Faculty, Graduate Program
The Ragon Institute of MGH, MIT and Harvard
IAVI Neutralizing Antibody Center, The Scripps Research Institute
Antibodies and Infectious Disease
The perception of man as the easy victor over microbes has changed dramatically in the last two decades. Vaccination has offered protection against a number of viral pathogens, but it is increasingly recognized that the strategies used in the past will not be successful against all viruses. We are focused on developing rational vaccine strategies, particularly against HIV and particularly using an approach termed “Reverse Vaccinology 2.0”. In this approach, broadly neutralizing antibodies isolated from natural HIV infection are investigated in interaction with their sole viral target, the HIV Envelope, and the data used to guide immunogen design and immunization strategies. Immunogens are then evaluated in detail in animal models and the results used to iteratively improve immunogens as we move toward an HIV vaccine suitable to protect humans.
Ph.D. (Physical Biochemistry), Lund University 1978
B.A. (Chemistry), University of Oxford 1974
2015-2017 Chairman, Immunology and Microbial Science (IMS), The Scripps Research Institute
1991-2017 Professor, Immunology and Microbial Science (IMS), The Scripps Research Institute
2015-2015 Distinguished Lecturer, The American Association of Immunologists
-2012 Professor (Joint Appointment), Molecular Biology, The Scripps Research Institute
1990-1991 Personal Chair, The University of Sheffield
1989-1991 Visiting Member, Research Institute of Scripps Clinic
1985-1991 Jenner Fellow, Lister Institute of Preventive Medicine
1987-1990 Senior Lecturer in Biochemistry, The University of Sheffield
1981-1987 Lecturer in Biochemistry, The University of Sheffield
1980-1981 Junior Research Fellow, Wolfson College, University of Oxford
1979-1981 Medical Research Council Training Fellowship, University of Oxford
Sok, D., Pauthner, M., Briney, B., Lee, J. H., Saye-Francisco, K. L., Hsueh, J., Ramos, A., Le, K. M., Jones, M., Jardine, J. G., Bastidas, R., Sarkar, A., et al. A prominent site of antibody vulnerability on HIV envelope incorporates a motif associated with CCR5 binding and its camouflaging glycans. (2016). Immunity, 45(1), 31-45. PMCID: PMC4990068.
van Gils, M. J., van den Kerkhof, T. L., Ozorowski, G., Cottrell, C. A., Sok, D., Pauthner, M., Pallesen, J., de Val, N., Yasmeen, A., de Taeye, S. W., Schorcht, A., Gumbs, S., et al. An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability. (2016). Nature Microbiology, 2.
Larrick, J. W., Alfenito, M. R., Scott, J. K., Parren, P. W. H. I., Burton, D. R., Bradbury, A. R. M., Lemere, C. A., Messer, A., Huston, J. S., Carter, P. J., Veldman, T., Chester, K. A., et al. Antibody Engineering & Therapeutics 2016: The Antibody Society's annual meeting, December 11-15, 2016, San Diego, CA. (2016). MAbs, 8(8), 1425-1434.
Liu, J., Ghneim, K., Sok, D., Bosche, W. J., Li, Y., Chipriano, E., Berkemeier, B., Oswald, K., Borducchi, E., Cabral, C., Peter, L., Brinkman, A., et al. Antibody-mediated protection against SHIV challenge includes systemic clearance of distal virus. (2016). Science, 353(6303), 1045-1049.
Burton, D. R. & Hangartner, L. Broadly neutralizing antibodies to HIV and their role in vaccine design. (2016). Annual Review of Immunology, 34, 635.
Briney, B., Le, K., Zhu, J. & Burton, D. R. Clonify: unseeded antibody lineage assignment from next-generation sequencing data. (2016). Scientific Reports, 6. PMCID: PMC4840318.
von Bredow, B., Arias, J. F., Heyer, L. N., Moldt, B., Le, K., Robinson, J. E., Zolla-Pazner, S., Burton, D. R. & Evans, D. T. Comparison of antibody-dependent cell-mediated cytotoxicity and virus neutralization by HIV-1 Env-specific monoclonal antibodies. (2016). Journal of Virology, 90(13), 6127-6139. PMCID: PMC4907221.
Behrens, A. J., Vasiljevic, S., Pritchard, L. K., Harvey, D. J., Andev, R. S., Krumm, S. A., Struwe, W. B., Cupo, A., Kumar, A., Zitzmann, N., Seabright, G. E., Kramer, H. B., et al. Composition and antigenic effects of individual glycan sites of a trimeric HIV-1 envelope glycoprotein. (2016). Cell Reports, 14(11), 2695-2706. PMCID: PMC4805854.
Havenar-Daughton, C., Carnathan, D. G., Torrents de la Peña, A., Pauthner, M., Briney, B., Reiss, S. M., Wood, J. S., Kaushik, K., van Gils, M. J., Rosales, S. L., van der Woude, P., Locci, M., et al. Direct probing of germinal center responses reveals immunological features and bottlenecks for neutralizing antibody responses to HIV Env trimer. (2016). Cell Reports, 17(9), 2195-2209. PMCID: PMC5142765.
MacLeod, D. T., Choi, N. M., Briney, B., Garces, F., Ver, L. S., Landais, E., Murrell, B., Wrin, T., Kilembe, W., Liang, C. H., Ramos, A., Bian, C. B., et al. Early antibody lineage diversification and independent limb maturation lead to broad HIV-1 neutralization targeting the Env high-mannose patch. (2016). Immunity, 44(5), 1215-1226. PMCID: PMC5003182.