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Displaying record number 2530

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MAb ID	a4 (Maba4)
HXB2 Location	Pol(862-881) DNA(4668..4727)	Pol Epitope Map
Author Location	Integrase(147-166 HXB2)
Epitope	SQGVVESMNKELKKIIGQVR	Epitope Alignment
Epitope Name	pep-a4
Ab Type	Integrase catalytic core
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords	antibody binding site, antibody generation, binding affinity, escape

Vaccine Details

Notes

Showing 1 of 1 note.

• a4: MAba4 was obtained by immunizing a mouse with IN peptide K159 (SQGVVESMNKELKKIIGQVRDQAEHLKTA); a4 recognized the N-terminal portion SQGVVESMNKELKKIIGQVR of K159 (pep-a4). A strong antigenic crossreactivity was observed between pep-a4 and the K159, as well as K156, a stabilized analogue of pep-a4 constrained into helix by seven helicogenic mutations, indicating that the epitope is freely accessible to the antibody inside the protein and that its recognition by the antibody is not influenced by the conformation of its backbone and the chemistry of amino acids submitted to helicogenic mutations. In contrast, the AA →Glu mutations of the hydrophilic residues Gln148, Lys156 and Lys159, known for their interactions with LTRs (long terminal repeats) and inhibitors (5CITEP, for instance), significantly impaired the binding of K156 to the antibody. Azzi2010 (antibody binding site, antibody generation, escape, binding affinity)

References

Showing 1 of 1 reference.

Isolation Paper
Azzi2010 Sandy Azzi, Vincent Parissi, Richard G. Maroun, Pierre Eid, Olivier Mauffret, and Serge Fermandjian. The HIV-1 Integrase alpha4-Helix Involved in LTR-DNA Recognition Is Also a Highly Antigenic Peptide Element. PLoS One, 5(12):e16001, 2010. PubMed ID: 21209864. Show all entries for this paper.