Positions and Honors

• 1991 - 1995 Predoctoral Fellow, Molecular Biology/Immunology
  Thesis: “The Antibody Response to HIV-1 as Probed by Phage Displayed Antibody Libraries”
  Performed at: The Scripps Research Institute, La Jolla, CA
  Awarded at: University of Sheffield, UK.
  Advisor: Prof. Dennis R. Burton.
• 1995 - 1999 Post-doctoral Fellow Aaron Diamond AIDS Research Center,
  The Rockefeller University, New York, NY.
  Laboratory of John P. Moore.
• 1999 - 2000 Research Scientist, Aaron Diamond AIDS Research Center,
  The Rockefeller University, New York, NY.
• 2000 - 2001 Instructor, Weill Medical College, Cornell University, New York, NY
• 2001 - 2004 Staff Scientist The Scripps Research Institute, La Jolla, CA
• 2002 - 2004 Scientific Coordinator/Project Manager, Neutralizing Antibody Consortium, International AIDS Vaccine Initiative, NY
• 2004 - present  Assistant Member, Torrey Pines Institute for Molecular Studies
  Laboratory of Infectious Diseases

The HIV epidemic rages on with over 40 million people infected worldwide. A vaccine represents a cheap and practical option for controlling the global epidemic and as such is one of the most compelling challenges in biomedical research today.

In the last 25 years since the discovery of HIV, inducing so-called "neutralizing antibodies", able to block HIV infection has been the single biggest challenge in vaccine development. Traditional approaches that have worked for viruses like smallpox, polio and measles have so far failed for HIV. It is sobering to consider that only 4 or 5 effective neutralizing antibodies (from among many hundreds) have been identified to date. It is becoming increasingly clear that the vast majority of antibodies generated during HIV infection are only able to recognize defective or "junk" forms of the HIV Envelope (Env) coat proteins. To make progress, we may need to understand why so many of these "junk" antibodies are induced by contemporary HIV vaccine candidates.

HIV Virus-Like Particles (VLPs) as a vaccine platform and for investigating the mechanism and specificity of antibody neutralization

We are using virus-like particles (termed "VLPs") - also known as pseudovirions - as a central commodity to investigate a variety of questions related to Env conformation, function, immunogenicity and neutralization. VLPs are synthetic viruses that look exactly like the real HIV virus, except that they are modified and treated to make them safe and non-infectious. Our approaches using VLPs stem from the fact that these particles are a facile way of analyzing the functional form of Env: gp120/gp41 trimers (Fig. 1).

Figure 1: Electron micrograph of a HIV-VLP particle. The surface of the particle is stippled with Envelope proteins that resemble the predicted trimeric structure (photograph, courtesy K. Roux; inset, courtesy P.Kwong).

Over the last few years, we have developed a number of protocols involving VLPs (outlined in Fig. 2). VLPs can be used to immunize animals, with a view to inducing neutralizing antibodies that are crucially important for a successful HIV vaccine. VLPs can also be used to investigate antibody neutralization, and modified assays can determine neutralization mechanism. In addition, VLPs can be used in virus capture and native PAGE assays, useful in mapping anti-Env antibodies and for evaluating the conformation of Env on particle surfaces. The common use of VLPs in these methods facilitates the direct cross-referencing of data, empowering each assay.

Figure 2: Multiple uses of VLPs. VLPs with or without modified forms of Env on their surfaces can be used to try to induce neutralizing antibodies in animals, to analyze neutralization and its mechanism, to map binding and neutralizing antibodies to HIV-1 and to investigate the conformation of Env on particle surfaces.

i) VLPs as a platform for an HIV vaccine

A VLP approach to a HIV vaccine is exciting for several reasons. First, from the most elementary perspective, making a vaccine that looks like the real virus makes perfect sense if one wishes to protect against a live HIV virus challenge. Second, it is a relatively unexplored vaccine approach that can be easily adapted or modified by simple molecular biology techniques, meaning that many exciting possibilities remain untested. Functional trimers (Fig.1) are exclusively recognized by neutralizing antibodies and represent ideal target molecules for a vaccine. However, unmodified particles (wild-type, WT-VLPs) have a tendency to shed gp120 (Fig. 3A), leaving behind nonfunctional Env that may have a negative effect on the ability of the particles to induce neutralizing antibodies. One approach to eliminate this problem is to ablate the cleavage site in the gp160 Env precursor (UNC-VLPs, Fig. 3B) or to introduce a disulfide bond to link gp120 and gp41 subunits in fully cleaved trimers (SOS-VLPs, Fig. 3C). These and other approaches are currently being tested.

