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J Biol Chem, Vol. 273, Issue 16, 9951-9958, April 17, 1998

Characterization of V3 Loop-Pseudomonas Exotoxin Chimeras
CANDIDATE VACCINES FOR HUMAN IMMUNODEFICIENCY VIRUS-1

David J. FitzGerald, Charlotte M. Fryling, Marian L. McKee, JoAnn C. Vennari^¶, Terri Wrin^¶, Mary E. M. Cromwell, Ann L. Daugherty, and Randall J. Mrsny

From the  Biotherapy Section, Laboratory of Molecular Biology, Division of Basic Science, NCI, National Institutes of Health, Bethesda, Maryland 20892-4255 and ^¶ Cell Banking and  Drug Delivery/Biology, Pharmaceutical Research and Development, Genentech Inc., South San Francisco, California 94080-4990

To develop a candidate vaccine for human immunodeficiency virus, type 1 (HIV-1), chimeric proteins were constructed by inserting sequences derived from the V3 loop of gp120 into a nontoxic form of Pseudomonas exotoxin (PE). Inserts of 14 or 26 amino acids, constrained by a disulfide bond, were introduced between domains II and III of PE. V3 loop-toxin proteins expressed in Escherichia coli and corresponding to either MN (subtype B) or Thai (subtype E) strains, were recognized by strain-specific monoclonal anti-gp120 antibodies. When loop sequences were introduced into an enzymatically active form of the toxin, there was no loss of toxin-mediated cell killing, suggesting that these sequences were co-transported to the cytosol. Sera from rabbits injected with nontoxic PE-V3 loop chimeras were reactive for strain-specific gp120s in Western blots, immunocapture assays, enzyme-linked immunosorbent assays, and neutralized HIV-1 infectivity. Since toxin vectors were designed to receive oligonucleotide duplexes encoding any V3 loop sequence, this approach should allow for the production of V3 loop-toxin chimeras corresponding to multiple HIV isolates.

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