Search Antibody Database

Found 1 matching record:

Displaying record number 805

Download this epitope record as JSON.

MAb ID	3D6 (IAM 41-3D6, CB HIV-1)
HXB2 Location	gp160(599-613) DNA(8019..8063)	gp160 Epitope Map
Author Location	gp41(604-617 BH10)
Research Contact	H. Katinger, Inst. Appl. Microbiol., Vienna, Austria and Viral Testing Systems, Houston, TX
Epitope	SGKLICTTAVPWNAS	Epitope Alignment
Ab Type	gp41 cluster I, immunodominant region
Neutralizing
Species (Isotype)	human(IgG1κ)
Patient
Immunogen	HIV-1 infection
Keywords	antibody binding site, antibody generation, antibody interactions, antibody sequence, assay or method development, binding affinity, dendritic cells, genital and mucosal immunity, kinetics, review, structure

Notes

Showing 17 of 17 notes.

• CB HIV1: Fusions of cloned CB-F7 with PBL obtained from individuals having anti-HIV antibody led to four independent hybrid cell lines producing specific human mAbs to HIV. Antibodies were detected by ELISA and verified by Western blot. Three hybrids produced antibodies against the p25 (core protein) and one (CB HIV1) against the gp41 (transmembrane protein) antigens. One of the anti-p25 antibodies was of the IgM class, the other three were of the IgGl subclass as estimated by ELISA. Grunow1988 (antibody generation)
• 3D6: A human hybridoma line described as CB HIV1 by Grunow1988 was purified to produce 3D6. Jungbauer1989 (assay or method development)
• 3D6: The capacity of 3D6 to block completely the activity of the anti-HIV peptide T20 was investigated. T20 inhibited the fusion or syncytia formation between co-cultured CHO-WT cells expressing HIV-1 HXB2 envelope glycoprotein on their surface and HeLaT4 cells. 3D6 was able to block the anti-fusion effect of T20. Vincent2012 (antibody interactions)
• 3D6: The inhibitory activity of HIV-1-specific Abs against HIV-1 replication in langerhans cells (LCs) and interstitial dendritic cells (IDCs) was analyzed. Five well-known NAbs 447-52D, 4E10, b12, 2G12, 2F5 strongly inhibited HIV-1BaL and HIV-1TV1 replication in LCs and IDCs, and their inhibitory activities were stronger than those measured on PBMCs. Inhibition was more efficient by IgGs than corresponding IgAs, due to an Fc receptor-dependent mechanism, where HIV-1 inhibition occurs by binding of the Fc portion of IgGs to Fc receptors. Nonneutralizing noninhibitory Abs 5F3 and 3D6, directed against gp41, which did not exhibit any inhibitory activity in previous assays, also had no inhibitory effects in this model system. Peressin2011 (genital and mucosal immunity, dendritic cells)
• 3D6: 58 mAbs, including 3 broadly neutralizing mAbs, were isolated from memory B cells of HIV-1 infected donors using an improved EBV immortalization method combined with a broad screening strategy. 3D6 competed for binding to gp41 with 5 of the new mAbs. Corti2010 (binding affinity)
• 3D6: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:3-9*01, IGHD:3-22, D-RF:2, IGHJ:3. Non-V3 mAbs preferentially used the VH1-69 gene segment. In contrast to V3 mAbs, these non-V3 mAbs used several VH4 gene segments and the D3-9 gene segment. Similarly to the V3 mAbs, the non-V3 mAbs used the VH3 gene family in a reduced manner. Gorny2009 (antibody sequence)
• 3D6: One of 24 MAbs and Fabs in this database that bind to the highly immunogenic gp41 cluster I region (aa 579 - 604). Only one of these has any neutralizing potential, clone 3. Gorny2003 (review)
• 3D6: Anti-gp41 MAbs were tested in a cell-cell fusion system to investigate the antigenic changes in gp41 during binding and fusion. Cluster I MAbs 50-69, F240, 240-D,3D6, and 246-D recognize a nonhelical hydrophobic region, positions 598-604, that forms a disulfide loop in the six-helix bundle. Cluster II MAbs 98-6 and 126-6 recognized residues 644-663 of gp41, a portion of the second heptad repeat. These MAbs were found to behave similarly, so 50-69 and 98-6 were used as representatives. Exposure of cluster I and cluster II epitopes required CD4 expression on HIV HXB2 Env expressing HeLa target cells, but not the CXCR4 co-receptor. Binding to CD4 exposed hidden cluster I and II epitopes. The MAbs were found to bind to gp120/gp41 complexes, not to gp41 after shedding of gp120, and were localized to at fusing-cell interfaces. Kinetic and binding results indicate that these MAbs are exposed in transitional structures during the fusion process, possibly the prehairpin intermediate prior to co-receptor binding, although other intermediate structures may be involved. They do not bind once syncytia begin to show extensive cytoplasmic mixing. These MAbs failed to inhibit fusion. The NAb 2F5 has a very different behavior in this study. Finnegan2002 (antibody binding site, kinetics)
• 3D6: Cavacini et al. note that both MAbs F223 and 3D6 are anti-HIV-1 Env MAbs that have an autoimmune response and that both use uses VH3 germline genes. Cavacini1999
• 3D6: Binds to the immunodominant region of gp41 -- a strong homology between heavy variable domains of hu MAb 3D6 and MAb F20 was observed, these MAbs may define a human Ab clonotype. Cavacini1998a (antibody sequence)
• 3D6: The complete V, J and D(H) domain was sequenced -- in contrast the sequences of five neutralizing MAbs, 3D6 had very little somatic mutation, with homologies of 97-98% relative to germline genes. Kunert1998 (antibody sequence)
• 3D6: 3D6 is V H3 -- V-region heavy chain usage was examined and a bias of enhanced V H1 and V H4, and reduced V H3, was noted among HIV infected individuals. Wisnewski1996 (antibody sequence)
• 3D6: Optimum peptide for binding 3D6 Fab was CSGKLICTTAVPW. Stigler1995 (antibody binding site)
• 3D6: Called IAM 41-3D6: binding increased after pretreatment of infected cells with sCD4 -- binding domain overlaps site that is critical for gp120-gp41 association. Sattentau1995 (antibody binding site)
• 3D6: This MAb binds to HIV gp41, and to a 43 kd protein found in human T, B and monocyte cell lines, proposed molecular mimicry. Chen1994
• 3D6: Fab fragment crystal structure. He1992 (structure)
• 3D6: Sequence of cDNA encoding V-regions. Felgenhauer1990 (antibody sequence)

