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Addition of carbohydrate side-chains at novel sites on influenza-virus hemagglutinin can modulate the folding, transport, and activity of the molecule

Academic Article
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Overview

authors

  • Gallagher, P.
  • Henneberry, J.
  • Wilson, Ian
  • Sambrook, J.
  • Gething, M. J.

publication date

  • December 1988

journal

  • Journal of Cell Biology  Journal

abstract

  • We have constructed and expressed a series of mutant influenza virus hemagglutinins, each containing a new consensus site for glycosylation in addition to the seven sites found on the wild-type protein. Oligosaccharide side chains were added with high efficiency at four of the five novel sites, located on areas of the protein's surface that are not normally shielded by carbohydrate. Investigations of the structure, intracellular transport, and biological activities of the mutant hemagglutinin molecules indicated that (a) supernumerary carbohydrate side chains can be used to shield or disrupt functional epitopes on the surface of hemagglutinin, and (b) the presence of an additional oligosaccharide may cause temperature-dependent defects in the transport of the glycoprotein. We discuss the addition of supernumerary oligosaccharides as a general tool for shielding chosen areas of the surface of proteins that enter or traverse the secretory pathway.

subject areas

  • Amino Acid Sequence
  • Antigens, Viral
  • Biological Transport
  • Cell Fusion
  • Computer Simulation
  • DNA Mutational Analysis
  • Epitopes
  • Fluorescent Antibody Technique
  • Glycosylation
  • Hemagglutinins, Viral
  • Influenza A virus
  • Membrane Glycoproteins
  • Molecular Weight
  • Protein Conformation
  • Structure-Activity Relationship
  • Temperature
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.107.6.2059

PubMed ID

  • 2461945
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Additional Document Info

start page

  • 2059

end page

  • 2073

volume

  • 107

issue

  • 6

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