HIV molecular immunology database

 

Search Antibody Database

Found 6 matching records:

Displaying record number 488

Download this epitope record as JSON.

MAb ID 924
HXB2 Location gp160(304-314)
DNA(7134..7166)
gp160 Epitope Map
Author Location gp120(309-318 IIIB)
Epitope RKSIRIQRGPG Epitope Alignment
RKSIRIQRGPG epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing  
Species (Isotype) mouse(IgG1κ)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type vaccinia
Vaccine strain B clade IIIB
Vaccine component gp160

Notes

Showing 6 of 6 notes.

References

Showing 7 of 7 references.

Chesebro1988 B. Chesebro and K. Wehrly. Development of a Sensitive Quantitative Focal Assay for Human Immunodeficiency Virus Infectivity. J. Virol., 62:3779-3788, 1988. PubMed ID: 3047430. Show all entries for this paper.

Pincus1991 S. H. Pincus, R. L. Cole, E. M. Hersh, D. Lake, Y. Masuho, P. J. Durda, and J. McClure. In Vitro Efficacy of Anti-HIV Immunotoxins Targeted by Various Antibodies to the Envelope Protein. J. Immunol., 146:4315-4324, 1991. Six MAbs, (907, 924, 110.1, 41.1, 86 and P5-3) and polyclonal pooled serum antibodies purified on gp160 were coupled to RAC to create immunotoxins. Only 41.1-RAC, an anti-gp41 MAb-immunotoxin and the polyclonal immunotoxin showed direct activity against multiple strains, and activity of an immunotoxin was found not to be directly correlated with cell surface binding. PubMed ID: 1710247. Show all entries for this paper.

Pincus1993 S. H. Pincus and J. McClure. Soluble CD4 Enhances the Efficacy of Immunotoxins Directed against gp41 of the Human Immunodeficiency Virus. Proc. Natl. Acad. Sci. U.S.A., 90:332-336, 1993. PubMed ID: 8419938. Show all entries for this paper.

Pincus1993a S. H. Pincus, K. G. Messer, D. H. Schwartz, G. K. Lewis, B. S. Graham, W. A. Blattner, and G. Fisher. Differences in the Antibody Response to Human Immunodeficiency Virus-1 Envelope Glycoprotein (gp160) in Infected Laboratory Workers and Vaccinees. J. Clin. Invest., 91:1987-1996, 1993. PubMed ID: 7683694. Show all entries for this paper.

Cook1994 D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of Human Immunodeficiency Virus Type 1 HIV-1 gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533. Show all entries for this paper.

Pincus1996 S. H. Pincus, K. Wehrly, R. Cole, H. Fang, G. K. Lewis, J. McClure, A. J. Conley, B. Wahren, M. R. Posner, A. L. Notkins, S. A. Tilley, A. Pinter, L. Eiden, M. Teintze, D. Dorward, and V. V. Tolstikov. In Vitro Effects of Anti-HIV Immunotoxins Directed against Multiple Epitopes on HIV Type 1 Envelope Glycoprotein 160. AIDS Res. Hum. Retroviruses, 12:1041-1051, 1996. A panel of anti-gp160 MAbs to was used to construct anti-HIV immunotoxins by coupling antibodies to ricin A chain (RAC). The ability of the immunotoxins to kill HIV-1-infected cells was tested in tissue culture. Immunotoxins that bind epitopes on the cell surface killed infected cells, although killing was not directly proportional to binding. The activity of anti-gp41 immunotoxins was markedly enhanced in the presence of sCD4. PubMed ID: 8827220. Show all entries for this paper.

Pincus1998 S. H. Pincus, R. L. Cole, R. Watson-McKown, A. Pinter, W. Honnen, B. Cole, and K. S. Wise. Immunologic Cross-Reaction between HIV Type 1 p17 and Mycoplasma hyorhinis Variable Lipoprotein. AIDS Res. Hum. Retroviruses, 14:419-425, 1998. PubMed ID: 9546801. Show all entries for this paper.


Displaying record number 489

Download this epitope record as JSON.

MAb ID 907
HXB2 Location gp160(304-314)
DNA(7134..7166)
gp160 Epitope Map
Author Location gp120(309-318)
Epitope RKSIRIQRGPG Epitope Alignment
RKSIRIQRGPG epitope logo
Ab Type  
Neutralizing L
Species (Isotype) mouse(IgG1κ)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type vaccinia
Vaccine strain B clade IIIB
Vaccine component gp160

Notes

Showing 4 of 4 notes.

