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Displaying record number 3561

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MAb ID	VRC22.01
HXB2 Location	gp160	gp160 Epitope Map
Author Location	Env
Epitope
Subtype	B
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	P (tier 2) View neutralization details
Species (Isotype)	human
Patient	N170
Immunogen	HIV-1 infection
Keywords	antibody binding site, antibody generation, antibody sequence, neutralization

Notes

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VRC22.01: The study compared the binding characteristics of V3-glycan antibodies, including 3 newly-derived lineages of broadly neutralizing mAbs from Donor N170. All 8 of the N170-derived mAbs bound to the JR-FL SOSIP trimer, and poorly or not at all to gp120 monomer. All were highly dependent on the N301 and N332 glycans, but with small differences in their preference and their angle of approach to V3. The gene usage for VRC22.01 is given as: IGHV 4-34*01, IGHJ 6*01, IGLV K1-17*01, IGLJ K1*01. At IC₅₀, it neutralized 24% of a panel of 28 pseudoviruses of clades A, B, and C. Longo2016 (antibody binding site, antibody generation, neutralization, antibody sequence)

References

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Isolation Paper
Longo2016 Nancy S. Longo, Matthew S. Sutton, Andrea R. Shiakolas, Javier Guenaga, Marissa C. Jarosinski, Ivelin S. Georgiev, Krisha McKee, Robert T. Bailer, Mark K. Louder, Sijy O'Dell, Mark Connors, Richard T. Wyatt, John R. Mascola, and Nicole A. Doria-Rose. Multiple Antibody Lineages in One Donor Target the Glycan-V3 Supersite of the HIV-1 Envelope Glycoprotein and Display a Preference for Quaternary Binding. J. Virol., 90(23):10574-10586, 1 Dec 2016. PubMed ID: 27654288. Show all entries for this paper.