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Found 17 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

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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
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

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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
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 648

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MAb ID MAG 55 (#55)
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact C. Y. Kang, IDEC Inc
Epitope
Ab Type gp120 CD4BS
Neutralizing L
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 3 of 3 notes.

References

Showing 3 of 3 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.

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.


Displaying record number 649

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MAb ID MAG 72 (L72)
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact C. Y. Kang or Dr. Hariharam, IDEC Pharmaceuticals Corp, La Jolla, CA
Epitope
Ab Type gp120 CD4BS
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.

Ditzel1997 H. J. Ditzel, P. W. Parren, J. M. Binley, J. Sodroski, J. P. Moore, C. F. Barbas, III, and D. R. Burton. Mapping the Protein Surface of Human Immunodeficiency Virus Type 1 gp120 Using Human Monoclonal Antibodies from Phage Display Libraries. J. Mol. Biol., 267:684-695, 1997. (Genbank: U82767 U82768 U82769 U82770 U82771 U82772 U82942 U82943 U82944 U82945 U82946 U82947 U82948 U82949 U82950 U82951 U82952 U82961 U82962) Recombinant monoclonal antibodies from phage display libraries provide a method for Env surface epitope mapping. Diverse epitopes are accessed by presenting gp120 to the library in different forms, such as sequential masking of epitopes with existing MAbs or sCD4 prior to selection or by selection on peptides. Fabs identified by these methods have specificities associated with epitopes presented poorly on native multimeric envelope. PubMed ID: 9126846. Show all entries for this paper.


Displaying record number 650

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MAb ID MAG 86
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact C. Y. Kang, IDEC Inc
Epitope
Ab Type gp120 CD4BS
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 651

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MAb ID MAG 96
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact C. Y. Kang, IDEC Inc
Epitope
Ab Type gp120 CD4BS
Neutralizing L
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 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.

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.


Displaying record number 652

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MAb ID MAG 116
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact C. Y. Kang, IDEC Inc
Epitope
Ab Type gp120 CD4BS
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 653

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MAb ID MAG 3B
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact C. Y. Kang, IDEC Inc
Epitope
Ab Type gp120 CD4BS
Neutralizing  
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 654

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MAb ID MAG 12B
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact C. Y. Kang, IDEC Inc
Epitope
Ab Type gp120 CD4BS
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 656

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MAb ID MAG 29B
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact C. Y. Kang, IDEC Inc
Epitope
Ab Type gp120 CD4BS
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 661

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MAb ID MAG 6B
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact C. Y. Kang, IDEC Inc
Epitope
Ab Type  
Neutralizing  
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 683

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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.

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.


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

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 685

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MAb ID MAG 97
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

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 686

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MAb ID MAG 104
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

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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