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J. Biol. Chem., Vol. 281, Issue 40, 29675-29683, October 6, 2006

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Multiple Antigenic Mimotopes of HIV Carbohydrate Antigens

Relating Structure and Antigenicity^*

Anastas D. Pashov, Jason Plaxco, Srinivas V. Kaveri, Behjatolah Monzavi-Karbassi, Donald Harn^¶, and Thomas Kieber-Emmons¹

From the Department of Pathology, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205, INSERM U681, Immunopathologie et Immunointervention Thérapeutique, Institut Biomédical des Cordeliers, 75006 Paris, France, and the ^¶Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts 02115

Carbohydrate mimetic peptides are designable, and they can carry T-cell epitopes and circumvent tolerance. A mimic-based human immunodeficiency virus (HIV) vaccine can be a viable alternative to carbohydrate-based antigens if the diversity of epitopes found on gp120 can be recapitulated. To improve existing mimics, an attempt was made to study the structural correlates of the observed polyspecificity of carbohydrate mimetic peptides based on the Y(P/R)Y motif in more detail. A carbohydrate mimetic peptide, D002 (RGGLCYCRYRYCVCVGR), bound a number of lectins with different specificities. Although this peptide reacted strongly with both lotus and concanavalin A (ConA) lectins, it bound to lotus stronger than ConA. By varying the central motif RYRY, five versions were produced in multiple antigen peptide format, and their avidity for lotus and ConA lectins was tested by surface plasmon resonance. Although the kinetic parameters were similar, the version based on the sequence YPYRY had an optimal affinity for both lectins as well as improved avidity for wheat germ agglutinin and phytohemagglutinin. Thus, as far as lectin specificity is concerned, YPYRY had improved multiple antigenic properties. Both RYRY and YPYRY precipitated antibodies from human IgG for intravenous use that bound to gp120 in vitro and immunoprecipitated gp120 from transfected CHO-PI cells. Thus, Y(P/R)Y motifs mimic multiple carbohydrate epitopes, many of which are found on HIV, and preimmune human IgG antibodies that bind to HIV carbohydrates cross-react to a comparable extent with both RYRY and YPYRY carbohydrate mimetic peptides.

Received for publication, May 1, 2006 , and in revised form, August 9, 2006.

^* This work was supported by National Institutes of Health Grant AI-49092. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Pathology, University of Arkansas for Medical Sciences, 4301 W. Markham St., Little Rock, AR 72205. Tel.: 501-526-7875; Fax: 501-526-25934; E-mail: tke{at}uams.edu.

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