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MAb ID	MAG 45 (#45, MAG45)
HXB2 Location	Env	Env Epitope Map
Author Location	gp120
Research Contact	C. Y. Kang, IDEC Inc, or Dr. Hariharam, IDEC Pharmaceuticals Corporation, La Jolla, CA
Epitope
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords	antibody binding site

Vaccine Details

Vaccine type	sCD4-gp120 complex
Vaccine strain	B clade HXB2
Vaccine component	gp120

Notes

Showing 5 of 5 notes.

MAG 45: IgG antibody phage display libraries were created from HIV-1+ individuals after pre-selection of PBMC with gp120, as an alternative to using bone marrow for generating libraries. MAG 45 was among a set of Abs used for competition studies to define the binding sites of the newly isolated MAbs, representing a MAb with a C1 epitope. Koefoed2005 (antibody binding site)
MAG 45: Called #45 -- a combination of gp41 fusion with the GNC4 trimeric sequences and disruption of the YU2 gp120-gp41 cleavage site resulted in stable gp140 trimers (gp140-GNC4) that preserve and expose some neutralizing epitopes while occluding some non-neutralizing epitopes -- CD4BS MAbs (F105 and F91) and CD4i (17b and 48d) recognized gp140-GNC4 as well as gp120 or gp140 -- non-neutralizing MAbs C11, A32, 522-149, M90, and #45 bound to the gp140-GNC4 glycoprotein at reduced levels compared to gp120 -- MAbs directed at the extreme termini of gp120 C1 (135/9 and 133/290) and C5 (CRA-1 and M91) bound efficiently to gp140-GNC4. Yang2000
MAG 45: Called #45 -- binds to efficiently sgp120 but not soluble gp120+gp41, suggesting its gp120 epitope is blocked by gp41 binding -- does not bind to HXBc2 gp120 if the 19 C-term amino acids, in conjunction with C1 positions 31-50, are deleted. Wyatt1997
MAG 45: Reciprocal binding inhibition with anti-C1-C5 and anti-C1-C4 discontinuous MAbs -- binding enhanced by anti-V3 5G11 -- inhibits binding of anti-CD4 binding site MAbs. Moore1996
MAG 45: Only observed amino acid substitution that reduces binding: 88 N/P -- does not bind to C1 region 20 mer peptides, tentative classification conformationally sensitive anti-C1 MAb. Kang1994

References

Showing 5 of 5 references.

Kang1994 C.-Y. Kang, K. Hariharan, P. L. Nara, J. Sodroski, and J. P. Moore. Immunization with a Soluble CD4-gp120 Complex Preferentially Induces Neutralizing Anti-Human Immunodeficiency Virus Type 1 Antibodies Directed to Conformation-Dependent Epitopes of gp120. J. Virol., 68:5854-5862, 1994. Most of the MAbs generated in this study were conformational, but there were four that bound a V3 loop peptide. These four could neutralize lab strains with different efficiencies. These MAbs were very sensitive to substitutions in the V3 loop, but also to substitutions in the base of the V1/V2 loop structure (120/121 VK/LE), indicating an underlying conformational character. Additionally, many anti-CD4 binding site MAbs were described, that shared a sensitivity to substitutions at residues 368 and 370. Another class of MAbs was found that appeared to be conformationally sensitive, and shared a reduction in binding with the amino acid substitution 88 N/P in the C1 domain. PubMed ID: 7520095. Show all entries for this paper.

Moore1996 J. P. Moore and J. Sodroski. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol., 70:1863-1872, 1996. 46 anti-gp120 monomer MAbs were used to create a competition matrix, and MAb competition groups were defined. The data suggests that there are two faces of the gp120 glycoprotein: a face occupied by the CD4BS, which is presumably also exposed on the oligomeric envelope glycoprotein complex, and a second face which is presumably inaccessible on the oligomer and interacts with a number of nonneutralizing antibodies. PubMed ID: 8627711. Show all entries for this paper.

Wyatt1997 R. Wyatt, E. Desjardin, U. Olshevsky, C. Nixon, J. Binley, V. Olshevsky, and J. Sodroski. Analysis of the Interaction of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein with the gp41 Transmembrane Glycoprotein. J. Virol., 71:9722-9731, 1997. This study characterized the binding of gp120 and gp41 by comparing Ab reactivity to soluble gp120 and to a soluble complex of gp120 and gp41 called sgp140. The occlusion of gp120 epitopes in the sgp140 complex provides a guide to the gp120 domains that interact with gp41, localizing them in C1 and C5 of gp120. Mutations that disrupt the binding of the occluded antibodies do not influence NAb binding or CD4 binding, thus if the gp41 binding domain is deleted, the immunologically desirable features of gp120 for vaccine design are still intact. PubMed ID: 9371638. Show all entries for this paper.

Yang2000 Xinzhen Yang, Michael Farzan, Richard Wyatt, and Joseph Sodroski. Characterization of Stable, Soluble Trimers Containing Complete Ectodomains of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins. J. Virol., 74(12):5716-5725, Jun 2000. PubMed ID: 10823881. Show all entries for this paper.

Koefoed2005 Klaus Koefoed, Lauge Farnaes, Meng Wang, Arne Svejgaard, Dennis R. Burton, and Henrik J. Ditzel. Molecular Characterization of the Circulating Anti-HIV-1 gp120-Specific B Cell Repertoire using Antibody Phage Display Libraries Generated from Pre-Selected HIV-1 gp120 Binding PBLs. J. Immunol. Methods, 297(1-2):187-201, Feb 2005. PubMed ID: 15777942. Show all entries for this paper.