Skip to main content
  • ASM
    • Antimicrobial Agents and Chemotherapy
    • Applied and Environmental Microbiology
    • Clinical Microbiology Reviews
    • Clinical and Vaccine Immunology
    • EcoSal Plus
    • Infection and Immunity
    • Journal of Bacteriology
    • Journal of Clinical Microbiology
    • Journal of Microbiology & Biology Education
    • Journal of Virology
    • mBio
    • Microbiology and Molecular Biology Reviews
    • Microbiology Resource Announcements
    • Microbiology Spectrum
    • Molecular and Cellular Biology
    • mSphere
    • mSystems
  • Log in
  • My alerts
  • My Cart

Main menu

  • Home
  • Articles
    • Current Issue
    • Accepted Manuscripts
    • COVID-19 Special Collection
    • Minireviews
    • JVI Classic Spotlights
    • Archive
  • For Authors
    • Submit a Manuscript
    • Scope
    • Editorial Policy
    • Submission, Review, & Publication Processes
    • Organization and Format
    • Errata, Author Corrections, Retractions
    • Illustrations and Tables
    • Nomenclature
    • Abbreviations and Conventions
    • Publication Fees
    • Ethics Resources and Policies
  • About the Journal
    • About JVI
    • Editor in Chief
    • Editorial Board
    • For Reviewers
    • For the Media
    • For Librarians
    • For Advertisers
    • Alerts
    • RSS
    • FAQ
  • Subscribe
    • Members
    • Institutions
  • ASM
    • Antimicrobial Agents and Chemotherapy
    • Applied and Environmental Microbiology
    • Clinical Microbiology Reviews
    • Clinical and Vaccine Immunology
    • EcoSal Plus
    • Infection and Immunity
    • Journal of Bacteriology
    • Journal of Clinical Microbiology
    • Journal of Microbiology & Biology Education
    • Journal of Virology
    • mBio
    • Microbiology and Molecular Biology Reviews
    • Microbiology Resource Announcements
    • Microbiology Spectrum
    • Molecular and Cellular Biology
    • mSphere
    • mSystems

User menu

  • Log in
  • My alerts
  • My Cart

Search

  • Advanced search
Journal of Virology
publisher-logosite-logo

Advanced Search

  • Home
  • Articles
    • Current Issue
    • Accepted Manuscripts
    • COVID-19 Special Collection
    • Minireviews
    • JVI Classic Spotlights
    • Archive
  • For Authors
    • Submit a Manuscript
    • Scope
    • Editorial Policy
    • Submission, Review, & Publication Processes
    • Organization and Format
    • Errata, Author Corrections, Retractions
    • Illustrations and Tables
    • Nomenclature
    • Abbreviations and Conventions
    • Publication Fees
    • Ethics Resources and Policies
  • About the Journal
    • About JVI
    • Editor in Chief
    • Editorial Board
    • For Reviewers
    • For the Media
    • For Librarians
    • For Advertisers
    • Alerts
    • RSS
    • FAQ
  • Subscribe
    • Members
    • Institutions
Pathogenesis and Immunity

Neutralization Profiles of Newly Transmitted Human Immunodeficiency Virus Type 1 by Monoclonal Antibodies 2G12, 2F5, and 4E10

Saurabh Mehandru, Terri Wrin, Justin Galovich, Gabriela Stiegler, Brigitta Vcelar, Arlene Hurley, Christine Hogan, Sandhya Vasan, Hermann Katinger, Christos J. Petropoulos, Martin Markowitz
Saurabh Mehandru
1Aaron Diamond AIDS Research Center, Rockefeller University, New York, New York
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Terri Wrin
2ViroLogic, Inc., South San Francisco, California
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Justin Galovich
2ViroLogic, Inc., South San Francisco, California
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Gabriela Stiegler
3Polymun Scientific, Vienna, Austria
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Brigitta Vcelar
3Polymun Scientific, Vienna, Austria
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Arlene Hurley
1Aaron Diamond AIDS Research Center, Rockefeller University, New York, New York
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Christine Hogan
1Aaron Diamond AIDS Research Center, Rockefeller University, New York, New York
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Sandhya Vasan
1Aaron Diamond AIDS Research Center, Rockefeller University, New York, New York
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Hermann Katinger
3Polymun Scientific, Vienna, Austria
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Christos J. Petropoulos
2ViroLogic, Inc., South San Francisco, California
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Martin Markowitz
1Aaron Diamond AIDS Research Center, Rockefeller University, New York, New York
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • For correspondence: mmarkowitz@adarc.org
DOI: 10.1128/JVI.78.24.14039-14042.2004
  • Article
  • Figures & Data
  • Info & Metrics
  • PDF
Loading

