Probing the functions of the paramyxovirus glycoproteins F and HN 3 with a panel of synthetic antibodies ( sABs ) 4 5
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چکیده
*To whom correspondence should be addressed: RAL Dept. of Molecular Biosciences, 18 Northwestern University, 2205 Tech Drive, Evanston, IL 60208-3500 Telephone: 847-491-5433; 19 Fax: 847-491-2467; e-mail: [email protected]; or AAK – Dept. of Biochemistry and 20 Molecular Biology, The University of Chicago, 900 E. 57th Street, Chicago, Illinois, 60637; 21 Telephone: 773-702-9257; Fax: 773-702-0439; e-mail: [email protected] 22 23 JVI Accepts, published online ahead of print on 13 August 2014 J. Virol. doi:10.1128/JVI.01707-14 Copyright © 2014, American Society for Microbiology. All Rights Reserved.
منابع مشابه
Probing the functions of the paramyxovirus glycoproteins F and HN with a panel of synthetic antibodies.
Paramyxoviruses are enveloped negative-strand RNA viruses that are significant human and animal pathogens. Most paramyxoviruses infect host cells via the concerted action of a tetrameric attachment protein (variously called HN, H, or G) that binds either sialic acid or protein receptors on target cells and a trimeric fusion protein (F) that merges the viral envelope with the plasma membrane at ...
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Monoclonal antibodies against the major glycoprotein (HN) and the nucleoprotein (NP) of paramyxovirus SV5 and human paramyxovirus (PF) type 3 have been obtained. Two different epitopes have been detected on the SV5 HN polypeptide, one being specific to SV5 and the other also cross-reacting with PF-2 HN polypeptide. Monoclonal antibody against SV5 NP polypeptide also reacted with PF-2 NP polypep...
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The fusion (F) and hemagglutinin-neuraminidase (HN) glycoproteins of the paramyxovirus simian virus 5 (SV5) were expressed individually or coexpressed in CV-1 cells by using SV40-based vectors and recombinant vaccinia viruses. The extent of detectable fusion in a syncytium formation assay was found to be affected by the expression system used. In addition, when HN was coexpressed with F, it was...
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