JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yuan, H.
Right arrow Articles by Schlegel, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yuan, H.
Right arrow Articles by Schlegel, R.

Journal of Virology, September 2001, p. 7848-7853, Vol. 75, No. 17
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.17.7848-7853.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Immunization with a Pentameric L1 Fusion Protein Protects against Papillomavirus Infection

Hang Yuan,1 Patricia A. Estes,2 Yan Chen,1 Joseph Newsome,1 Vanessa A. Olcese,1 Robert L. Garcea,2 and Richard Schlegel1,*

Department of Pathology, Georgetown University School of Medicine, Washington, D.C. 20007,1 and Section of Pediatric Hematology/Oncology, University of Colorado School of Medicine, Denver, Colorado 802622

Received 22 January 2001/Accepted 23 May 2001

The prophylactic papillomavirus vaccines currently in clinical trials are composed of viral L1 capsid protein that is synthesized in eukaryotic expression systems and purified in the form of virus-like particles (VLPs). To evaluate whether VLPs are necessary for effective vaccination, we expressed the L1 protein as a glutathione S-transferase (GST) fusion protein in Escherichia coli and assayed its immunogenic activity in an established canine oral papillomavirus (COPV) model that previously validated the efficacy of VLP vaccines. The GST-COPV L1 fusion protein formed pentamers, but these capsomere-like structures did not assemble into VLPs. Despite the lack of VLP formation, the GST-COPV L1 protein retained its native conformation as determined by reactivity with conformation-specific anti-COPV antibodies. Most importantly, the GST-COPV L1 pentamers completely protected dogs from high-dose viral infection of their oral mucosa. L1 fusion proteins expressed in bacteria represent an economical alternative to VLPs as a human papillomavirus vaccine.


* Corresponding author. Mailing address: Department of Pathology, Georgetown University School of Medicine, 3900 Reservoir Rd., Washington, DC 20007. Phone: (202) 687-1704. Fax: (202) 687-8934. E-mail: schleger{at}georgetown.edu.


Journal of Virology, September 2001, p. 7848-7853, Vol. 75, No. 17
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.17.7848-7853.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 2001 by the American Society for Microbiology. All rights reserved.