Ralph Pantophlet

Summary

Affiliation: The Scripps Research Institute
Country: USA

Publications

  1. pmc Analysis of the neutralization breadth of the anti-V3 antibody F425-B4e8 and re-assessment of its epitope fine specificity by scanning mutagenesis
    Ralph Pantophlet
    The Scripps Research Institute, Department of Immunology, IMM2, La Jolla, CA 92037, USA
    Virology 364:441-53. 2007
  2. ncbi request reprint GP120: target for neutralizing HIV-1 antibodies
    Ralph Pantophlet
    Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA
    Annu Rev Immunol 24:739-69. 2006
  3. ncbi request reprint Improved design of an antigen with enhanced specificity for the broadly HIV-neutralizing antibody b12
    R Pantophlet
    Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA
    Protein Eng Des Sel 17:749-58. 2004
  4. pmc Neutralizing activity of antibodies to the V3 loop region of HIV-1 gp120 relative to their epitope fine specificity
    Ralph Pantophlet
    The Scripps Research Institute, Department of Immunology and Microbial Science, IMM2, 10550 North Torrey Pines Road La Jolla, CA 92037, USA
    Virology 381:251-60. 2008
  5. ncbi request reprint Immunofocusing: antigen engineering to promote the induction of HIV-neutralizing antibodies
    Ralph Pantophlet
    Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Trends Mol Med 9:468-73. 2003
  6. pmc O-antigen diversity among Acinetobacter baumannii strains from the Czech Republic and Northwestern Europe, as determined by lipopolysaccharide-specific monoclonal antibodies
    R Pantophlet
    Division of Medical and Biochemical Microbiology, Research Center Borstel, Borstel, Germany
    J Clin Microbiol 39:2576-80. 2001
  7. pmc Identification of Acinetobacter isolates from species belonging to the Acinetobacter calcoaceticus-Acinetobacter baumannii complex with monoclonal antibodies specific for O Antigens of their lipopolysaccharides
    Ralph Pantophlet
    Research Center Borstel, Division of Medical and Biochemical Microbiology, Borstel, Germany
    Clin Diagn Lab Immunol 9:60-5. 2002
  8. pmc Structure of antibody F425-B4e8 in complex with a V3 peptide reveals a new binding mode for HIV-1 neutralization
    Christian H Bell
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 375:969-78. 2008
  9. pmc Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design
    Ralph Pantophlet
    Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA
    J Virol 77:5889-901. 2003
  10. pmc Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors
    Amandeep K Dhillon
    The Scripps Research Institute, Department of Immunology IMM 2, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Virol 81:6548-62. 2007

