pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin

Arch Virol. 1998;143(2):227-39. doi: 10.1007/s007050050282.

Abstract

We previously reported the expression of soluble A/Victoria/3/75 (H3N2) hemagglutinin in insect cells and the molecular and immunological structure of an aggregated fraction, only observed in cell supernatant when expression was performed at low pH [23]. Here we report that besides this aggregated a monomeric and possibly a trimeric structure is detected in cell supernatant, irrespective of the pH of the medium. Evidence is presented that the aggregated fraction is generated out of monomeric HAOs molecules due to a low intracellular pH encountered during secretion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology
  • Cell Line
  • Hemagglutinin Glycoproteins, Influenza Virus / chemistry*
  • Hemagglutinin Glycoproteins, Influenza Virus / metabolism
  • Hydrogen-Ion Concentration
  • Protein Folding
  • Recombinant Proteins / chemistry
  • Spodoptera

Substances

  • Antibodies, Monoclonal
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Recombinant Proteins