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Displaying record number 3623

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MAb ID	BG18 (354BG18)
HXB2 Location	Env	Env Epitope Map
Author Location	gp160
Epitope
Subtype	B
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	P (tier 2) View neutralization details
Contacts and Features	View contacts and features
Species (Isotype)	human(IgG)
Patient	EB354
Immunogen	HIV-1 infection
Keywords	antibody binding site, antibody generation, broad neutralizer, immunotherapy, neutralization, review, structure, therapeutic vaccine

Notes

Showing 3 of 3 notes.

BG18:This review discusses the identification of super-Abs, where and how such Abs may be best applied and future directions for the field. BG18 was isolated from human B cell clones and is functionally similar to super-Abs PGT121, PGT128 and PGT135. Antigenic region V3 glycan (Table:1). Walker2018 (antibody binding site, review, broad neutralizer)
BG18: A 3.8^oA crystal structure of the anti-V3 glycan bNAb, BG18, complexed with natively glycosylated Env Clade A trimer (BG505) or Clade B trimer (B41) shows that while BG18 D-gene encoded residues contact with HIV-1 N332_gp120 and the gp120 GDIR peptide motif in a manner conserved with other V3/N332_gp120 bNAbs PGT121 and 10-1074; it has a distinct orientation. This novel orientation provides additional contacts with N392_gp120 and N386_gp120 oligomannose glycans at the base of V3- and also contacts residues of the V1-loops and is due to rearrangements in the V_H and V_L domains. The increased surface contact with Env could account for the high potency of BG18. VH1-2 CD4bs-binding IOMA Ab (and gp120-gp41 interface-spanning Ab 35O22) binding modes to the Env trimer were not altered by binding of 3 BG18 Fabs in crystal structures of BG18-BG505-35O22, BG18-41-35O22 or BG18-BG505-IOMA. Barnes2018 (therapeutic vaccine, structure)
BG18: Neutralizing antibodies were derived from long-term non-progressing donor EB354. Samples were donated at five different time points, enabling the isolation of three bNAbs (BG1, BG18, NC37) that largely account for the donor's serologic neutralizing activity. Sequencing of viruses from the donor revealed that viruses sensitive to the antibodies coexisted with the bNAbs for long periods of time. BG18, the most potent of the three antibodies, is directed against the Asn332 gp120-centered glycan patch at the base of the V3 loop. BG18 neutralized 64% of viruses in a 118-virus panel. BG18 utilizes germline genes IGHV4-4 and IGLV3-25. In a mouse model, monotherapy with BG18 transiently suppressed viremia, and the combination of BG18, NC37, and BG1 produced a prolonged and sustained drop in viremia. Freund2017 (antibody generation, neutralization, immunotherapy, structure)

References

Showing 3 of 3 references.

Isolation Paper
Freund2017 Natalia T. Freund, Haoqing Wang, Louise Scharf, Lilian Nogueira, Joshua A. Horwitz, Yotam Bar-On, Jovana Golijanin, Stuart A. Sievers, Devin Sok, Hui Cai, Julio C. Cesar Lorenzi, Ariel Halper-Stromberg, Ildiko Toth, Alicja Piechocka-Trocha, Harry B. Gristick, Marit J. van Gils, Rogier W. Sanders, Lai-Xi Wang, Michael S. Seaman, Dennis R. Burton, Anna Gazumyan, Bruce D. Walker, Anthony P. West, Jr., Pamela J. Bjorkman, and Michel C. Nussenzweig. Coexistence of Potent HIV-1 Broadly Neutralizing Antibodies and Antibody-Sensitive Viruses in a Viremic Controller. Sci. Transl. Med., 9(373), 18 Jan 2017. PubMed ID: 28100831. Show all entries for this paper.

Barnes2018 Christopher O. Barnes, Harry B. Gristick, Natalia T. Freund, Amelia Escolano, Artem Y. Lyubimov, Harald Hartweger, Anthony P. West, Jr., Aina E. Cohen, Michel C. Nussenzweig, and Pamela J. Bjorkman. Structural Characterization of a Highly-Potent V3-Glycan Broadly Neutralizing Antibody Bound to Natively-Glycosylated HIV-1 Envelope. Nat. Commun., 9(1):1251, 28 Mar 2018. PubMed ID: 29593217. Show all entries for this paper.

Walker2018 Laura M. Walker and Dennis R. Burton. Passive Immunotherapy of Viral Infections: `Super-Antibodies' Enter the Fray. Nat. Rev. Immunol., 18(5):297-308, May 2018. PubMed ID: 29379211. Show all entries for this paper.