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Journal of Virology, August 2006, p. 7688-7698, Vol. 80, No. 15
0022-538X/06/$08.00+0     doi:10.1128/JVI.00235-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Assembly of Human Immunodeficiency Virus (HIV) Antigens on Bacteriophage T4: a Novel In Vitro Approach To Construct Multicomponent HIV Vaccines

Taheri Sathaliyawala,1 Mangala Rao,2 Danielle M. Maclean,2 Deborah L. Birx,2 Carl R. Alving,2 and Venigalla B. Rao1*

Department of Biology, The Catholic University of America, Washington, D.C.,1 Division of Retrovirology, Walter Reed Army Institute of Research, Rockville, Maryland2

Received 1 February 2006/ Accepted 30 April 2006

Bacteriophage T4 capsid is an elongated icosahedron decorated with 155 copies of Hoc, a nonessential highly antigenic outer capsid protein. One Hoc monomer is present in the center of each major capsid protein (gp23*) hexon. We describe an in vitro assembly system which allows display of HIV antigens, p24-gag, Nef, and an engineered gp41 C-peptide trimer, on phage T4 capsid surface through Hoc-capsid interactions. In-frame fusions were constructed by splicing the human immunodeficiency virus (HIV) genes to the 5' or 3' end of the Hoc gene. The Hoc fusion proteins were expressed, purified, and displayed on hoc– phage particles in a defined in vitro system. Single or multiple antigens were efficiently displayed, leading to saturation of all available capsid binding sites. The displayed p24 was highly immunogenic in mice in the absence of any external adjuvant, eliciting strong p24-specific antibodies, as well as Th1 and Th2 cellular responses with a bias toward the Th2 response. The phage T4 system offers new direction and insights for HIV vaccine development with the potential to increase the breadth of both cellular and humoral immune responses.

* Corresponding author. Mailing address: Department of Biology, 103 McCort Ward Hall, The Catholic University of America, 620 Michigan Ave., NE, Washington, DC 20064. Phone: (202) 319-5271. Fax: (202) 319-6161. E-mail: rao{at}cua.edu.

Journal of Virology, August 2006, p. 7688-7698, Vol. 80, No. 15
0022-538X/06/$08.00+0     doi:10.1128/JVI.00235-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Steers, N. J., Peachman, K. K., McClain, S. R., Alving, C. R., Rao, M. (2009). Human Immunodeficiency Virus Type 1 Gag p24 Alters the Composition of Immunoproteasomes and Affects Antigen Presentation. J. Virol. 83: 7049-7061 [Abstract] [Full Text]  
  • Comeau, A. M., Krisch, H. M. (2008). The Capsid of the T4 Phage Superfamily: The Evolution, Diversity, and Structure of Some of the Most Prevalent Proteins in the Biosphere. Mol Biol Evol 25: 1321-1332 [Abstract] [Full Text]  


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