Figure 3: Shown on the cover of Virology, September 30, 2007, a schematic depiction of VLP candidate vaccines. A) unmodified wild type (WT-VLPs) bearing functional gp120/gp41 trimers. Gp120 can sometimes be shed from these trimers, leaving behind gp41 stumps. B) UNC-VLPs in which the gp120-gp41 cleavage site is ablated to eliminate gp120 shedding, but which renders trimers non-functional. C) SOS-VLPs in which a disulfide bond links gp120-gp41 to prevent shedding, while retaining functional properties similar to WT-VLPs

ii) Studying Env conformation and mapping the specificity and mechanism of neutralization.

Some VLPs are capable of a single round of infection of susceptible cells. Infection is simple to assay using a luciferase readout. A powerful aspect of VLPs is that since they are expressed by plasmid transfection, the researcher has the ability to express viruses bearing any Envelope of choice (e.g. from North America or Africa, from a drug resistant mutant or field isolate, from HIV or its simian counterpart, SIV). Because Env is expressed in a functionally relevant form, VLPs provide a way to examine Env structure-function relationships, and to investigate Env recognition by neutralizing and non-neutralizing antibodies. In particular, we are using VLPs to better understand why some HIV+ patient plasmas broadly neutralize HIV-1, while others do not. We have developed a series of assays (Fig. 2) including:

Modified neutralization assays. We have developed several new formats to help identify the stage at which an antibody can neutralize virus, i.e. pre-attachment, post-CD4 binding, post-CD4/CCR5 binding. For example, neutralization post-CD4/CCR5 binding can be assayed by allowing SOS-VLPs (Fig. 3) to attach to target cells, engaging CD4 and CCR5. The SOS bond prevents infection from proceeding until a low concentration of reducing agent is added to disrupt the disulfide bond between gp120 and gp41. Thus, neutralizing antibody can be titrated against the cells with receptor-bound virus and then reducing agent added to allow any residual virus to infect (the non-neutralized fraction).

Virus capture assays. Here, an antibody, usually monoclonal, is used to capture virus on an ELISA plate, by a protocol very similar to traditional ELISA. Susceptible cells are then added, to evaluate how efficiently the virus was captured. Surprisingly, several groups have now confirmed that many non-neutralizing "junk" antibodies are able to specifically capture virus, suggesting non-functional Env as well as functional trimers are present on virus surfaces. We have adapted virus capture for mapping antibody specificities. This works by titrating the antibody sample against the VLPs and looking for a decrease in virus capture by any of a panel of index monoclonal antibody prototypes directed to common Env epitopes.

Blue native PAGE (BN-PAGE). Env trimers derived from particles can be visualized in native gels. We have shown that only neutralizing monoclonal antibodies and sera are able to bind to these trimers, retarding their migration in native conditions. We are now adapting this method to try to map the important contact residues of neutralizing antibodies in neutralizing patient plasmas and vaccine sera. We are also using this method to investigate the conformation of various modified forms of Env expressed on VLP surfaces.

Together, these assays can be used to profile neutralizing antibodies in complex polyclonal samples and help define the properties of various HIV Envs and mutants, with an overarching view to advancing AIDS vaccine research.

