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Displaying record number 2700

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MAb ID	11H6H1
HXB2 Location	Tat(6-14) DNA(5846..5872)	Tat Epitope Map
Author Location
Epitope	PKLEPWHP	Epitope Alignment
Ab Type	N-term
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords	antibody binding site, antibody generation, binding affinity

Vaccine Details

Notes

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• 11H6H1: The 11H6H1 MAb, specific for N-terminal region of Tat, was obtained after immunization of mice with the N-terminus of the HIV-1 Tat2.1 protein (Glu2-Pro18) and clonal selection of hybridoma against the immunizing antigen. The minimal epitope recognized by 11H6H1 was restricted to the 9-mer peptide 6PKLEPWKHP14 centered on Trp11. The substitution of Trp11 by a phenylalanine completely abolished the binding of 11H6H1, whereas the transactivating activity of Tat was preserved. MAb 11H6H1 recognized the full-length active Tat and the smaller 15-mer peptide and the 9-mer minimal epitope with similar affinities, suggesting that the antibody/peptide interaction is close to that observed with the full-length protein. The crystal structure of the N-terminal Tat region stabilized with MAb 11H6H1 was solved and revealed that 15-mer and 9-mer Tat peptides adopt a standard type I β-turn conformation. The central Trp11 that is critical for Fab′ recognition was further stabilized by π-stacking interactions. Serriere2011 (antibody binding site, antibody generation, binding affinity)

References

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Isolation Paper
Serriere2011 Jennifer Serrière, Jean-Marc Dugua, Marc Bossus, Bernard Verrier, Richard Haser, Patrice Gouet, and Christophe Guillon. Fab'-Induced Folding of Antigenic N-Terminal Peptides from Intrinsically Disordered HIV-1 Tat Revealed by X-Ray Crystallography. J. Mol. Biol., 405(1):33-42, 7 Jan 2011. PubMed ID: 21035463. Show all entries for this paper.