ABSTRACT

As the AIDS epidemic continues unabated, the development of a human immunodeficiency virus (HIV) vaccine is critical. Ideally, an effective vaccine should elicit cell-mediated and neutralizing humoral immune responses. We have determined the in vitro susceptibility profile of sexually transmitted viruses from 91 patients with acute and early HIV-1 infection to three monoclonal antibodies, 2G12, 2F5, and 4E10. Using a recombinant virus assay to measure neutralization, we found all transmitted viruses were neutralized by 4E10, 80% were neutralized by 2F5, and only 37% were neutralized by 2G12. We propose that the induction of 4E10-like antibodies should be a priority in designing immunogens to prevent HIV-1 infection.

The global human immunodeficiency virus (HIV)/AIDS epidemic marches on, with an estimated 5 million new infections occurring in 2003 (25). Demand for an effective HIV-1 vaccine remains unanswered, and there remains a lack of consensus on which immune responses a successful vaccine should induce (6). Enthusiasm for the potential of inducing neutralizing antibodies as an effective vaccine strategy waned early during the epidemic when it became clear that the neutralization profiles of field isolates were markedly different from laboratory-adapted strains (14, 21). Coupled with the observed relationship between host cell-mediated immune responses and plasma viremia in vivo (19), the vaccine effort swung toward the design of immunogens such as DNA and recombinant viral vectors, theoretically capable of stimulating cell-mediated responses (24, 26). More recently however, it is clear that in the simian immunodeficiency virus model, these immunogens may at best alter early events and clinical course but may not provide adequate protection from clinically significant infection (16, 17). Thus, interest in immunogens capable of inducing neutralizing antibodies has once again emerged.

Our initial interest in studying neutralizing antibodies was mainly therapeutic and stimulated by passive immunotherapy studies in which HIV-1 or simian immunodeficiency virus infection could be prevented or the clinical course ameliorated (5, 7-9, 13, 15). The identification and availability of broadly reactive human monoclonal antibodies (MAbs) offer a novel therapeutic modality, perhaps as a potential adjunct to highly active antiretroviral therapy. We have previously hypothesized that subjects identified during acute and early infection and treated promptly and aggressively with highly active antiretroviral therapy would have minimal residual viral burdens after 2 to 3 years of therapy, a viral burden that may be amenable to control with adjunctive therapies that may assist the host in immunologically controlling the infection if treatment is interrupted or discontinued (12).

Three neutralizing MAbs, 2G12, 2F5, and 4E10, have been produced commercially and are available for experimental use both prophylactically (5, 7, 9, 13, 15) and therapeutically (1, 22). 2G12 recognizes a cluster of carbohydrate residues on gp120. This is an unusual antibody with a unique structure capable of binding to clusters of oligomannose-type sugars and interfering with viral binding and entry (3). There are two additional MAbs, 2F5 and 4E10, that recognize adjacent but distinct epitopes on the membrane-proximal region of the gp41 ectodomain and probably act by inhibiting the fusion process. The antibody 2F5 binds to the ELDKWA motif on the ectodomain of gp41 (18), whereas 4E10 likely recognizes an ordered helical peptide structure in gp41 created in part by the epitope NWFDIT slightly upstream from the 2F5 binding site (4, 23, 27).

As a prelude to recruiting patients for a phase I trial of these MAbs, we examined the neutralization profiles of newly transmitted viruses to 2G12, 2F5, and 4E10 and compared this to the profiles of NL4-3, an X-4-tropic laboratory-adapted strain of HIV-1, and JRCSF, an R5-tropic strain of HIV-1. Plasma from 91 newly infected subjects (Table 1), defined by the presence of HIV-1 viremia with either a negative or indeterminate serology or a negative detuned enzyme-linked immunosorbent assay (10), was chosen for susceptibility testing.