Binley Research Group

Publications

1. Binley, J.M., Ngo-Abdalla, S., Moore, P., Bobardt, M., Chatterji, U., Gallay, P., Burton, D.R., Wilson, I.A., Elder, J.H., and de Parseval, A. Inhibition of HIV Env binding to cellular receptors by monoclonal antibody 2G12 as probed by Fc-tagged gp 120. Retrovirology, 3(1):39, 2006.
2. Boggiano, C., Jiang, S., Lu, H., Zhao, Q., Liu, S., Binley, J., Blondelle, S. Identificaiton of D-amino acid decapeptide HIV-1 entry inhibitors. Biochem. and Biophysical Res. Comm. 374:909-915, 2006.
3. Crooks, E.T., Moore, P.L., Richman, D., Robinson, J., Crooks, J.A., Franti, M., Schulke, N., Binley, J.M. Characterizing anti-HIV monoclonal antibodies and immune sera by defining the mechanism of neutralization. Hum. Antibodies 14:101-113, 2006.
4. Derby, N.R., Kraft, Z., Kan, E., Barnett, S.W., Srivastava, I.K., Binley, J. and Stamatatos, L. Comparative analysis of antibody responses elicited in macaques immunized with HIV-1 SF162-derived gp140 envelope immunogens with those elicited during homologous SHIVSF162 and heterologous HIV-1 infection. J.Virol. 80:8745-8762, 2006.
5. Metzner, K.J., Binley, J.M., Gettie, A., Marx, P., Nixon, D.F., Connor, R.I. Treatment of macaques infected with live, attenuated SIV with tenofovir prevents replication of pathogenic SIV with reduced drug sensitivity. Retrovirology 3:97, 2006.
6. Moore, P.L., Crooks, E.T., Porter, L., Shu, P., Cayanan, C.S., Corcoran, P., Zwick, M.B., Franti, M., Morris, L., Roux, K.H., Burton, D.R., Binley, J.M. Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1. J. Virol. 80:2515-2528, 2006.

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7. Abrahamyan, L.G., Mkrtchyan, S.R., Binley, J., Lu, M., Melikyan, G.B., Cohen, F.S. The cytoplasmic tail slows the folding of human immunodeficiency virus type 1 env from a late prebundle configuration into the six-helix bundle. J. Virol. 79:106-115, 2005.
8. Cardoso, R.M., Zwick, M.B., Stanfield, R.L., Kunert, R., Binley, J.M., Katinger, H., Burton, D.R., Wilson, I.A. Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity 22:163-173, 2005.
9. Crooks, E.T., Moore, P.L., Richman, D., Robinson, J., Crooks, J.A., Franti, M., Schulke, N., and Binley, J.M. Characterizing anti-HIV monoclonal antibodies and immune sera by defining the mechanism of neutralization. Human Antibodies 14(3-4):101-113, 2005.
10. Hosie, M.J., Klein, D., Binley, J.M., Dunsford, T.H., Jarrett, O., Neil, J.C., Knapp, E., Giannecchini, S., Matteucci, D., Bendinelli, M., Hoxie, J.A., Willett, B.J. Vaccination with an inactivated virulent feline immunodeficiency virus engineered to express high levels of Env. J. Virol. 79:1954-1957, 2005.
11. Metzner, K.J., Moretto, W.J., Donahoe, S.M., Jin, X., Gettie, A., Montefiori, D.C., Marx, P.A., Binley, J.M., Nixon, D.F., Connor, R.I. Evaluation of CD8+ T-cell and antibody responses following transient increased viraemia in rhesus macaques infected with live, attenuated simian immunodeficiency virus. J. Gen. Virol. 86:3375-84, 2005.

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12. Binley, J.M., Wrin, T., Korber, B., Zwick, M.B., Wang, M., Chappey, C., Stiegler, G., Kunert, R., Zolla-Pazner, S., Katinger, H., Petropoulos, C.J., Burton, D.R. Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies. J. Virol. 78:13232-13252, 2004.

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13. Binley, J.M., Cayanan, C.S., Wiley, C., Schülke, N., Olson, W.C., Burton, D.R. Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions. J. Virol. 77:5678-5684, 2003.
14. Labrijn, A.F., Poignard, P., Raja, A., Zwick, M.B., Delgado, K., Franti, M., Binley, J., Vivona, V., Grundner, C., Huang, C.C., Venturi, M., Petropoulos, C.J., Wrin, T., Dimitrov, D.S., Robinson, J., Kwong, P.D., Wyatt, R.T., Sodroski, J., Burton, D.R. Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1. J. Virol 77: 10557-10565, 2003.