References

Showing 18 of 18 references.

Isolation Paper
Grunow1988 R. Grunow, S. Jahn, T. Porstmann, S. S. Kiessig, H. Steinkellner, F. Steindl, D. Mattanovich, L. Gurtler, F. Deinhardt, and H. Katinger. The High Efficiency, Human B Cell Immortalizing Heteromyeloma CB-F7. Production of Human Monoclonal Antibodies to Human Immunodeficiency Virus. J. Immunol. Methods, 106(2):257-265, 10 Feb 1988. PubMed ID: 2828478. Show all entries for this paper.

Felgenhauer1990 M. Felgenhauer, J. Kohl, and F. Ruker. Nucleotide Sequence of the cDNA Encoding the V-Regions of the H- and L-Chains of a Human Monoclonal Antibody Specific to HIV-1 gp41. Nucl. Acids Res., 18:4927, 1990. PubMed ID: 1697678. Show all entries for this paper.

He1992 X. M. He, F. Ruker, E. Casale, and D. C. Carter. Structure of a Human Monoclonal Antibody Fab Fragment against gp41 of Human Immunodeficiency Virus Type 1. Proc. Natl. Acad. Sci. U.S.A., 89:7154-7158, 1992. PubMed ID: 1496010. Show all entries for this paper.

Chen1994 Y.-H. Chen, A. Susanna, G. Bock, F. Steindl, H. Katinger, and M. P. Dierich. HIV-1 gp41 Shares a Common Immunologic Determinant with Human T, B and Monocyte Cell Lines. Immunol. Lett., 39:219-222, 1994. The MAb 3D6 binds to HIV gp41, and to a 43 kd protein found in human T, B and monocyte cell lines. The authors suggest the possibility of molecular mimicry. PubMed ID: 7518416. Show all entries for this paper.

Sattentau1995 Q. J. Sattentau, S. Zolla-Pazner, and P. Poignard. Epitope Exposure on Functional, Oligomeric HIV-1 gp41 Molecules. Virology, 206:713-717, 1995. Most gp41 epitopes are masked when associated with gp120 on the cell surface. Weak binding of anti-gp41 MAbs can be enhanced by treatment with sCD4. MAb 2F5 binds to a membrane proximal epitope which binds in the presence of gp120 without sCD4. PubMed ID: 7530400. Show all entries for this paper.

Stigler1995 R. D. Stigler, F. Ruker, D. Katinger, G. Elliott, W. Hohne, P. Henklein, J. X. Ho, K. Keeling, D. C. Carter, E. Nugel, and et al. Interaction between a Fab Fragment against gp41 of Human Immunodeficiency Virus 1 and Its Peptide Epitope: Characterization Using a Peptide Epitope Library and Molecular Modeling. Protein Eng., 8:471-479, 1995. PubMed ID: 8532669. 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.