Collaborators

Detail Information

Publications26

  1. pmc Analysis of the neutralization breadth of the anti-V3 antibody F425-B4e8 and re-assessment of its epitope fine specificity by scanning mutagenesis
    Ralph Pantophlet
    The Scripps Research Institute, Department of Immunology, IMM2, La Jolla, CA 92037, USA
    Virology 364:441-53. 2007
    ....
  2. ncbi request reprint GP120: target for neutralizing HIV-1 antibodies
    Ralph Pantophlet
    Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA
    Annu Rev Immunol 24:739-69. 2006
    ..These include (a) the construction of mimics of the viral envelope spike and (b) the design of antigens specifically tailored to induce broadly neutralizing antibodies...
  3. ncbi request reprint Improved design of an antigen with enhanced specificity for the broadly HIV-neutralizing antibody b12
    R Pantophlet
    Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA
    Protein Eng Des Sel 17:749-58. 2004
    ..These hyperglycosylated variants expand our panel of glycoengineered gp120s that are currently being evaluated for their ability to elicit broadly neutralizing antibodies...
  4. pmc Neutralizing activity of antibodies to the V3 loop region of HIV-1 gp120 relative to their epitope fine specificity
    Ralph Pantophlet
    The Scripps Research Institute, Department of Immunology and Microbial Science, IMM2, 10550 North Torrey Pines Road La Jolla, CA 92037, USA
    Virology 381:251-60. 2008
    ..Based on the data we propose an angle of interaction with V3 that is less stringent on access for antibodies with cross-neutralizing activity compared to antibodies that neutralize relatively fewer viruses...
  5. ncbi request reprint Immunofocusing: antigen engineering to promote the induction of HIV-neutralizing antibodies
    Ralph Pantophlet
    Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Trends Mol Med 9:468-73. 2003
    ..This template-based approach to immunogen design shows promise as a means to engineer innovative AIDS vaccine candidates...
  6. pmc O-antigen diversity among Acinetobacter baumannii strains from the Czech Republic and Northwestern Europe, as determined by lipopolysaccharide-specific monoclonal antibodies
    R Pantophlet
    Division of Medical and Biochemical Microbiology, Research Center Borstel, Borstel, Germany
    J Clin Microbiol 39:2576-80. 2001
    ..baumannii serotypes in the clinical environment. It is also shown that O-antigen-specific MAbs are useful for the follow-up of strains causing outbreaks in hospitals...
  7. pmc Identification of Acinetobacter isolates from species belonging to the Acinetobacter calcoaceticus-Acinetobacter baumannii complex with monoclonal antibodies specific for O Antigens of their lipopolysaccharides
    Ralph Pantophlet
    Research Center Borstel, Division of Medical and Biochemical Microbiology, Borstel, Germany
    Clin Diagn Lab Immunol 9:60-5. 2002
    ..This study contributes to the completion of a serotype-based identification scheme for Acinetobacter species, in particular, those which are presently of the most clinical importance...
  8. pmc Structure of antibody F425-B4e8 in complex with a V3 peptide reveals a new binding mode for HIV-1 neutralization
    Christian H Bell
    Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 375:969-78. 2008
    ..The structure helps explain how B4e8 can tolerate a certain degree of sequence variation within V3 and, hence, is able to neutralize an appreciable number of different HIV-1 isolates...
  9. pmc Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design
    Ralph Pantophlet
    Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA
    J Virol 77:5889-901. 2003
    ..The hyperglycosylated mutant and its analogues described here are novel antigens that may provide a new approach to eliciting antibodies with b12-like neutralizing properties...
  10. pmc Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors
    Amandeep K Dhillon
    The Scripps Research Institute, Department of Immunology IMM 2, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Virol 81:6548-62. 2007
    ..The most likely epitope recognized by the monomeric gp120 binding neutralizing fraction is the CD4 binding site, although other epitopes, such as the glycan shield, cannot be excluded...
  11. pmc Comparing antigenicity and immunogenicity of engineered gp120
    Suganya Selvarajah
    The Scripps Research Institute, Department of Immunology, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Virol 79:12148-63. 2005
    ..More precise focusing to a neutralizing epitope will likely require several iterations comparing antigenicity and immunogenicity of engineered proteins...
  12. pmc A glycoconjugate antigen based on the recognition motif of a broadly neutralizing human immunodeficiency virus antibody, 2G12, is immunogenic but elicits antibodies unable to bind to the self glycans of gp120
    Rena D Astronomo
    The Scripps Research Institute, Department of Immunology and Microbial Science, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Virol 82:6359-68. 2008
    ....
  13. pmc Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus type 1 gp120
    Ralph Pantophlet
    Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA
    J Virol 77:642-58. 2003
    ..These reengineered gp120s are prospective immunogens that may prove capable of eliciting broadly neutralizing antibodies...
  14. pmc Defining criteria for oligomannose immunogens for HIV using icosahedral virus capsid scaffolds
    Rena D Astronomo
    Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA
    Chem Biol 17:357-70. 2010
    ..The results presented reveal important design considerations for a carbohydrate-based vaccine component for HIV...
  15. pmc Structure of a high-affinity "mimotope" peptide bound to HIV-1-neutralizing antibody b12 explains its inability to elicit gp120 cross-reactive antibodies
    Erica Ollmann Saphire
    Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    J Mol Biol 369:696-709. 2007
    ....
  16. pmc 2G12-expressing B cell lines may aid in HIV carbohydrate vaccine design strategies
    Katie J Doores
    Department of Immunology and Microbial Science, Scripps Research Institute, La Jolla, California, USA
    J Virol 87:2234-41. 2013
    ..Additionally, a molecule capable of activating 2G12 gl cells might also be required. The results highlight broadly neutralizing antibody-expressing mouse B cells as potentially useful tools for carbohydrate immunogen screening...
  17. ncbi request reprint Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design
    E O Saphire
    Department of Molecular Biology, Department of Immunology, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
    Science 293:1155-9. 2001
    ..The structure, together with mutagenesis studies, provides a rationale for the extensive cross-reactivity of b12 and a valuable framework for the design of HIV-1 vaccines capable of eliciting b12-like activity...
  18. pmc The human immunodeficiency virus type 1 envelope spike of primary viruses can suppress antibody access to variable regions
    Ralph Pantophlet
    Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California 92037, USA
    J Virol 83:1649-59. 2009
    ....
  19. pmc Generation and serological characterization of murine monoclonal antibodies against O antigens from Acinetobacter reference strains
    R Pantophlet
    Research Center Borstel, Division of Medical and Biochemical Microbiology, Borstel, Germany
    Clin Diagn Lab Immunol 8:825-7. 2001
    ..The antibodies aid in the further completion of an O-serotyping scheme for Acinetobacter and, due to their high specificity, are especially useful to all working with these strains...
  20. pmc Susceptibility of recently transmitted subtype B human immunodeficiency virus type 1 variants to broadly neutralizing antibodies
    Esther D Quakkelaar
    Department of Clinical Viro Immunology, Sanquin Research and Landsteiner Laboratory of the Academic Medical Center, University of Amsterdam, Plesmanlaan 125, 1066 CX Amsterdam, The Netherlands
    J Virol 81:8533-42. 2007
    ....
  21. pmc Increased sensitivity to CD4 binding site-directed neutralization following in vitro propagation on primary lymphocytes of a neutralization-resistant human immunodeficiency virus IIIB strain isolated from an accidentally infected laboratory worker
    Tim Beaumont
    Sanquin Research, Plesmanlaan 125, 1066 CX Amsterdam, The Netherlands
    J Virol 78:5651-7. 2004
    ....
  22. ncbi request reprint Mode of action for linear peptide inhibitors of HIV-1 gp120 interactions
    Alyssa C Biorn
    Department of Biochemistry, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102, USA
    Biochemistry 43:1928-38. 2004
    ..More importantly, these results indicate that 12p1 binds to a unique site that may prove to be a prototypic target for novel CD4-gp120 inhibitors...
  23. ncbi request reprint Crystal structure of the broadly cross-reactive HIV-1-neutralizing Fab X5 and fine mapping of its epitope
    Ramalakshmi Darbha
    Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, Maryland 21702, USA
    Biochemistry 43:1410-7. 2004
    ..The X5 structure and fine mapping of its epitope may assist in the elucidation of the mechanisms of viral entry and neutralization, and the development of HIV-1 inhibitors and vaccines...
  24. ncbi request reprint The carbohydrate epitope of the neutralizing anti-HIV-1 antibody 2G12
    Christopher N Scanlan
    The Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom
    Adv Exp Med Biol 535:205-18. 2003
  25. pmc The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1-->2 mannose residues on the outer face of gp120
    Christopher N Scanlan
    The Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom
    J Virol 76:7306-21. 2002
    ....
  26. pmc A dominant role for CD8+-T-lymphocyte selection in simian immunodeficiency virus sequence variation
    DAVID H O'CONNOR
    Wisconsin Primate Research Center, Department of Pathology, Laboratoty of Medicine, University of Wisconsin, 1300 University Ave, Madison, WI 53706, USA
    J Virol 78:14012-22. 2004
    ..We also found that >60% of viral variation outside of the viral envelope occurs within recognized CD8-TL epitopes. Therefore, we conclude that CD8-TL selection is the dominant cause of SIV diversification outside of the envelope...