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Found 4 matching records:

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
NTRKSIRIQRGPGRAFVTIG epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) mouse
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

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

Notes

Showing 2 of 2 notes.

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
NTRKSIRIQRGPGRAFVTIG epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) mouse
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

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

Notes

Showing 1 of 1 note.

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

Download this epitope record as JSON.

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

Vaccine Details

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

Notes

Showing 1 of 1 note.

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

Download this epitope record as JSON.

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
NTRKSIRIQRGPGRAFVTIG epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) mouse
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

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

Notes

Showing 1 of 1 note.

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.


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