A previously described recombinant viral assay was used to measure virus-antibody neutralization (20). In brief, nucleic acid derived from HIV-positive plasma was amplified by reverse transcription-PCR and incorporated into an expression vector (pCXAS) by conventional cloning methods. Recombinant HIV-1 stocks expressing patient virus envelope proteins were prepared by cotransfecting HEK293 cells with a replication-defective, luciferase expression cassette containing HIV-1 genomic viral vector and an appropriate envelope expression vector. Pseudotyped recombinant viruses were harvested 48 h posttransfection and incubated for 1 h at 37°C with serial fourfold dilutions of the three MAbs and plasma controls. U87 cells that express CD4, CCR5, and CXCR4 were inoculated with virus-antibody dilutions. Luciferase activity determined 72 h postinoculation was used as the indicator of infectivity. Neutralizing activity was displayed as the percent inhibition of luciferase production at each antibody concentration compared to that of an antibody-negative control. The 50% inhibitory concentration (IC50) is defined as the concentration of MAb required to inhibit virus infectivity by 50%. For the purposes of this study, viruses were classified as susceptible to neutralization if the IC50 for a particular antibody was ≤50 μg/ml.

All 91 viruses tested were neutralized by 4E10, whereas 74 of 91 (81%) were susceptible to neutralization to 2F5. In contrast, only 38 of 91 (38%) of the transmitted isolates were susceptible to neutralization by 2G12 (Table 2). Thirty-three of 91 subjects (36%) harbored transmitted virus susceptible to neutralization by all three MAbs, and 78 of 91 (86%) isolates were susceptible to at least two MAbs.

The range of susceptibilities was quite broad, although in general if susceptible, IC50s were below 10 μg/ml (Fig. 1). Mean IC50s of 2F5, 2G12, and 4E10 for susceptible isolates were 7.64, 12.17, and 9.74 μg/ml, respectively. Susceptibility to neutralization by 4E10 and 2F5 was highly correlated (R = 0.667, P < 0.0001), whereas susceptibility to 2G12 did not predict susceptibility to the other two MAbs. Both NL4-3 and JRCSF were on average more susceptible to neutralization by all three MAbs, although both were markedly more susceptible to the effect of 2G12 when compared to the 91 transmitted isolates. It is worth noting that the median values for susceptibility of the 91 isolates to 2F5 and 4E10 were 5.45 and 6.53 μg/ml, respectively, and were quite comparable to the IC50s observed for both NL4-3 and JRCSF (Table 2). We could not demonstrate a relationship between the duration of infection, CD4 cell count, or HIV-1 RNA levels and degree of susceptibility to neutralization.

These findings have important implications for vaccine development. We have found that essentially all newly acquired isolates screened for susceptibility to three available MAbs were susceptible to neutralization by 4E10. These data are in agreement with data cited by Binley and Burton in a recent editorial (2). Importantly, all 91 viruses tested here were recently transmitted, in the range of weeks to months. It is critical to note that all isolates are clade B and 98% were transmitted to men having sex with men. This would imply that the identification of an immunogen capable of eliciting a 4E10-like antibody response in vivo could well provide an effective vaccine strategy for HIV-1 prophylaxis. This said, it must be emphasized that the viruses studied were not necessarily identical to the viruses transmitted as infection had been established weeks to months prior to presentation and the in vivo generation time of HIV-1 of 2 days (11) would allow for some degree of viral diversity.

The relatively low number of newly transmitted viruses susceptible to 2G12 was somewhat unexpected and differs from a previous report in which 22 of 30 (73%) of clade B isolates were susceptible to neutralization by 2G12 (2). Barring confounding factors, such as assay differences and variation in lots of MAbs, an explanation for this observation is that the isolates tested here were newly transmitted and may be less susceptible to neutralization by 2G12. That the duration of infection did not positively correlate with 2G12 susceptibility argues against this explanation. This said, studies are currently under way to better understand the correlation of envelope structure and 2G12 susceptibility.