References

Showing 4 of 4 references.

Chesebro1988 B. Chesebro and K. Wehrly. Development of a Sensitive Quantitative Focal Assay for Human Immunodeficiency Virus Infectivity. J. Virol., 62:3779-3788, 1988. PubMed ID: 3047430. Show all entries for this paper.

Pincus1989 S. H. Pincus, K. Wehrly, and B. Chesebro. Treatment of HIV Tissue Culture Infection with Monoclonal Antibody-Ricin A Chain Conjugates. J. Immunol., 142:3070-3075, 1989. PubMed ID: 2540236. Show all entries for this paper.

Pincus1991 S. H. Pincus, R. L. Cole, E. M. Hersh, D. Lake, Y. Masuho, P. J. Durda, and J. McClure. In Vitro Efficacy of Anti-HIV Immunotoxins Targeted by Various Antibodies to the Envelope Protein. J. Immunol., 146:4315-4324, 1991. Six MAbs, (907, 924, 110.1, 41.1, 86 and P5-3) and polyclonal pooled serum antibodies purified on gp160 were coupled to RAC to create immunotoxins. Only 41.1-RAC, an anti-gp41 MAb-immunotoxin and the polyclonal immunotoxin showed direct activity against multiple strains, and activity of an immunotoxin was found not to be directly correlated with cell surface binding. PubMed ID: 1710247. Show all entries for this paper.

Pincus1996 S. H. Pincus, K. Wehrly, R. Cole, H. Fang, G. K. Lewis, J. McClure, A. J. Conley, B. Wahren, M. R. Posner, A. L. Notkins, S. A. Tilley, A. Pinter, L. Eiden, M. Teintze, D. Dorward, and V. V. Tolstikov. In Vitro Effects of Anti-HIV Immunotoxins Directed against Multiple Epitopes on HIV Type 1 Envelope Glycoprotein 160. AIDS Res. Hum. Retroviruses, 12:1041-1051, 1996. A panel of anti-gp160 MAbs to was used to construct anti-HIV immunotoxins by coupling antibodies to ricin A chain (RAC). The ability of the immunotoxins to kill HIV-1-infected cells was tested in tissue culture. Immunotoxins that bind epitopes on the cell surface killed infected cells, although killing was not directly proportional to binding. The activity of anti-gp41 immunotoxins was markedly enhanced in the presence of sCD4. PubMed ID: 8827220. Show all entries for this paper.


Displaying record number 581

Download this epitope record as JSON.

MAb ID 110.1 (110-1)
HXB2 Location gp160(491-500)
DNA(7695..7724)
gp160 Epitope Map
Author Location gp120(491-500 LAI)
Research Contact Genetic Systems Corp, Seattle WA, E. Kinney-Thomas
Epitope IEPLGVAPTK Epitope Alignment
IEPLGVAPTK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) mouse(IgG1κ)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody generation, immunotoxin

Vaccine Details

Vaccine type HIV infected-cell lysate
Vaccine strain B clade BRU
Vaccine component HIV-1

Notes

Showing 11 of 11 notes.

References

Showing 12 of 12 references.

Isolation Paper
Gosting1987 L. H. Gosting, J. McClure, E. S. Dickinson, S. M. Watanabe, K. Shriver, and L. C. Goldstein. Monoclonal antibodies to gp110 and gp41 of human immunodeficiency virus. J. Clin. Microbiol., 25:845-848, 1987. PubMed ID: 2438302. Show all entries for this paper.

Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.

Callahan1991 Lawrence N. Callahan, Michael Phelan, Margherita Mallinson, and Michael A. Norcross. Dextran Sulfate Blocks Antibody Binding to the Principal Neutralizing Domain of Human Immunodeficiency Virus Type 1 without Interfering with gp120-CD4 Interactions. J. Virol., 65(3):1543-1550, Mar 1991. PubMed ID: 1995952. Show all entries for this paper.

Cook1994 D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of Human Immunodeficiency Virus Type 1 HIV-1 gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.

