Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1995 Nov;69(11):6609–6617. doi: 10.1128/jvi.69.11.6609-6617.1995

Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG.

A Trkola 1, A B Pomales 1, H Yuan 1, B Korber 1, P J Maddon 1, G P Allaway 1, H Katinger 1, C F Barbas 3rd 1, D R Burton 1, D D Ho 1, et al.
PMCID: PMC189569  PMID: 7474069

Abstract

We have tested three human monoclonal antibodies (MAbs) IgG1b12, 2G12, and 2F5) to the envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1), and a tetrameric CD4-IgG molecule (CD4-IgG2), for the ability to neutralize primary HIV-1 isolates from the genetic clades A through F and from group O. Each of the reagents broadly and potently neutralized B-clade isolates. The 2F5 MAb and the CD4-IgG2 molecule also neutralized strains from outside the B clade, with the same breadth and potency that they showed against B-clade strains. The other two MAbs were able to neutralize a significant proportion of strains from outside the B clade, although there was a reduction in their efficacy compared with their activity against B-clade isolates. Neutralization of isolates by 2F5 correlated with their possession of the LDKW motif in a segment of gp41 near the membrane-spanning domain. The other two MAbs and CD4-IgG2 recognize discontinuous binding sites on gp120, and so no comparison between genetic sequence and virus neutralization was possible. Our data show that a vaccine based on the induction of humoral immunity that is broadly active across the genetic clades is not impossible if immunogens that express the epitopes for MAbs such as 2F5, 2G12, and IgG1b12 in immunogenic configurations can be created. Furthermore, if the three MAbs and CD4-IgG2 produce clinical benefit in immunotherapeutic trials in the United States or Europe, they may also do so elsewhere in the world.

Full Text

The Full Text of this article is available as a PDF (301.8 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abimiku A. G., Stern T. L., Zwandor A., Markham P. D., Calef C., Kyari S., Saxinger W. C., Gallo R. C., Robert-Guroff M., Reitz M. S. Subgroup G HIV type 1 isolates from Nigeria. AIDS Res Hum Retroviruses. 1994 Nov;10(11):1581–1583. doi: 10.1089/aid.1994.10.1581. [DOI] [PubMed] [Google Scholar]
  2. Allaway G. P., Davis-Bruno K. L., Beaudry G. A., Garcia E. B., Wong E. L., Ryder A. M., Hasel K. W., Gauduin M. C., Koup R. A., McDougal J. S. Expression and characterization of CD4-IgG2, a novel heterotetramer that neutralizes primary HIV type 1 isolates. AIDS Res Hum Retroviruses. 1995 May;11(5):533–539. doi: 10.1089/aid.1995.11.533. [DOI] [PubMed] [Google Scholar]
  3. Ashkenazi A., Smith D. H., Marsters S. A., Riddle L., Gregory T. J., Ho D. D., Capon D. J. Resistance of primary isolates of human immunodeficiency virus type 1 to soluble CD4 is independent of CD4-rgp120 binding affinity. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7056–7060. doi: 10.1073/pnas.88.16.7056. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bachmann M. H., Delwart E. L., Shpaer E. G., Lingenfelter P., Singal R., Mullins J. I. Rapid genetic characterization of HIV type 1 strains from four World Health Organization-sponsored vaccine evaluation sites using a heteroduplex mobility assay. WHO Network for HIV Isolation and Characterization. AIDS Res Hum Retroviruses. 1994 Nov;10(11):1345–1353. doi: 10.1089/aid.1994.10.1345. [DOI] [PubMed] [Google Scholar]
  5. Barbas C. F., 3rd, Hu D., Dunlop N., Sawyer L., Cababa D., Hendry R. M., Nara P. L., Burton D. R. In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity. Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3809–3813. doi: 10.1073/pnas.91.9.3809. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bobkov A., Cheingsong-Popov R., Garaev M., Rzhaninova A., Kaleebu P., Beddows S., Bachmann M. H., Mullins J. I., Louwagie J., Janssens W. Identification of an env G subtype and heterogeneity of HIV-1 strains in the Russian Federation and Belarus. AIDS. 1994 Dec;8(12):1649–1655. doi: 10.1097/00002030-199412000-00002. [DOI] [PubMed] [Google Scholar]
