HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Martin-Gallardo, A. Articles by Paradiso, P. R. Search for Related Content PubMed PubMed Citation Articles by Martin-Gallardo, A. Articles by Paradiso, P. R. Agricola Articles by Martin-Gallardo, A. Articles by Paradiso, P. R.

Expression of the G glycoprotein gene of human respiratory syncytial virus in Salmonella typhimurium

Antonia Martin-Gallardo^1,

¹ Department of Virology, Praxis Biologics Inc., 300 East River Road, Rochester, New York 14623
and² Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892, U.S.A.

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 P_L 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.

Present address: Lawrence Livermore National Laboratory, Human Genome Center, L-452, 7000 East Avenue, Livermore, California 94550, U.S.A.

Received 5 November 1991; accepted 3 November 1992.

This article has been cited by other articles:

				C. Bourgeois, J. B. Bour, K. Lidholt, C. Gauthray, and P. Pothier Heparin-Like Structures on Respiratory Syncytial Virus Are Involved in Its Infectivity In Vitro J. Virol., September 1, 1998; 72(9): 7221 - 7227. [Abstract] [Full Text] [PDF]

				R. A. Dudas and R. A. Karron Respiratory Syncytial Virus Vaccines Clin. Microbiol. Rev., July 1, 1998; 11(3): 430 - 439. [Abstract] [Full Text] [PDF]