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Displaying record number 3720

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MAb ID	IOMA (IOMA.25)
HXB2 Location	Env	Env Epitope Map
Author Location	gp120
Epitope	(Discontinuous epitope)
Subtype	B
Ab Type	gp120 CD4BS
Neutralizing	Tier 2 View neutralization details
Contacts and Features	View contacts and features
Species (Isotype)	human(IgG1)
Patient	R1
Immunogen	HIV-1 infection
Keywords	antibody binding site, antibody generation, antibody interactions, antibody lineage, antibody sequence, binding affinity, broad neutralizer, glycosylation, neutralization, structure

Notes

Showing 2 of 2 notes.

IOMA: Analyses of all PDB HIV1-Env trimer (prefusion, closed) structures fulfilling certain parameters of resolution were performed to classify them on the basis of (a) antibody class which was informed by parental B cells as well as structural recognition, and (b) Env residues defining recognized HIV epitopes. Structural features of the 206 HIV epitope and bNAb paratopes were correlated with functional properties of the breadth and potency of neutralization against a 208-strain panel. bNAbs with >25% breadth of neutralization belonged to 20 classes of antibody with a large number of protruding loops and somatic hypermutation (SHM). HIV epitopes recognized placed the bNAbs into 6 categories (viz. V1V2, Glycan-V3, CD4-binding site, Silent face center, Fusion peptide and Subunit Interface). The epitopes contained high numbers of independent sequence segments and glycosylated surface area. IOMA-Env formed a distinct group within the CD4bs category, Class IOMA. IOMA has less rare SHM as well as CDRH3 characteristics, making it less difficult to re-elicit. Data for bNAb IOMA complexed to fully and natively glycosylated BG505 SOSIP.664 trimer as a 3.5A crystal structure was found in PDB ID: 5T3Z. Chuang2019 (antibody binding site, antibody interactions, neutralization, binding affinity, antibody sequence, structure, antibody lineage, broad neutralizer)
IOMA: Crystal structures of the HIV-1 Env trimer with fully processed and native glycosylation are presented, complexed with the V3-loop bNAb 10-1074 and IOMA, a new CD4bs bNAb. This is the first full description of the interplay between heterogeneous untrimmed high-mannose and complex-type N-glycans within the CD4bs and V3-loop epitopes, thereby revealing antibody-vulnerable glycan holes and roles of complex-type N-glycans on Env. IOMA bNAb defines a new class of CD4-mimetic bNAbs derived from the VH1-2*02 germline. It combines features of VH1-2/VRC01-class bNAbs with CD4-mimetic CD4bs bNAbs derived from the VH1-46 germline. IOMA is unique in having both an N279 gp120 /N280 gp120-W100F_HC interaction and a normal-length CDRL3, a combination made possible because its CDRL3 is displaced from gp120 loop D and toward the V5 loop. Like VH1-46 but unlike VH1-2 bNAbs, IOMA has a normal-length, 8-residue CDRL3 and fewer SHMs than VRC01-class bNAbs, yet neutralized 50% of tested strains with an IC50 of 2.3 µg/ml. Gristick2016 (antibody binding site, antibody generation, glycosylation, structure)

References

Showing 3 of 3 references.

Isolation Paper
Gristick2016 Harry B. Gristick, Lotta von Boehmer, Anthony P. West, Jr., Michael Schamber, Anna Gazumyan, Jovana Golijanin, Michael S. Seaman, Gerd Fätkenheuer, Florian Klein, Michel C. Nussenzweig, and Pamela J. Bjorkman. Natively Glycosylated HIV-1 Env Structure Reveals New Mode for Antibody Recognition of the CD4-Binding Site. Nat. Struct. Mol. Biol., 23(10):906-915, Oct 2016. PubMed ID: 27617431. 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.

Chuang2019 Gwo-Yu Chuang, Jing Zhou, Priyamvada Acharya, Reda Rawi, Chen-Hsiang Shen, Zizhang Sheng, Baoshan Zhang, Tongqing Zhou, Robert T. Bailer, Venkata P. Dandey, Nicole A. Doria-Rose, Mark K. Louder, Krisha McKee, John R. Mascola, Lawrence Shapiro, and Peter D. Kwong. Structural Survey of Broadly Neutralizing Antibodies Targeting the HIV-1 Env Trimer Delineates Epitope Categories and Characteristics of Recognition. Structure, 27(1):196-206.e6, 2 Jan 2019. PubMed ID: 30471922. Show all entries for this paper.