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Displaying record number 436

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MAb ID	5025B
HXB2 Location	gp160(309-316) DNA(7152..7172)	gp160 Epitope Map
Author Location	gp120(310-316 BH10)
Epitope	IQRGPGRA	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords	antibody generation, antibody lineage, binding affinity, novel epitope, optimal epitope

Vaccine Details

Notes

Showing 1 of 1 note.

• 5025B: Generation and fine mapping of murine MAbs. 5025B was raised in mice against PND (principal neutralization domain) RIQRGPGRAFV, specifically peptide RIQRGPGRAFVTIGK. Reactive epitope was IQRGPGRA (309-316) with the core being QRGPGR. Overall 5025B had high-intermediate affinity for the PND peptide. 316A was replaceable by many but not all amino acids. Langedijk1991 (antibody generation, optimal epitope, binding affinity, antibody lineage, novel epitope)

References

Showing 1 of 1 reference.

Langedijk1991 J. P. M. Langedijk, N. K. T. Back, P. J. Durda, J. Goudsmit, and R. H. Meloen. Neutralizing activity of anti-peptide antibodies against the principal neutralization domain of human immunodeficiency virus type 1. J. Gen. Virol., 72:2519-2526, 1991. MAbs were raised against RIQRGPGRAFVTIGK by immunizing mice. Fine structure of MAb binding sites was mapped using pepscan. Preservation of the $\beta$ turn at the tip of the loop was critical. PubMed ID: 1919529. Show all entries for this paper.

Displaying record number 437

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MAb ID	5023B
HXB2 Location	gp160(309-316) DNA(7149..7172)	gp160 Epitope Map
Author Location	gp120(309-316 BH10)
Epitope	IQRGPGRA	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords	antibody generation, antibody interactions, binding affinity, novel epitope, optimal epitope

Vaccine Details

Notes

Showing 1 of 1 note.

• 5023B: Generation and fine mapping of murine MAbs. 5023B was raised in mice against PND (principal neutralization domain) RIQRGPGRAFV, specifically peptide RIQRGPGRAFVTIGK. Reactive epitope was IQRGPGRA (309-316) with the optimal core being IQRGP. 315R and 316A had a minor contributions to reactivity. Langedijk1991 (antibody generation, antibody interactions, optimal epitope, binding affinity, novel epitope)

References

Showing 1 of 1 reference.

Langedijk1991 J. P. M. Langedijk, N. K. T. Back, P. J. Durda, J. Goudsmit, and R. H. Meloen. Neutralizing activity of anti-peptide antibodies against the principal neutralization domain of human immunodeficiency virus type 1. J. Gen. Virol., 72:2519-2526, 1991. MAbs were raised against RIQRGPGRAFVTIGK by immunizing mice. Fine structure of MAb binding sites was mapped using pepscan. Preservation of the $\beta$ turn at the tip of the loop was critical. PubMed ID: 1919529. Show all entries for this paper.

Displaying record number 492

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MAb ID	5021
HXB2 Location	gp160(310-316) DNA(7152..7172)	gp160 Epitope Map
Author Location	gp120
Epitope	IQRGPGRA	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords	antibody generation, antibody interactions, binding affinity, novel epitope, optimal epitope

Vaccine Details

Notes

Showing 2 of 2 notes.

• 5021: Binding to native gp120 100-300 fold greater than to denatured -- 314G/W substitution abolishes binding, changes outside the loop have little effect. Moore1993c
• 5021: Generation and fine mapping of murine MAbs. 5021 was raised in mice against PND (principal neutralization domain) RIQRGPGRAFV, specifically peptide RIQRGPGRAFVTIGK. Reactive epitope was IQRGPGRA (309-316) with the optimal core being GPGRA. 309I had a minor contribution to reactivity, while 311R had none. Langedijk1991 (antibody generation, antibody interactions, optimal epitope, binding affinity, novel epitope)

References

Showing 4 of 4 references.

Durda1988 P. J. Durda, B. Leece, A. M. Jenoski, H. Rabin, A. Fisher, R. Gallo, and F. Wong-Staal. Characterization of Murine Monoclonal Antibodies to HIV-1 Induced by Synthetic Peptides. AIDS Res. Hum. Retroviruses, 4:331-342, 1988. PubMed ID: 2848556. Show all entries for this paper.

Durda1990 P. J. Durda, L. Bacheler, P. Clapham, A. M. Jenoski, B. Leece, T. J. Matthews, A. McKnight, R. Pomerantz, M. Rayner, and K. J. Weinhold. HIV-1 Neutralizing Monoclonal Antibodies Induced by a Synthetic Peptide. AIDS Res. Hum. Retroviruses, 6:1115, 1990. PubMed ID: 1702301. Show all entries for this paper.

Langedijk1991 J. P. M. Langedijk, N. K. T. Back, P. J. Durda, J. Goudsmit, and R. H. Meloen. Neutralizing activity of anti-peptide antibodies against the principal neutralization domain of human immunodeficiency virus type 1. J. Gen. Virol., 72:2519-2526, 1991. MAbs were raised against RIQRGPGRAFVTIGK by immunizing mice. Fine structure of MAb binding sites was mapped using pepscan. Preservation of the $\beta$ turn at the tip of the loop was critical. PubMed ID: 1919529. Show all entries for this paper.

Moore1993c J. P. Moore, M. Thali, B. A. Jameson, F. Vignaux, G. K. Lewis, S.-W. Poon, M. S. Fung, P. J. Durda, L. Akerblom, B. Wahren, D. D. Ho, Q. J. Sattentau, and J. Sodroski. Immunochemical Analysis of the gp120 Surface Glycoprotein of Human Immunodeficiency Virus Type 1: Probing the Structure of the C4 and V4 Domains and the Interaction of the C4 Domain with the V3 Loop. J. Virol., 73:4785-4796, 1993. General observations: C4 and V3 MAbs are sensitive to the way the epitopes are presented, and this sensitivity cannot be correlated to peptide binding. Some V3-C4 domain interaction was indicated based on mutation and interference studies. PubMed ID: 7687303. Show all entries for this paper.