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Journal of Virology, April 2005, p. 4527-4532, Vol. 79, No. 7
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.7.4527-4532.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Modulation of Protective Immunity, Eosinophilia, and Cytokine Responses by Selective Mutagenesis of a Recombinant G Protein Vaccine against Respiratory Syncytial Virus

Yan Huang and Robert Anderson*

Department of Microbiology & Immunology, Dalhousie University, Halifax, Nova Scotia, Canada

Received 10 May 2004/ Accepted 13 October 2004

Using an Escherichia coli-grown plasmid vector encoding a fragment of thioredoxin (Trx) fused to a central region (amino acids 128 to 229) of the respiratory syncytial virus (RSV) (Long strain) G protein, we employed site-directed mutagenesis to investigate the importance of selected amino acids to vaccine efficacy. Mice were immunized with a total of 10 wild-type or mutant Trx-G proteins and challenged intranasally with RSV. Striking differences in the induction of RSV G-protein-specific antibodies, protection against RSV challenge, cytokine RNA responses, and induction of RSV-associated eosinophilic inflammation were observed among the mutant proteins examined. Taken together, the results identify a critical role for specific amino acids in the induction of protective immunity and priming for eosinophilia against RSV.

* Corresponding author. Mailing address: Department of Microbiology & Immunology, Dalhousie University, Halifax, Nova Scotia B3H 4H7, Canada. Phone: (902) 494-1063. Fax: (902) 494-5125. E-mail: robert.anderson{at}dal.ca.

Journal of Virology, April 2005, p. 4527-4532, Vol. 79, No. 7
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.7.4527-4532.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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