Linsley1988 P. S. Linsley, J. A. Ledbetter, E. Kinney-Thomas, and S.-L. Hu. Effects of Anti-gp120 Monoclonal Antibodies on CD4 Receptor Binding by the env Protein of Human Immunodeficiency Virus Type 1. J. Virol., 62:3695-3702, 1988. PubMed ID: 2458487. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

McDougal1996 J. S. McDougal, M. S. Kennedy, S. L. Orloff, J. K. A. Nicholson, and T. J. Spira. Mechanisms of Human Immunodeficiency Virus Type 1 (HIV-1) Neutralization: Irreversible Inactivation of Infectivity by Anti-HIV-1 Antibody. J. Virol., 70:5236-5245, 1996. Studies of polyclonal sera autologous virus inactivation indicates that in individuals over time, viral populations emerge that are resistant to inactivating effects of earlier sera. PubMed ID: 8764033. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Pincus1991 S. H. Pincus, R. L. Cole, E. M. Hersh, D. Lake, Y. Masuho, P. J. Durda, and J. McClure. In Vitro Efficacy of Anti-HIV Immunotoxins Targeted by Various Antibodies to the Envelope Protein. J. Immunol., 146:4315-4324, 1991. Six MAbs, (907, 924, 110.1, 41.1, 86 and P5-3) and polyclonal pooled serum antibodies purified on gp160 were coupled to RAC to create immunotoxins. Only 41.1-RAC, an anti-gp41 MAb-immunotoxin and the polyclonal immunotoxin showed direct activity against multiple strains, and activity of an immunotoxin was found not to be directly correlated with cell surface binding. PubMed ID: 1710247. Show all entries for this paper.

Thomas1988 E. Kinney Thomas, J. N. Weber, J. McClure, P. R. Clapham, M. C. Singhal, M. K. Shriver, and R. A. Weiss. Neutralizing Monoclonal Antibodies to the AIDS Virus. AIDS, 2:25-29, 1988. PubMed ID: 2451922. Show all entries for this paper.

Valenzuela1998 A. Valenzuela, J. Blanco, B. Krust, R. Franco, and A. G. Hovanessian. Neutralizing Antibodies against the V3 Loop of Human Immunodeficiency Type 1 gp120 Block the CD4-Dependent and Independent Binding of the Virus to Cells. J. Virol., 71:8289-8298, 1998. PubMed ID: 9343181. Show all entries for this paper.


Displaying record number 799

Download this epitope record as JSON.

MAb ID 41-1 (41.1, gp41-1)
HXB2 Location gp160(579-608)
DNA(7959..8048)
gp160 Epitope Map
Author Location gp41(584-609 LAV)
Epitope RILAVERYLKDQQLLGIWGCSGKLICTTAV Epitope Alignment
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG1κ)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody generation

Vaccine Details

Vaccine type protein
Vaccine component gp160

Notes

Showing 7 of 7 notes.

References

Showing 7 of 7 references.

Isolation Paper
Gosting1987 L. H. Gosting, J. McClure, E. S. Dickinson, S. M. Watanabe, K. Shriver, and L. C. Goldstein. Monoclonal antibodies to gp110 and gp41 of human immunodeficiency virus. J. Clin. Microbiol., 25:845-848, 1987. PubMed ID: 2438302. Show all entries for this paper.

Thomas1988 E. Kinney Thomas, J. N. Weber, J. McClure, P. R. Clapham, M. C. Singhal, M. K. Shriver, and R. A. Weiss. Neutralizing Monoclonal Antibodies to the AIDS Virus. AIDS, 2:25-29, 1988. PubMed ID: 2451922. Show all entries for this paper.

Mani1994 J.-C. Mani, V. Marchi, and C. Cucurou. Effect of HIV-1 Peptide Presentation on the Affinity Constants of Two Monoclonal Antibodies Determined by BIAcore Technology. Mol. Immunol., 31:439-444, 1994. Two MAbs are described; one 41-1 did not require the Cys-Cys disulfide bridge and loop formation, the other 9-11 depends on loop formation. PubMed ID: 7514268. Show all entries for this paper.

Pincus1991 S. H. Pincus, R. L. Cole, E. M. Hersh, D. Lake, Y. Masuho, P. J. Durda, and J. McClure. In Vitro Efficacy of Anti-HIV Immunotoxins Targeted by Various Antibodies to the Envelope Protein. J. Immunol., 146:4315-4324, 1991. Six MAbs, (907, 924, 110.1, 41.1, 86 and P5-3) and polyclonal pooled serum antibodies purified on gp160 were coupled to RAC to create immunotoxins. Only 41.1-RAC, an anti-gp41 MAb-immunotoxin and the polyclonal immunotoxin showed direct activity against multiple strains, and activity of an immunotoxin was found not to be directly correlated with cell surface binding. PubMed ID: 1710247. Show all entries for this paper.