Kunert1998 R. Kunert, F. Ruker, and H. Katinger. Molecular Characterization of Five Neutralizing Anti-HIV Type 1 Antibodies: Identification of Nonconventional D Segments in the Human Monoclonal Antibodies 2G12 and 2F5. AIDS Res. Hum. Retroviruses, 14:1115-1128, 1998. Study identifies five human MAbs which were able to neutralize primary isolates of different clades in vitro and reports the nucleotide and amino acid sequences of the heavy and light chain V segments of the antibodies. PubMed ID: 9737583. Show all entries for this paper.

Cavacini1998 L. A. Cavacini, M. H. Samore, J. Gambertoglio, B. Jackson, M. Duval, A. Wisnewski, S. Hammer, C. Koziel, C. Trapnell, and M. R. Posner. Phase I Study of a Human Monoclonal Antibody Directed against the CD4-Binding Site of HIV Type 1 Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:545-550, 1998. In an immunotherapeutic study, administration of a single dose of F105 was non-toxic and the Ab persisted, yet no benefit was observed in 4 individuals. The authors suggest it may be more helpful in other settings, for example, patients with no pre-existing anti-CD4 BS Abs, or in combination with other MAbs. PubMed ID: 9591708. Show all entries for this paper.

Cavacini1998a L. A. Cavacini, C. L. Emes, A. V. Wisnewski, J. Power, G. Lewis, D. Montefiori, and M. R. Posner. Functional and molecular characterization of human monoclonal antibody. AIDS Res. Hum. Retroviruses, 14:1271-80, 1998. PubMed ID: 9764911. Show all entries for this paper.

Cavacini1999 L. A. Cavacini, A. Wisnewski, J. E. Peterson, D. Montefiori, C. Emes, M. Duval, G. Kingsbury, A. Wang, D. Scadden, and M. R. Posner. A Human Anti-HIV Autoantibody Enhances EBV Transformation and HIV infection. Clin. Immunol., 93:263-273, 1999. PubMed ID: 10600338. Show all entries for this paper.

Finnegan2002 Catherine M. Finnegan, Werner Berg, George K. Lewis, and Anthony L. DeVico. Antigenic Properties of the Human Immunodeficiency Virus Transmembrane Glycoprotein during Cell-Cell Fusion. J. Virol., 76(23):12123-12134, Dec 2002. PubMed ID: 12414953. 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.

Corti2010 Davide Corti, Johannes P. M. Langedijk, Andreas Hinz, Michael S. Seaman, Fabrizia Vanzetta, Blanca M. Fernandez-Rodriguez, Chiara Silacci, Debora Pinna, David Jarrossay, Sunita Balla-Jhagjhoorsingh, Betty Willems, Maria J. Zekveld, Hanna Dreja, Eithne O'Sullivan, Corinna Pade, Chloe Orkin, Simon A. Jeffs, David C. Montefiori, David Davis, Winfried Weissenhorn, Áine McKnight, Jonathan L. Heeney, Federica Sallusto, Quentin J. Sattentau, Robin A. Weiss, and Antonio Lanzavecchia. Analysis of Memory B Cell Responses and Isolation of Novel Monoclonal Antibodies with Neutralizing Breadth from HIV-1-Infected Individuals. PLoS One, 5(1):e8805, 2010. PubMed ID: 20098712. Show all entries for this paper.

Peressin2011 M. Peressin, V. Holl, S. Schmidt, T. Decoville, D. Mirisky, A. Lederle, M. Delaporte, K. Xu, A. M. Aubertin, and C. Moog. HIV-1 Replication in Langerhans and Interstitial Dendritic Cells Is Inhibited by Neutralizing and Fc-Mediated Inhibitory Antibodies. J. Virol., 85(2):1077-1085, Jan 2011. PubMed ID: 21084491. Show all entries for this paper.

Vincent2012 Nadine Vincent and Etienne Malvoisin. Ability of Antibodies Specific to the HIV-1 Envelope Glycoprotein to Block the Fusion Inhibitor T20 in a Cell-Cell Fusion Assay. Immunobiology, 217(10):943-950, Oct 2012. PubMed ID: 22387075. Show all entries for this paper.

Jungbauer1989 Alois Jungbauer, Chrisa Tauer, Elisabeth Wenisch, Franz Steindl, Martin Purtscher, Manfred Reiter, Florian Unterluggauer, Andrea Buchacher, Karola Uhl, and Hermann Katinger. Pilot Scale Production of a Human Monoclonal Antibody against Human Immunodeficiency Virus HIV-1. J. Biochem. Biophys. Methods, 19(2-3):223-240, Aug-Sep 1989. PubMed ID: 2584609. Show all entries for this paper.