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Journal of Virology, December 2004, p. 12975-12986, Vol. 78, No. 23
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.23.12975-12986.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Characterization of the Outer Domain of the gp120 Glycoprotein from Human Immunodeficiency Virus Type 1

Xinzhen Yang,1,2 Vesko Tomov,1 Svetla Kurteva,1 Liping Wang,1 Xinping Ren,1,2 Miroslaw K. Gorny,3 Susan Zolla-Pazner,3,4 and Joseph Sodroski1,2,5*

Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute,1 Department of Pathology, Division of AIDS, Harvard Medical School,2 Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts,5 Department of Pathology, New York University School of Medicine,3 Research Enhancement Award Program, Veterans Affairs New York Harbor System, New York, New York4

Received 4 June 2004/ Accepted 3 August 2004

The core of the gp120 glycoprotein from human immunodeficiency virus type 1 (HIV-1) is comprised of three major structural domains: the outer domain, the inner domain, and the bridging sheet. The outer domain is exposed on the HIV-1 envelope glycoprotein trimer and contains binding surfaces for neutralizing antibodies such as 2G12, immunoglobulin G1b12, and anti-V3 antibodies. We expressed the outer domain of HIV-1YU2 gp120 as an independent protein, termed OD1. OD1 efficiently bound 2G12 and a large number of anti-V3 antibodies, indicating its structural integrity. Immunochemical studies with OD1 indicated that antibody responses against the outer domain of the HIV-1 gp120 envelope glycoprotein are rare in HIV-1-infected human sera that potently neutralize the virus. Surprisingly, such outer-domain-directed antibody responses are commonly elicited by immunization with recombinant monomeric gp120. Immunization with soluble, stabilized HIV-1 envelope glycoprotein trimers elicited antibody responses that more closely resembled those in the sera of HIV-1-infected individuals. These results underscore the qualitatively different humoral immune responses elicited during natural infection and after gp120 vaccination and help to explain the failure of gp120 as an effective vaccine.

* Corresponding author. Mailing address: Dana-Farber Cancer Institute, 44 Binney St., JFB 824, Boston, MA 02115. Phone: (617) 632-3371. Fax: (671) 632-4338. E-mail: joseph_sodroski{at}dfci.harvard.edu.

Journal of Virology, December 2004, p. 12975-12986, Vol. 78, No. 23
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.23.12975-12986.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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