Pincus1993 S. H. Pincus and J. McClure. Soluble CD4 Enhances the Efficacy of Immunotoxins Directed against gp41 of the Human Immunodeficiency Virus. Proc. Natl. Acad. Sci. U.S.A., 90:332-336, 1993. PubMed ID: 8419938. Show all entries for this paper.

Pincus1996 S. H. Pincus, K. Wehrly, R. Cole, H. Fang, G. K. Lewis, J. McClure, A. J. Conley, B. Wahren, M. R. Posner, A. L. Notkins, S. A. Tilley, A. Pinter, L. Eiden, M. Teintze, D. Dorward, and V. V. Tolstikov. In Vitro Effects of Anti-HIV Immunotoxins Directed against Multiple Epitopes on HIV Type 1 Envelope Glycoprotein 160. AIDS Res. Hum. Retroviruses, 12:1041-1051, 1996. A panel of anti-gp160 MAbs to was used to construct anti-HIV immunotoxins by coupling antibodies to ricin A chain (RAC). The ability of the immunotoxins to kill HIV-1-infected cells was tested in tissue culture. Immunotoxins that bind epitopes on the cell surface killed infected cells, although killing was not directly proportional to binding. The activity of anti-gp41 immunotoxins was markedly enhanced in the presence of sCD4. PubMed ID: 8827220. Show all entries for this paper.

Pincus1998 S. H. Pincus, R. L. Cole, R. Watson-McKown, A. Pinter, W. Honnen, B. Cole, and K. S. Wise. Immunologic Cross-Reaction between HIV Type 1 p17 and Mycoplasma hyorhinis Variable Lipoprotein. AIDS Res. Hum. Retroviruses, 14:419-425, 1998. PubMed ID: 9546801. Show all entries for this paper.


Displaying record number 748

Download this epitope record as JSON.

MAb ID 86 (No. 86)
HXB2 Location gp160(579-613)
DNA(7959..8063)
gp160 Epitope Map
Author Location gp41(586-620 IIIB)
Research Contact Evan Hersh and Yoh-Ichi Matsumoto
Epitope RILAVERYLKDQQLLGIWGCSGKLICTTAVPWNAS Epitope Alignment
Ab Type  
Neutralizing  
Species (Isotype) human(IgG1κ)
Patient  
Immunogen HIV-1 infection
Keywords antibody binding site, antibody generation, antibody sequence, complement, enhancing activity, immunotoxin, review, variant cross-reactivity

Notes

Showing 10 of 10 notes.

References

Showing 9 of 9 references.

Isolation Paper
Sugano1988 T. Sugano, Y. Masuho, Y.-I. Matsumoto, D. Lake, C. Gschwind, E. A. Petersen, and E. M. Hersh. Human monoclonal antibody against glycoproteins of human immunodeficiency virus. Biochem. Biophys. Res. Commun., 155:1105-1112, 1988. PubMed ID: 2845963. Show all entries for this paper.

Robinson1990a W. E. Robinson, Jr., T. Kawamura, M. K. Gorny, D. Lake, J.-Y. Xu, Y. Matsumoto, T. Sugano, Y. Masuho, W. M. Mitchell, E. Hersh, and S. Zolla-Pazner. Human Monoclonal Antibodies to the Human Immunodeficiency Virus Type 1 (HIV-1) Transmembrane Glycoprotein gp41 Enhance HIV-1 Infection In Vitro. Proc. Natl. Acad. Sci. U.S.A., 87:3185-3189, 1990. Three gp41 MAbs out of 16 Env and Gag MAbs tested enhanced HIV-1 IIIB infection of MT-2 cells. The enhancing antibodies were competitive with the immunodominant epitopes of gp41 recognized by sera from HIV-1 infected subjects. PubMed ID: 2326277. Show all entries for this paper.

Robinson1990b W. E. Robinson, Jr., T. Kawamura, D. Lake, Y. Masuho, W. M. Mitchell, and E. M. Hersh. Antibodies to the Primary Immunodominant Domain of Human Immunodeficiency Virus Type 1 (HIV-1) Glycoprotein gp41 Enhance HIV-1 Infection In Vitro. J. Virol., 64:5301-5305, 1990. PubMed ID: 1698995. Show all entries for this paper.

