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J. Biol. Chem., Vol. 280, Issue 32, 28959-28965, August 12, 2005

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Antigenic Properties of Peptide Mimotopes of HIV-1-associated Carbohydrate Antigens^*

Anastas Pashov, Gabriela Canziani¶, Behjatolah Monzavi-Karbassi, Srini V. Kaveri||, Stewart MacLeod, Rinku Saha, Marty Perry**, Thomas C. VanCott, and Thomas Kieber-Emmons

From the Department of Pathology, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205, ^¶Centocor, Inc., Radnor, Pennsylvania 19087, the ^**Department of Chemistry, Ouachita Baptist University, Arkadelphia, Arkansas 71998, Advanced BioScience Laboratories, Inc., Kensington, Maryland 20895, and ^||INSERM U681, Immunopathologie et Immunointervention Thérapeutique, Institut Biomédical des Cordeliers, 75006 Paris, France

The glycan shield of the human immunodeficiency virus (HIV) envelope protein presents many potential epitopes for vaccine development. To augment immune responses to HIV, type 1 (HIV-1), envelope-associated carbohydrate antigens, we are defining peptide mimics of HIV-associated carbohydrate antigens that function as antigen mimotopes that upon immunization will induce antibodies cross-reactive with carbohydrate antigens. We have previously defined peptides with a putative sequence tract RYRY that mimic concanavalin A-binding glycans. To imitate the multivalent binding of carbohydrates, we compared the avidity of a linear (911) and cyclic peptide (D002) reactive with concanavalin A presented in a multiple antigen peptide (MAP) format. The affinity of the MAP-D002 peptide was higher than that of the peptide MAP-911, whereas the avidity of D002 peptide was lower than that of 911. Serum from mice immunized with MAP-911 had lower titer for oligomannose-9 than those elicited by MAP-D002 under the same conditions, but both immunogens elicited antibodies that can block the binding of GP120 to dendritic cells. Antibodies that bind to the studied MAPs were found in a preparation of normal human immunoglobulin for intravenous use. Those that were purified on 911 bound back to 911 and D002, whereas anti-D002 antibodies were specific only for D002. Human antibodies reactive with both mimotopes and with a mannosyl preparation were observed to bind to envelope protein. These results suggested the potential to fine-tune the antibody response to carbohydrate antigens by modifying structural features of peptide mimotope-based immunogens.

Received for publication, March 17, 2005 , and in revised form, May 23, 2005.

^* This work was supported by National Institutes of Health Grant R01AI049092, the Arkansas BRIN Program, and the Arkansas BioSciences Institute. 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.

Both authors contributed equally to this work.

To whom correspondence should be addressed: Dept. of Pathology, ACRC No. 824, University of Arkansas for Medical Sciences, 4301 Markham St., Little Rock, AR 72205. E-mail: tke{at}uams.edu.

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