title: pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin.
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.
authors.affiliation: Laboratory of Molecular Biology, Flanders Interuniversity Institute of Biotechnology, University of Ghent, Belgium.
authors.forename: P
authors.initials: P
authors.lastname: Vanlandschoot
authors.forename: E
authors.initials: E
authors.lastname: Beirnaert
authors.forename: J
authors.initials: J
authors.lastname: Grooten
authors.forename: W M
authors.initials: WM
authors.lastname: Jou
authors.forename: W
authors.initials: W
authors.lastname: Fiers
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D002460:Cell Line; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D018411:Spodoptera
chemical_list: D000911:Antibodies, Monoclonal; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D011994:Recombinant Proteins