Pincus1991 S. H. Pincus, R. L. Cole, E. M. Hersh, D. Lake, Y. Masuho, P. J. Durda, and J. McClure. In Vitro Efficacy of Anti-HIV Immunotoxins Targeted by Various Antibodies to the Envelope Protein. J. Immunol., 146:4315-4324, 1991. Six MAbs, (907, 924, 110.1, 41.1, 86 and P5-3) and polyclonal pooled serum antibodies purified on gp160 were coupled to RAC to create immunotoxins. Only 41.1-RAC, an anti-gp41 MAb-immunotoxin and the polyclonal immunotoxin showed direct activity against multiple strains, and activity of an immunotoxin was found not to be directly correlated with cell surface binding. PubMed ID: 1710247. Show all entries for this paper.

Moran1993 M. J. Moran, J. S. Andris, Y.-I. Matsumato, J. D. Capra, and E. M. Hersh. Variable Region Genes of Anti-HIV Human Monoclonal Antibodies: Non-Restricted Use of the V Gene Repertoire and Extensive Somatic Mutation. Mol. Immunol., 30:1543-1551, 1993. Sequenced variable regions from four human anti-HIV-1 MAbs: anti-gp120 13, S1-1 and HBW4; and anti-gp41 No.86. Extensive somatic mutation was observed and under-representation of V$_H$ III usage. PubMed ID: 8232339. Show all entries for this paper.

Wisnewski1996 A. Wisnewski, L. Cavacini, and M. Posner. Human antibody variable region gene usage in HIV-1 infection. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol., 11:31-38, 1996. PubMed ID: 8528730. Show all entries for this paper.

Mitchell1998 W. M. Mitchell, L. Ding, and J. Gabriel. Inactivation of a Common Epitope Responsible for the Induction of Antibody-Dependent Enhancement of HIV. AIDS, 12:147-156, 1998. PubMed ID: 9468363. Show all entries for this paper.

Gorny2003 Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162. Show all entries for this paper.

Gorny2009 Miroslaw K. Gorny, Xiao-Hong Wang, Constance Williams, Barbara Volsky, Kathy Revesz, Bradley Witover, Sherri Burda, Mateusz Urbanski, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, Susan Zolla-Pazner, and Arthur Nadas. Preferential Use of the VH5-51 Gene Segment by the Human Immune Response to Code for Antibodies against the V3 Domain of HIV-1. Mol. Immunol., 46(5):917-926, Feb 2009. PubMed ID: 18952295. Show all entries for this paper.


Displaying record number 721

Download this epitope record as JSON.

MAb ID P5-3
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact Evan Hersh and Yoh-Ichi Matsumoto
Epitope
Ab Type  
Neutralizing  
Species (Isotype) human(IgG1λ)
Patient  
Immunogen HIV-1 infection
Keywords  

Notes

Showing 3 of 3 notes.

References

Showing 2 of 2 references.

Robinson1990a W. E. Robinson, Jr., T. Kawamura, M. K. Gorny, D. Lake, J.-Y. Xu, Y. Matsumoto, T. Sugano, Y. Masuho, W. M. Mitchell, E. Hersh, and S. Zolla-Pazner. Human Monoclonal Antibodies to the Human Immunodeficiency Virus Type 1 (HIV-1) Transmembrane Glycoprotein gp41 Enhance HIV-1 Infection In Vitro. Proc. Natl. Acad. Sci. U.S.A., 87:3185-3189, 1990. Three gp41 MAbs out of 16 Env and Gag MAbs tested enhanced HIV-1 IIIB infection of MT-2 cells. The enhancing antibodies were competitive with the immunodominant epitopes of gp41 recognized by sera from HIV-1 infected subjects. PubMed ID: 2326277. Show all entries for this paper.

Pincus1991 S. H. Pincus, R. L. Cole, E. M. Hersh, D. Lake, Y. Masuho, P. J. Durda, and J. McClure. In Vitro Efficacy of Anti-HIV Immunotoxins Targeted by Various Antibodies to the Envelope Protein. J. Immunol., 146:4315-4324, 1991. Six MAbs, (907, 924, 110.1, 41.1, 86 and P5-3) and polyclonal pooled serum antibodies purified on gp160 were coupled to RAC to create immunotoxins. Only 41.1-RAC, an anti-gp41 MAb-immunotoxin and the polyclonal immunotoxin showed direct activity against multiple strains, and activity of an immunotoxin was found not to be directly correlated with cell surface binding. PubMed ID: 1710247. Show all entries for this paper.


Questions or comments? Contact us at immuno@lanl.gov
 
Managed by Triad National Security, LLC for the U.S. Department of Energy’s National Nuclear Security Administration
Copyright © 2022 Triad National Security, LLC | Disclaimer/Privacy

Dept of Health & Human Services Los Alamos National Institutes of Health