  7. Bolognesi D. P. Prospects for prevention of and early intervention against HIV. JAMA. 1989 May 26;261(20):3007–3013. [PubMed] [Google Scholar]
  8. Bou-Habib D. C., Roderiquez G., Oravecz T., Berman P. W., Lusso P., Norcross M. A. Cryptic nature of envelope V3 region epitopes protects primary monocytotropic human immunodeficiency virus type 1 from antibody neutralization. J Virol. 1994 Sep;68(9):6006–6013. doi: 10.1128/jvi.68.9.6006-6013.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Broder C. C., Earl P. L., Long D., Abedon S. T., Moss B., Doms R. W. Antigenic implications of human immunodeficiency virus type 1 envelope quaternary structure: oligomer-specific and -sensitive monoclonal antibodies. Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11699–11703. doi: 10.1073/pnas.91.24.11699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Buchacher A., Predl R., Strutzenberger K., Steinfellner W., Trkola A., Purtscher M., Gruber G., Tauer C., Steindl F., Jungbauer A. Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization. AIDS Res Hum Retroviruses. 1994 Apr;10(4):359–369. doi: 10.1089/aid.1994.10.359. [DOI] [PubMed] [Google Scholar]
  11. Burton D. R., Pyati J., Koduri R., Sharp S. J., Thornton G. B., Parren P. W., Sawyer L. S., Hendry R. M., Dunlop N., Nara P. L. Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science. 1994 Nov 11;266(5187):1024–1027. doi: 10.1126/science.7973652. [DOI] [PubMed] [Google Scholar]
  12. Cao Y., Qin L., Zhang L., Safrit J., Ho D. D. Virologic and immunologic characterization of long-term survivors of human immunodeficiency virus type 1 infection. N Engl J Med. 1995 Jan 26;332(4):201–208. doi: 10.1056/NEJM199501263320401. [DOI] [PubMed] [Google Scholar]
  13. Capon D. J., Chamow S. M., Mordenti J., Marsters S. A., Gregory T., Mitsuya H., Byrn R. A., Lucas C., Wurm F. M., Groopman J. E. Designing CD4 immunoadhesins for AIDS therapy. Nature. 1989 Feb 9;337(6207):525–531. doi: 10.1038/337525a0. [DOI] [PubMed] [Google Scholar]
  14. Chamat S., Nara P., Berquist L., Whalley A., Morrow W. J., Köhler H., Kang C. Y. Two major groups of neutralizing anti-gp120 antibodies exist in HIV-infected individuals. Evidence for epitope diversity around the CD4 attachment site. J Immunol. 1992 Jul 15;149(2):649–654. [PubMed] [Google Scholar]
  15. Cheingsong-Popov R., Lister S., Callow D., Kaleebu P., Beddows S., Weber J. Serotyping HIV type 1 by antibody binding to the V3 loop: relationship to viral genotype. WHO Network for HIV Isolation and Characterization. AIDS Res Hum Retroviruses. 1994 Nov;10(11):1379–1386. doi: 10.1089/aid.1994.10.1379. [DOI] [PubMed] [Google Scholar]
  16. Conley A. J., Kessler J. A., 2nd, Boots L. J., Tung J. S., Arnold B. A., Keller P. M., Shaw A. R., Emini E. A. Neutralization of divergent human immunodeficiency virus type 1 variants and primary isolates by IAM-41-2F5, an anti-gp41 human monoclonal antibody. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3348–3352. doi: 10.1073/pnas.91.8.3348. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Cordell J., Moore J. P., Dean C. J., Klasse P. J., Weiss R. A., McKeating J. A. Rat monoclonal antibodies to nonoverlapping epitopes of human immunodeficiency virus type 1 gp120 block CD4 binding in vitro. Virology. 1991 Nov;185(1):72–79. doi: 10.1016/0042-6822(91)90755-z. [DOI] [PubMed] [Google Scholar]
  18. Daar E. S., Li X. L., Moudgil T., Ho D. D. High concentrations of recombinant soluble CD4 are required to neutralize primary human immunodeficiency virus type 1 isolates. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6574–6578. doi: 10.1073/pnas.87.17.6574. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. De Wolf F., Hogervorst E., Goudsmit J., Fenyö E. M., Rübsamen-Waigmann H., Holmes H., Galvao-Castro B., Karita E., Wasi C., Sempala S. D. Syncytium-inducing and non-syncytium-inducing capacity of human immunodeficiency virus type 1 subtypes other than B: phenotypic and genotypic characteristics. WHO Network for HIV Isolation and Characterization. AIDS Res Hum Retroviruses. 1994 Nov;10(11):1387–1400. doi: 10.1089/aid.1994.10.1387. [DOI] [PubMed] [Google Scholar]