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15. Binley, J.M., Sanders, R.W., Master, A., Cayanan, C.S., Wiley, C.L., Schiffner, L., Travis, B., Kuhmann, S., Burton, D.R., Hu, S.L., Olson, W.C., Moore, J.P. Enhancing the proteolytic maturation of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 76:2606-2616, 2002.
16. Jin, X., Ramanathan Jr., M., Barsoum, S., Deschenes, G.R., Ba, L., Binley, J., Schiller, D., Bauer, D.E., Chen, D.C., Hurley, A., Gebuhrer, L., El Habib, R., Caudrelier, P., Klein, M., Zhang, L., Ho, D.D., Markowitz, M. Safety and immunogenicity of ALVAC vCP1452 and recombinant gp160 in newly human immunodeficiency virus type 1-infected patients treated with prolonged highly active antiretroviral therapy. J. Virol. 76: 2206-2216, 2002.
17. Moulard, M., Phogat, S.K., Shu, Y., Labrijn, A.F., Xiao, X., Binley, J.M., Zhang, M.Y., Sidorov, I.A., Broder, C.C., Robinson, J., Parren, P.W., Burton, D.R., Dimitrov, D.S. Broadly cross-reactive HIV-1-neutralizing human monoclonal Fab selected for binding to gp120-CD4-CCR5 complexes. Proc. Natl. Acad. Sci. USA 99:6913-6918, 2002.
18. Schulke, N., Vesanen, M.S., Sanders, R.W., Zhu, P., Lu, M., Anselma, D.J., Villa, A.R., Parren, P.W., Binley, J.M., Roux, K.H., Maddon, P.J., Moore, J.P., Olson, W.C. Oligomeric and conformational properties of a proteolytically mature, disulfide-stabilized human immunodeficiency virus type 1 gp140 envelope glycoprotein. J. Virol. 76:7760-7776, 2002.

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19. Parker, C.E., Deterding, L.J., Hager-Braun, C., Binley, J.M., Schulke, N., Katinger, H., Moore, J.P., Tomer, K.B. Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody 2F5. J. Virol. 75:10906-10911, 2001.
20. Zwick, M.B., Labrijn, A.F., Wang, M., Spenlehauer, C., Saphire, E.O., Binley, J.M., Moore, J.P., Stiegler, G., Katinger, H., Burton, D.R., Parren, P.W. Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J. Virol. 75:10892-10905, 2001.

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21. Binley, J.M., Clas, B., Gettie, A., Vesanen, M., Montefiori, D.C., Sawyer, L., Booth, J., Lewis, M., Marx, P., Bonhoeffer, S., Moore, J.P. Passive infusion of immune serum into simian immunodeficiency virus-infected rhesus macaques undergoing a rapid disease course has minimal effects on plasma viremia. Virology 279:237-249, 2000.
22. Binley, J.M., Sanders, R.W., Clas, B., Schuelke, N., Master, A., Guo, Y., Kajumo, F., Anselma, D.J., Maddon, P.J., Olson, W.C., Moore, J.P. A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure. J. Virol. 74:627-643, 2000.
23. Binley, J.M., Schiller, D.S., Ortiz, G.M., Hurley, A., Nixon, D.F., Markowitz, M.M., Moore, J.P. The relationship between T-proliferative responses and plasma viremia during treatment of HIV-1 infection with combination antiviral therapy. J. Infect. Dis. 181:1249-1263, 2000.
24. Binley, J.M., Trkola, A., Ketas, T., Schiller, D., Clas, B., Hurley, A., Markowitz, M., Moore, J.P. The effect of highly active anti-retroviral therapy on binding and neutralizing antibody responses to human immunodeficiency virus type 1 infection. J. Infect. Dis. 182:945-949, 2000.
25. Sanders, R., Schiffner, L., Master, A., Kajumo, F., Guo, Y., Dragic, T., Moore, J.P., Binley, J.M. Incomplete processing of variable loop-deleted forms of the human immunodeficiency virus type 1 gp120-gp41 glycoprotein complex by the introduction of an intermolecular disulfide bridge between gp120 and the gp41 ectodomain. J. Virol. 74:5091-5100, 2000.
26. Schiller, D.S., Binley, J.M., Roux, K.H., Adamson, C.S., Jones, I.M., Krausslich, H-.G., Hurley, A., Markowitz, M., Moore, J.P. Parameters influencing measurement of the gag antigen-specific T-proliferative response to HIV-1 infection. AIDS Res. Hum. Retroviruses 16:259-271, 2000.

