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Maturation of measles virus hemagglutinin glycoprotein

Archives of Virology
|January 1, 1985
PubMed

Insights

Measles virus hemagglutinin glycoprotein (H) undergoes significant processing in infected cells, maturing into larger forms. This maturation is crucial for its expression on the cell surface.

Area of Science:

  • Virology
  • Cell Biology
  • Glycobiology

Background:

  • Measles virus hemagglutinin (H) glycoprotein is essential for viral entry.
  • Understanding H glycoprotein processing is key to viral pathogenesis.

Purpose of the Study:

  • To elucidate the post-translational processing pathway of measles virus H glycoprotein.
  • To characterize the molecular changes during H glycoprotein maturation.

Main Methods:

  • Pulse-chase experiments to track protein synthesis and modification.
  • Two-dimensional isoelectric focusing and SDS-polyacrylamide gel electrophoresis to analyze protein size and charge.

Main Results:

  • H glycoprotein is initially synthesized as smaller polypeptides, then processed into larger forms with reduced charge.
  • Maturation involves changes associated with cell surface expression.
  • Sialic acid removal shifts the isoelectric point to a more basic range.
  • Maturation takes approximately 5 hours, with carbohydrates comprising 12% of the weight.

Conclusions:

  • Measles virus H glycoprotein undergoes extensive post-translational modification.
  • These modifications are critical for its function and cell surface localization.
  • The identified monosaccharides (mannose, galactose, fucose, N-acetylglucosamine, N-acetylneuraminic acid) are integral to H glycoprotein structure.

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