We believe that these data should be interpreted cautiously. It is not clear that the definition of susceptibility (that is an IC50 of ≤50 μg/ml) is clinically relevant. Ideally one would want to achieve ICs in the 99% range, and the susceptibility curves suggest that these antibody concentrations are substantially higher than the IC50s determined (Fig. 2). Furthermore, given the nature of HIV-1 transmission and dissemination, concentrations of neutralizing antibodies in plasma may not necessarily be predictive of such at mucosal surfaces or in tissue compartments. Nevertheless, we believe our unique data set supports the renewed interest in the design of immunogens with the potential to induce neutralizing antibodies, and the design of those with 4E10-like induction capacity should assume the highest priority.

FIG. 1.
  • Open in new tab
  • Download powerpoint
FIG. 1.

Neutralization profile of each of the three MAbs. The mean IC50 of the three MAbs (micrograms per milliliter), grouped on the x axis, is represented against the number of susceptible viral isolates on the y axis.

FIG. 2.
  • Open in new tab
  • Download powerpoint
FIG. 2.

Recombinant viral assay to determine the sensitivity of patient-derived virus to the MAbs 2F5, 2G12, and 4E10. (A) Patient sample demonstrating susceptibility to all three MAbs: 2F5 (IC50, 1.74 μg/ml), 2G12 (IC50, 4.32 μg/ml), and 4E10 (IC50, 1.88 μg/ml). (B) Patient sample susceptible to both 2F5 (IC50, 6.49 μg/ml) and 4E10 (IC50, 5.88 μg/ml) but not to 2G12 (IC50, >50 μg/ml). (C) Susceptibility to 4E10 is preserved (IC50, 8.87 μg/ml) in the face of resistance to both 2G12 (IC50, >50 μg/ml) and 2F5 (IC50, >50 μg/ml).

View this table:
  • View inline
  • View popup
TABLE 1.

Patient characteristics in this study

View this table:
  • View inline
  • View popup
TABLE 2.

Susceptibility profile of transmitted viruses from 91 newly infected patients to MAbs 2F5, 2G12, and 4E10

FOOTNOTES

    • Received 7 May 2004.
    • Accepted 6 August 2004.
  • Copyright © 2004 American Society for Microbiology