  20. Delwart E. L., Shpaer E. G., Louwagie J., McCutchan F. E., Grez M., Rübsamen-Waigmann H., Mullins J. I. Genetic relationships determined by a DNA heteroduplex mobility assay: analysis of HIV-1 env genes. Science. 1993 Nov 19;262(5137):1257–1261. doi: 10.1126/science.8235655. [DOI] [PubMed] [Google Scholar]
  21. Dumitrescu O., Kalish M. L., Kliks S. C., Bandea C. I., Levy J. A. Characterization of human immunodeficiency virus type 1 isolates from children in Romania: identification of a new envelope subtype. J Infect Dis. 1994 Feb;169(2):281–288. doi: 10.1093/infdis/169.2.281. [DOI] [PubMed] [Google Scholar]
  22. Gao F., Yue L., Craig S., Thornton C. L., Robertson D. L., McCutchan F. E., Bradac J. A., Sharp P. M., Hahn B. H. Genetic variation of HIV type 1 in four World Health Organization-sponsored vaccine evaluation sites: generation of functional envelope (glycoprotein 160) clones representative of sequence subtypes A, B, C, and E. WHO Network for HIV Isolation and Characterization. AIDS Res Hum Retroviruses. 1994 Nov;10(11):1359–1368. doi: 10.1089/aid.1994.10.1359. [DOI] [PubMed] [Google Scholar]
  23. Gürtler L. G., Hauser P. H., Eberle J., von Brunn A., Knapp S., Zekeng L., Tsague J. M., Kaptue L. A new subtype of human immunodeficiency virus type 1 (MVP-5180) from Cameroon. J Virol. 1994 Mar;68(3):1581–1585. doi: 10.1128/jvi.68.3.1581-1585.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Hanson C. V. Measuring vaccine-induced HIV neutralization: report of a workshop. AIDS Res Hum Retroviruses. 1994 Jun;10(6):645–648. doi: 10.1089/aid.1994.10.645. [DOI] [PubMed] [Google Scholar]
  25. Hariharan K., Nara P. L., Shabazz L. A., McCutchan J. A., Kang C. Y. Analysis of B cell repertoire specific to the neutralizing epitopes of glycoprotein 120 in HIV-infected individuals. AIDS Res Hum Retroviruses. 1994 Dec;10(12):1629–1637. doi: 10.1089/aid.1994.10.1629. [DOI] [PubMed] [Google Scholar]
  26. Ho D. D., McKeating J. A., Li X. L., Moudgil T., Daar E. S., Sun N. C., Robinson J. E. Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody. J Virol. 1991 Jan;65(1):489–493. doi: 10.1128/jvi.65.1.489-493.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Javaherian K., Langlois A. J., McDanal C., Ross K. L., Eckler L. I., Jellis C. L., Profy A. T., Rusche J. R., Bolognesi D. P., Putney S. D. Principal neutralizing domain of the human immunodeficiency virus type 1 envelope protein. Proc Natl Acad Sci U S A. 1989 Sep;86(17):6768–6772. doi: 10.1073/pnas.86.17.6768. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Kalish M. L., Luo C. C., Weniger B. G., Limpakarnjanarat K., Young N., Ou C. Y., Schochetman G. Early HIV type 1 strains in Thailand were not responsible for the current epidemic. AIDS Res Hum Retroviruses. 1994 Nov;10(11):1573–1575. doi: 10.1089/aid.1994.10.1573. [DOI] [PubMed] [Google Scholar]
  29. Kang C. Y., Hariharan K., Nara P. L., Sodroski J., Moore J. P. Immunization with a soluble CD4-gp120 complex preferentially induces neutralizing anti-human immunodeficiency virus type 1 antibodies directed to conformation-dependent epitopes of gp120. J Virol. 1994 Sep;68(9):5854–5862. doi: 10.1128/jvi.68.9.5854-5862.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Korber B. T., Allen E. E., Farmer A. D., Myers G. L. Heterogeneity of HIV-1 and HIV-2. AIDS. 1995;9 (Suppl A):S5–18. [PubMed] [Google Scholar]
  31. Korber B. T., MacInnes K., Smith R. F., Myers G. Mutational trends in V3 loop protein sequences observed in different genetic lineages of human immunodeficiency virus type 1. J Virol. 1994 Oct;68(10):6730–6744. doi: 10.1128/jvi.68.10.6730-6744.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Korber B. T., Osmanov S., Esparza J., Myers G. The World Health Organization Global Programme on AIDS proposal for standardization of HIV sequence nomenclature. WHO Network for HIV Isolation and Characterization. AIDS Res Hum Retroviruses. 1994 Nov;10(11):1355–1358. doi: 10.1089/aid.1994.10.1355. [DOI] [PubMed] [Google Scholar]
