%0 Journal Article %A Martin-Gallardo, Antonia %A Fleischer, Edward %A Doyle, Shawn A. %A Arumugham, Rasappa %A Collins, Peter L. %A Hildreth, Stephen W. %A Paradiso, Peter R. %T Expression of the G glycoprotein gene of human respiratory syncytial virus in Salmonella typhimurium %D 1993 %J Journal of General Virology, %V 74 %N 3 %P 453-458 %@ 1465-2099 %R https://doi.org/10.1099/0022-1317-74-3-453 %I Microbiology Society, %X The attachment protein, G, of human respiratory syncytial virus (RSV) is an M r 84K to 90K species which has a high content of N-linked and O-linked carbohydrates. The unglycosylated form of this protein was expressed by inserting a full-length cDNA copy of the mRNA from the A2 strain of RSV into a prokaryotic expression vector under the control of the lambda PL promoter. Salmonella typhimurium cells transformed with the G-containing plasmid synthesized a protein of M r 40000 that specifically reacted with polyclonal and two neutralizing monoclonal antibodies raised against the native RSV G glycoprotein. Recombinant G protein was purified by immunoaffinity chromatography using a neutralizing monoclonal antibody. Cotton rats immunized with the recombinant G protein produced serum antibodies to the G glycoprotein that neutralized RSV in vitro. The study demonstrates that the G protein of RSV can be expressed in bacteria and that at least one neutralizing epitope is not structurally dependent on carbohydrates. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-74-3-453