pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin.
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.
Vanlandschoot
P
P
Laboratory of Molecular Biology, Flanders Interuniversity Institute of Biotechnology, University of Ghent, Belgium.
Beirnaert
E
E
Grooten
J
J
Jou
W M
WM
Fiers
W
W
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
D000911:Antibodies, Monoclonal; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D011994:Recombinant Proteins