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27. Markowitz, M., Vesanen, M., Tenner-Racz, K., Cao, Y., Binley, J.M., Talal, A., Hurley, A., Jin, X., Heath-Chiozzi, M., Leonard, J.M., Moore, J.P., Racz, P., Nixon, D.F., Ho, D.D. The impact of combination antiretroviral therapy commenced soon after infection on HIV-1 replication and antiviral immune responses. J. Infect. Dis. 179:527-537, 1999.
28. Ortiz, G.M., Nixon, D.F., Trkola, A., Binley, J.M., Jin, X., Bonhoeffer, S., Kuebler, P.J., Donahoe, S.M., Demoitie, M-.A., Kakimoto, W.M., Ketas, T., Clas, B., Heyman, J.J., Zhang, L., Cao, Y., Hurley, A., Moore, J.P., Ho, D.D., Markowitz, M. HIV-1-specific immune responses in subjects who temporarily contain virus replication after discontinuation of HAART. J. Clin. Invest. 104:R13-R18, 1999.
29. Ramratnam, B., Bonhoeffer, S., Binley, J.M., Hurley, A., Zhang, L., Mittler, J.E., Markowitz, M., Moore, J.P., Perelson, A., Ho, D.D. Rapid production and clearance of HIV-1 and hepatitis C virus assessed by large volume plasma apheresis. Lancet 354:1782-5, 1999.

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30. Binley, J.M., Jin, X., Huang, Y., Zhang, L., Cao, Y., Ho, D.D., Moore, J.P. Persistent antibody responses but declining CTL responses to multiple human immunodeficiency type 1 antigens in a long-term nonprogressing individual with a defective p17 proviral sequence and no detectable viral RNA expression. J. Virol. 72:3472-3474, 1998.
31. Binley, J.M., Wyatt, R., Desjardin, E., Kwong, P.D., Hendrickson, W., Moore, J.P., Sodroski, J. Analysis of the interaction of antibodies with a conserved, enzymatically deglycosylated core of the HIV-1 gp120 envelope glycoprotein. AIDS Res. Hum. Retroviruses 14:191-198, 1998.
32. Connor, R.I., Montefiori, D.C., Binley, J.M., Moore, J.P., Bonhoeffer, S., Gettie, A., Sheridan, K.E., Ho, D.D., Dailey, P.J., Marx, P.A. Temporal analyses of virus replication, immune responses and efficacy in rhesus macaques immunized with a live, attenuated SIV vaccine. J. Virol. 72:7501-7509, 1998.
33. LaCasse, R.A., Follis, K.E., Moudgil, T., Trahey, M., Binley, J.M., Planelles, V., Zolla-Pazner, S., Nunberg, J.H. Coreceptor utilization by human immunodeficiency virus type 1 is not a primary determinant of neutralization sensitivity. J. Virol. 72:2491-2495, 1998.
34. Morris, L., Binley, J.M., Clas, B.A., Astill, T.P., Kost, R., Hurley, A., Bonhoeffer, S., Cao, Y., Markowitz, M., Ho, D.D., Moore, J.P. HIV-1 antigen-specific and non-specific B cell responses are sensitive to combination anti-retroviral therapy. J. Exp. Med. 188:233-245, 1998.
35. Parren, P.W.H.I., Wang, M., Trkola, A., Binley, J.M., Purtscher, M., Katinger, H., Moore, J.P., Burton, D.R. Antibody neutralization-resistant primary isolates of HIV-1. J. Virol. 71:10270-10274, 1998.
36. Sullivan, N., Sun, Y., Binley, J.M., Lee, J., Barbas, C.F., Parren, P.W.H.I., Burton, D.R., Sodroski, J. Determinants of HIV-1 envelope glycoprotein activation by soluble CD4 and monoclonal antibodies. J. Virol. 72:6332-6338, 1998.
37. Trkola, A., Ketas, T., KewalRamani, V.N., Endorf, F., Binley, J.M., Katinger, H., Robinson, J., Littman, D.R., Moore, J.P. Neutralization sensitivity of human immunodeficiency virus type-1 primary isolates to antibodies and CD4-based reagents is independent of co-receptor usage. J. Virol. 72:1876-1885, 1998.