REFERENCES

  1. 1.↵
    Armbruster, C., G. M. Stiegler, B. A. Vcelar, W. Jager, N. L. Michael, N. Vetter, and H. W. Katinger. 2002. A phase I trial with two human monoclonal antibodies (hMAb 2F5, 2G12) against HIV-1. AIDS16:227-233.
    OpenUrlCrossRefPubMedWeb of Science
  2. 2.↵
    Burton, D. R., R. C. Desrosiers, R. W. Doms, W. C. Koff, P. D. Kwong, J. P. Moore, G. J. Nabel, J. Sodroski, I. A. Wilson, and R. T. Wyatt. 2004. HIV vaccine design and the neutralizing antibody problem. Nat. Immunol.5:233-236.
    OpenUrlCrossRefPubMedWeb of Science
  3. 3.↵
    Calarese, D. A., C. N. Scanlan, M. B. Zwick, S. Deechongkit, Y. Mimura, R. Kunert, P. Zhu, M. R. Wormald, R. L. Stanfield, K. H. Roux, J. W. Kelly, P. M. Rudd, R. A. Dwek, H. Katinger, D. R. Burton, and I. A. Wilson. 2003. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science300:2065-2071.
    OpenUrlAbstract/FREE Full Text
  4. 4.↵
    Cardosa, R., M. B. Zwick, R. Kunert, H. Katinger, D. R. Burton, and I. A. Wilson. 2003. Structural insights for 4E10 antibody neutralization on HIV-1. AIDS Vaccine 2003, New York, N.Y. [Online.] http://www.aidsvaccine2003.org .
  5. 5.↵
    Conley, A. J., J. A. Kessler II, L. J. Boots, P. M. McKenna, W. A. Schleif, E. A. Emini, G. E. Mark III, H. Katinger, E. K. Cobb, S. M. Lunceford, S. R. Rouse, and K. K. Murthy. 1996. The consequence of passive administration of an anti-human immunodeficiency virus type 1 neutralizing monoclonal antibody before challenge of chimpanzees with a primary virus isolate. J. Virol.70:6751-6758.
    OpenUrlAbstract/FREE Full Text
  6. 6.↵
    Desrosiers, R. C. 2004. Prospects for an AIDS vaccine. Nat. Med.10:221-223.
    OpenUrlCrossRefPubMedWeb of Science
  7. 7.↵
    Ferrantelli, F., R. Hofmann-Lehmann, R. A. Rasmussen, T. Wang, W. Xu, P. L. Li, D. C. Montefiori, L. A. Cavacini, H. Katinger, G. Stiegler, D. C. Anderson, H. M. McClure, and R. M. Ruprecht. 2003. Post-exposure prophylaxis with human monoclonal antibodies prevented SHIV89.6P infection or disease in neonatal macaques. AIDS17:301-309.
    OpenUrlCrossRefPubMedWeb of Science
  8. 8.
    Ferrantelli, F., R. A. Rasmussen, R. Hofmann-Lehmann, W. Xu, H. M. McClure, and R. M. Ruprecht. 2002. Do not underestimate the power of antibodies—lessons from adoptive transfer of antibodies against HIV. Vaccine20(Suppl. 4):A61-A65.
    OpenUrlCrossRefPubMed
  9. 9.↵
    Hofmann-Lehmann, R., J. Vlasak, R. A. Rasmussen, B. A. Smith, T. W. Baba, V. Liska, F. Ferrantelli, D. C. Montefiori, H. M. McClure, D. C. Anderson, B. J. Bernacky, T. A. Rizvi, R. Schmidt, L. R. Hill, M. E. Keeling, H. Katinger, G. Stiegler, L. A. Cavacini, M. R. Posner, T.-C. Chou, J. Andersen, and R. M. Ruprecht. 2001. Postnatal passive immunization of neonatal macaques with a triple combination of human monoclonal antibodies against oral simian-human immunodeficiency virus challenge. J. Virol.75:7470-7480.
    OpenUrlAbstract/FREE Full Text
  10. 10.↵
    Janssen, R. S., G. A. Satten, S. L. Stramer, B. D. Rawal, T. R. O'Brien, B. J. Weiblen, F. M. Hecht, N. Jack, F. R. Cleghorn, J. O. Kahn, M. A. Chesney, and M. P. Busch. 1998. New testing strategy to detect early HIV-1 infection for use in incidence estimates and for clinical and prevention purposes. JAMA280:42-48.
    OpenUrlCrossRefPubMedWeb of Science
  11. 11.↵
    Markowitz, M., M. Louie, A. Hurley, E. Sun, M. Di Mascio, A. S. Perelson, and D. D. Ho. 2003. A novel antiviral intervention results in more accurate assessment of human immunodeficiency virus type 1 replication dynamics and T-cell decay in vivo. J. Virol.77:5037-5038.
    OpenUrlAbstract/FREE Full Text
  12. 12.↵
    Markowitz, M., M. Vesanen, K. Tenner-Racz, Y. Cao, J. M. Binley, A. Talal, A. Hurley, X. Jin, M. R. Chaudhry, M. Yaman, S. Frankel, M. Heath-Chiozzi, J. M. Leonard, J. P. Moore, P. Racz, D. F. Nixon, D. D. Ho, and X. Jin. 1999. The effect of commencing combination antiretroviral therapy soon after human immunodeficiency virus type 1 infection on viral replication and antiviral immune responses. J. Infect. Dis.179:527-537.
    OpenUrlCrossRefPubMedWeb of Science
  13. 13.↵
    Mascola, J. R., M. G. Lewis, G. Stiegler, D. Harris, T. C. VanCott, D. Hayes, M. K. Louder, C. R. Brown, C. V. Sapan, S. S. Frankel, Y. Lu, M. L. Robb, H. Katinger, and D. L. Birx. 1999. Protection of macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies. J. Virol.73:4009-4018.
