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Displaying record number 684

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MAb ID	MAG 95
HXB2 Location	Env	Env Epitope Map
Author Location	gp120
Research Contact	C. Y. Kang, IDEC Inc
Epitope
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords

Vaccine Details

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

Notes

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MAG 95: 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

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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.