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Displaying record number 408

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MAb ID	MAG 49 (#49)
HXB2 Location	gp160(302-321) DNA(7128..7187)	gp160 Epitope Map
Author Location	gp120(302-321 BH10)
Epitope	NTRKSIRIQRGPGRAFVTIG	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Notes

Showing 2 of 2 notes.

• MAG 49: Called #49 in this text. Binding enhanced by anti-C1 MAbs 133/290, 135/9, and by many anti-CD4 binding site MAbs -- reciprocal enhancement of some anti-V2 MAbs -- reciprocal binding inhibition of anti-V3 MAbs. Moore1996
• MAG 49: Binds a V3 loop peptide -- sensitive to both V3 loop mutations and a mutation at the base of the V1/V2 loop structure (120/121 VK/LE) Kang1994

References

Showing 2 of 2 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.

Displaying record number 409

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MAb ID	MAG 53
HXB2 Location	gp160(302-321) DNA(7128..7187)	gp160 Epitope Map
Author Location	gp120(302-321 BH10)
Epitope	NTRKSIRIQRGPGRAFVTIG	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Notes

Showing 1 of 1 note.

• MAG 53: Binds a V3 loop peptide -- sensitive to both V3 loop mutations and a mutation at the base of the V1/V2 loop structure (120/121 VK/LE) Kang1994

References

Showing 1 of 1 reference.

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.

Displaying record number 410

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MAb ID	MAG 56
HXB2 Location	gp160(302-321) DNA(7128..7187)	gp160 Epitope Map
Author Location	gp120(302-321)
Epitope	NTRKSIRIQRGPGRAFVTIG	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Notes

Showing 1 of 1 note.

• MAG 56: Binds a V3 loop peptide -- sensitive to both V3 loop mutations and a mutation at the base of the V1/V2 loop structure (120/121 VK/LE) Kang1994

References

Showing 1 of 1 reference.

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.

Displaying record number 411

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MAb ID	MAG 109
HXB2 Location	gp160(302-321) DNA(7128..7187)	gp160 Epitope Map
Author Location	gp120(302-321 BH10)
Epitope	NTRKSIRIQRGPGRAFVTIG	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Notes

Showing 1 of 1 note.

• MAG 109: Binds a V3 loop peptide -- sensitive to both V3 loop mutations and a mutation at the base of the V1/V2 loop structure (120/121 VK/LE) Kang1994

References

Showing 1 of 1 reference.

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.