    OpenUrlAbstract/FREE Full Text
  14. 14.↵
    Mascola, J. R., S. W. Snyder, O. S. Weislow, S. M. Belay, R. B. Belshe, D. H. Schwartz, M. L. Clements, R. Dolin, B. S. Graham, G. J. Gorse, M. C. Keefer, M. J. McElrath, M. C. Walker, K. F. Wagner, J. G. McNeil, F. E. McCutchan, D. S. Burke, et al. 1996. Immunization with envelope subunit vaccine products elicits neutralizing antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus type 1. J. Infect. Dis.173:340-348.
    OpenUrlCrossRefPubMedWeb of Science
  15. 15.↵
    Mascola, J. R., G. Stiegler, T. C. VanCott, H. Katinger, C. B. Carpenter, C. E. Hanson, H. Beary, D. Hayes, S. S. Frankel, D. L. Birx, and M. G. Lewis. 2000. Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies. Nat. Med.6:207-210.
    OpenUrlCrossRefPubMedWeb of Science
  16. 16.↵
    Mortara, L., F. Letourneur, H. Gras-Masse, A. Venet, J.-G. Guillet, and I. Bourgault-Villada. 1998. Selection of virus variants and emergence of virus escape mutants after immunization with an epitope vaccine. J. Virol.72:1403-1410.
    OpenUrlAbstract/FREE Full Text
  17. 17.↵
    Mortara, L., F. Letourneur, P. Villefroy, C. Beyer, H. Gras-Masse, J. G. Guillet, and I. Bourgault-Villada. 2000. Temporal loss of Nef-epitope CTL recognition following macaque lipopeptide immunization and SIV challenge. Virology278:551-561.
    OpenUrlCrossRefPubMedWeb of Science
  18. 18.↵
    Muster, T., F. Steindl, M. Purtscher, A. Trkola, A. Klima, G. Himmler, F. Ruker, and H. Katinger. 1993. A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J. Virol.67:6642-6647.
    OpenUrlAbstract/FREE Full Text
  19. 19.↵
    Ogg, G. S., X. Jin, S. Bonhoeffer, P. R. Dunbar, M. A. Nowak, S. Monard, J. P. Segal, Y. Cao, S. L. Rowland-Jones, V. Cerundolo, A. Hurley, M. Markowitz, D. D. Ho, D. F. Nixon, and A. J. McMichael. 1998. Quantitation of HIV-1-specific cytotoxic T lymphocytes and plasma load of viral RNA. Science279:2103-2106.
    OpenUrlAbstract/FREE Full Text
  20. 20.↵
    Petropoulos, C. J., N. T. Parkin, K. L. Limoli, Y. S. Lie, T. Wrin, W. Huang, H. Tian, D. Smith, G. A. Winslow, D. J. Capon, and J. M. Whitcomb. 2000. A novel phenotypic drug susceptibility assay for human immunodeficiency virus type 1. Antimicrob. Agents Chemother.44:920-928.
    OpenUrlAbstract/FREE Full Text
  21. 21.↵
    Sattentau, Q. J. 1996. Neutralization of HIV-1 by antibody. Curr. Opin. Immunol.8:540-545.
    OpenUrlCrossRefPubMed
  22. 22.↵
    Stiegler, G., C. Armbruster, B. Vcelar, H. Stoiber, R. Kunert, N. L. Michael, L. L. Jagodzinski, C. Ammann, W. Jager, J. Jacobson, N. Vetter, and H. Katinger. 2002. Antiviral activity of the neutralizing antibodies 2F5 and 2G12 in asymptomatic HIV-1-infected humans: a phase I evaluation. AIDS16:2019-2025.
    OpenUrlCrossRefPubMedWeb of Science
  23. 23.↵
    Stiegler, G., R. Kunert, M. Purtscher, S. Wolbank, R. Voglauer, F. Steindl, and H. Katinger. 2001. A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1. AIDS Res. Hum. Retrovir.17:1757-1765.
    OpenUrlCrossRefPubMedWeb of Science
  24. 24.↵
    Tang, D. C., M. DeVit, and S. A. Johnston. 1992. Genetic immunization is a simple method for eliciting an immune response. Nature356:152-154.
    OpenUrlCrossRefPubMedWeb of Science
  25. 25.↵
    UNAIDS. 2003. AIDS epidemic update 2003. [Online.] http://wwwunaids.org .
  26. 26.↵
    Wang, B., K. E. Ugen, V. Srikantan, M. G. Agadjanyan, K. Dang, Y. Refaeli, A. I. Sato, J. Boyer, W. V. Williams, and D. B. Weiner. 1993. Gene inoculation generates immune responses against human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. USA90:4156-4160.
    OpenUrlAbstract/FREE Full Text
  27. 27.↵
    Zwick, M. B., A. F. Labrijn, M. Wang, C. Spenlehauer, E. O. Saphire, J. M. Binley, J. P. Moore, G. Stiegler, H. Katinger, D. R. Burton, and P. W. H. I. Parren. 2001. Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J. Virol.75:10892-10905.
    OpenUrlAbstract/FREE Full Text
PreviousNext
Back to top
Download PDF
Citation Tools
Neutralization Profiles of Newly Transmitted Human Immunodeficiency Virus Type 1 by Monoclonal Antibodies 2G12, 2F5, and 4E10
Saurabh Mehandru, Terri Wrin, Justin Galovich, Gabriela Stiegler, Brigitta Vcelar, Arlene Hurley, Christine Hogan, Sandhya Vasan, Hermann Katinger, Christos J. Petropoulos, Martin Markowitz
Journal of Virology Nov 2004, 78 (24) 14039-14042; DOI: 10.1128/JVI.78.24.14039-14042.2004

