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Displaying record number 2775

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MAb ID	1-863/5-25
HXB2 Location	gp160	gp160 Epitope Map
Author Location
Epitope
Ab Type	gp120 CD4i, gp120 V3 // V3 glycan (V3g), gp41
Neutralizing	P
Species (Isotype)	human(IgG)
Patient
Immunogen	HIV-1 infection
Keywords	antibody generation, binding affinity, broad neutralizer, neutralization

Notes

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1-863/5-25: A bispecific Ab (BiAb) that can bind bivalently by virtue of one scFv arm recognizing gp120 and a second arm recognizing gp41, has been engineered to show increased neutralizing potency. The individual arms of the BiAbs preserved the binding specificities of the original anti-HIV IgGs (1-863 and 5-25) and together bound simultaneously to gp120 and gp41. Results showed that heteroligation by bivalent antibody binding to two different epitopes on gp160 can lead to enhanced recognition and more efficient viral neutralization compared to the parental antibodies. Repertoire and reactivity of the antibodies are described in Table S1. It showed strong neutralizing activity against DJ263.8 (Clade A), SS1196.1 and 6535.3 (Clade B)viruses. Mouquet2012 (antibody generation, neutralization, binding affinity, broad neutralizer)

References

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Isolation Paper
Mouquet2012 Hugo Mouquet, Malte Warncke, Johannes F. Scheid, Michael S. Seaman, and Michel C. Nussenzweig. Enhanced HIV-1 Neutralization by Antibody Heteroligation. Proc. Natl. Acad. Sci. U.S.A., 109(3):875-880, 17 Jan 2012. PubMed ID: 22219363. Show all entries for this paper.