact with it; some support virus replication, while others inhibit it. Once virus succeeds to establish its life cycle in the target cell, the progeny viruses disseminate within the tissues or systemically via :// Martin Blackledge's research works w citations and 9, reads, including: Revealing the mechanism of repressor inactivation during switching of a temperate bacteriophage   Measles is a highly transmissible disease caused by measles virus and remains a major cause of child mortality in developing countries. Measles virus nucleoprotein (N) encapsidates the RNA genome of the virus for providing protection from host cell endonucleases and for specific recognition of viral RNA as template for transcription and ://

Virus-cell interaction. The interaction of a virus with its cellular receptor is mediated by one or more surface proteins. In enveloped viruses, the envelope glycoproteins (e.g. the influenza virus hemagglutinin); in naked viruses, the capsid proteins (e.g. exon protein of the adenovirus). Little is known concerning the region of F that interacts with the HN/H/G stalk, but recent studies implicate residues near the base of the prefusion measles virus F head. Chimeric F proteins generated between PIV5 F and simian virus 41 F have also been used to map the HN interaction site [ 65 ], but the identified region is relatively :// Measles virus (MV) was isolated in (Enders and Peeble ). It is among the most contagious of viruses and a leading cause of mortality in children in developing countries (Murray and Lopez In common with most viruses, measles virus (MV) relies on the integrity of the cytoskeleton of its host cells both with regard to efficient replication in these cells, but also retention of their motility which favors viral dissemination. It is, however, the surface interaction of the viral glycoprotein (gp) complex with receptors present on lymphocytes and dendritic cells (DCs), that signals