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
Print

Alerts
Sign In to Email Alerts with your Email Address
Email

Thank you for sharing this Journal of Virology article.

NOTE: We request your email address only to inform the recipient that it was you who recommended this article, and that it is not junk mail. We do not retain these email addresses.

Enter multiple addresses on separate lines or separate them with commas.
Neutralization Profiles of Newly Transmitted Human Immunodeficiency Virus Type 1 by Monoclonal Antibodies 2G12, 2F5, and 4E10
(Your Name) has forwarded a page to you from Journal of Virology
(Your Name) thought you would be interested in this article in Journal of Virology.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
Neutralization Profiles of Newly Transmitted Human Immunodeficiency Virus Type 1 by Monoclonal Antibodies 2G12, 2F5, and 4E10
Saurabh Mehandru, Terri Wrin, Justin Galovich, Gabriela Stiegler, Brigitta Vcelar, Arlene Hurley, Christine Hogan, Sandhya Vasan, Hermann Katinger, Christos J. Petropoulos, Martin Markowitz
Journal of Virology Nov 2004, 78 (24) 14039-14042; DOI: 10.1128/JVI.78.24.14039-14042.2004
del.icio.us logo Digg logo Reddit logo Twitter logo CiteULike logo Facebook logo Google logo Mendeley logo
  • Top
  • Article
    • ABSTRACT
    • FOOTNOTES
    • REFERENCES
  • Figures & Data
  • Info & Metrics
  • PDF

KEYWORDS

Antibodies, Monoclonal
HIV Antibodies
HIV Infections
HIV-1

Related Articles

Cited By...

About

  • About JVI
  • Editor in Chief
  • Editorial Board
  • Policies
  • For Reviewers
  • For the Media
  • For Librarians
  • For Advertisers
  • Alerts
  • RSS
  • FAQ
  • Permissions
  • Journal Announcements

Authors

  • ASM Author Center
  • Submit a Manuscript
  • Article Types
  • Ethics
  • Contact Us

Follow #Jvirology

@ASMicrobiology

       

 

JVI in collaboration with

American Society for Virology

ASM Journals

ASM journals are the most prominent publications in the field, delivering up-to-date and authoritative coverage of both basic and clinical microbiology.

About ASM | Contact Us | Press Room

 

ASM is a member of

Scientific Society Publisher Alliance

 

American Society for Microbiology
1752 N St. NW
Washington, DC 20036
Phone: (202) 737-3600

Copyright © 2021 American Society for Microbiology | Privacy Policy | Website feedback

Print ISSN: 0022-538X; Online ISSN: 1098-5514