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38. Binley, J.M., Arshad, H., Fouts, T.R., Moore, J.P. An investigation of the high-avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses 13:1007-1015, 1997
39. Binley, J.M., Klasse, P.J., Cao, Y., Jones, I., Markowitz, M., Ho, D.D., Moore, J.P. Differential regulation of the antibody responses to gag and env proteins of human immunodeficiency virus type 1. J. Virol. 71:2799-2809, 1997.
40. Ditzel, H.J., Parren, P.W.H.I., Binley, J.M., Sodroski, J., Moore, J.P., Barbas, C.F., Burton, D.R. Mapping the protein surface of HIV-1 gp120 using human monoclonal antibodies from phage display libraries. J. Mol. Biol. 267:684-695, 1997
41. Wyatt, R., Desjardin, E., Olshevsky, U., Nixon, C., Binley, J., Olshevsky, V., Sodroski, J. 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.

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42. Binley, J.M., Ditzel, H.J., Barbas, C.F., Sullivan, N., Sodroski, J., Parren, P.W.H.I., Burton, D.R. Human antibody responses to HIV-1 glycoprotein 41 cloned in phage display libraries suggest three major epitopes are recognized and give evidence for conserved antibody motifs in antigen binding. AIDS Res. Hum. Retroviruses 12: 911-924, 1996.
43. Fouts, T.R., Binley, J.M., Trkola, A., Robinson, J.E., Moore, J.P. Neutralization of the Human Immunodeficiency Virus Type 1 primary isolate JR-FL by human monoclonal antibodies correlates with antibody binding to the oligomeric form of the envelope glycoprotein complex. J. Virol. 71:2779-2785, 1996.
44. Parren, P.W.H.I., Fisicaro, P., Labrijn, A., Binley, J.M., Yang, W., Ditzel, H.J., Barbas, C.F., Burton, D.R. In vitro antigen “challenge” of human antibody libraries for vaccine evaluation: The human immunodeficiency virus type 1 envelope. J. Virol. 70:9046-9050, 1996.
45. Seligman, S.J., Binley, J.M., Gorny, M.K., Burton, D.R., Zolla-Pazner, S., Sokolowski, K.A. Characterization by serial deletion competition ELISAs of HIV-1 V3 loop epitopes recognized by monoclonal antibodies. Mol. Immunol. 33:737-745, 1996.
46. Trkola, A., Dragic, T., Arthos, J., Binley, J.M., Olson, W.C., Allaway, G.P., Cheng-Mayer, C., Robinson, J., Maddon, P.J., Moore, J.P. CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5. Nature 384:184-187, 1996.

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47. Ditzel, H.J., Binley, J.M., Moore, J.P., Sodroski, J., Sullivan, N., Sawyer, L.S.W., Hendry, R.M., Yang, W., Barbas III, C.F., Burton, D. Neutralizing recombinant human antibodies to a site-sensitive epitope of HIV-1 gp120 isolated using an epitope masking procedure. J. Immunol. 154:893-906, 1995.
48. Parren, P.W.H.I., Ditzel, H.J., Gulizia, R.J., Binley, J.M., Barbas, C.F., Burton, D.R., Mosier, D.E. Protection against human immunodeficiency virus type I infection by induction of passive immunity with a neutralizing human monoclonal antibody directed against the envelope glycoprotein's CD4 binding site. AIDS 9:F1-F6, 1995.

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49. Barbas, C.F., Collet, T.A., Amberg, W., Roben., P., Binley, J.M., Hoekestra, D., Cababa, D., Jones, T.M., Williamson., R.A., Pilkington, G.R., Haigwood, N.L., Cabezas, E., Satterthwait, A., Sanz, I., Burton, D.R. Molecular profile of an antibody response to HIV-1 as probed by combinatorial libraries. J. Mol. Biol. 230:812-823, 1993.