  33. Kostrikis L. G., Bagdades E., Cao Y., Zhang L., Dimitriou D., Ho D. D. Genetic analysis of human immunodeficiency virus type 1 strains from patients in Cyprus: identification of a new subtype designated subtype I. J Virol. 1995 Oct;69(10):6122–6130. doi: 10.1128/jvi.69.10.6122-6130.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Louwagie J., Delwart E. L., Mullins J. I., McCutchan F. E., Eddy G., Burke D. S. Genetic analysis of HIV-1 isolates from Brazil reveals presence of two distinct genetic subtypes. AIDS Res Hum Retroviruses. 1994 May;10(5):561–567. doi: 10.1089/aid.1994.10.561. [DOI] [PubMed] [Google Scholar]
  35. Louwagie J., Janssens W., Mascola J., Heyndrickx L., Hegerich P., van der Groen G., McCutchan F. E., Burke D. S. Genetic diversity of the envelope glycoprotein from human immunodeficiency virus type 1 isolates of African origin. J Virol. 1995 Jan;69(1):263–271. doi: 10.1128/jvi.69.1.263-271.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Louwagie J., McCutchan F. E., Peeters M., Brennan T. P., Sanders-Buell E., Eddy G. A., van der Groen G., Fransen K., Gershy-Damet G. M., Deleys R. Phylogenetic analysis of gag genes from 70 international HIV-1 isolates provides evidence for multiple genotypes. AIDS. 1993 Jun;7(6):769–780. doi: 10.1097/00002030-199306000-00003. [DOI] [PubMed] [Google Scholar]
  37. Mascola J. R., Louwagie J., McCutchan F. E., Fischer C. L., Hegerich P. A., Wagner K. F., Fowler A. K., McNeil J. G., Burke D. S. Two antigenically distinct subtypes of human immunodeficiency virus type 1: viral genotype predicts neutralization serotype. J Infect Dis. 1994 Jan;169(1):48–54. doi: 10.1093/infdis/169.1.48. [DOI] [PubMed] [Google Scholar]
  38. Matthews T. J. Dilemma of neutralization resistance of HIV-1 field isolates and vaccine development. AIDS Res Hum Retroviruses. 1994 Jun;10(6):631–632. doi: 10.1089/aid.1994.10.631. [DOI] [PubMed] [Google Scholar]
  39. McCutchan F. E., Hegerich P. A., Brennan T. P., Phanuphak P., Singharaj P., Jugsudee A., Berman P. W., Gray A. M., Fowler A. K., Burke D. S. Genetic variants of HIV-1 in Thailand. AIDS Res Hum Retroviruses. 1992 Nov;8(11):1887–1895. doi: 10.1089/aid.1992.8.1887. [DOI] [PubMed] [Google Scholar]
  40. Moore J. P., Burkly L. C., Connor R. I., Cao Y., Tizard R., Ho D. D., Fisher R. A. Adaptation of two primary human immunodeficiency virus type 1 isolates to growth in transformed T cell lines correlates with alterations in the responses of their envelope glycoproteins to soluble CD4. AIDS Res Hum Retroviruses. 1993 Jun;9(6):529–539. doi: 10.1089/aid.1993.9.529. [DOI] [PubMed] [Google Scholar]
  41. Moore J. P., Cao Y., Ho D. D., Koup R. A. Development of the anti-gp120 antibody response during seroconversion to human immunodeficiency virus type 1. J Virol. 1994 Aug;68(8):5142–5155. doi: 10.1128/jvi.68.8.5142-5155.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Moore J. P., Cao Y., Qing L., Sattentau Q. J., Pyati J., Koduri R., Robinson J., Barbas C. F., 3rd, Burton D. R., Ho D. D. Primary isolates of human immunodeficiency virus type 1 are relatively resistant to neutralization by monoclonal antibodies to gp120, and their neutralization is not predicted by studies with monomeric gp120. J Virol. 1995 Jan;69(1):101–109. doi: 10.1128/jvi.69.1.101-109.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Moore J. P., Ho D. D. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J Virol. 1993 Feb;67(2):863–875. doi: 10.1128/jvi.67.2.863-875.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Moore J. P., Ho D. D. HIV-1 neutralization: the consequences of viral adaptation to growth on transformed T cells. AIDS. 1995;9 (Suppl A):S117–S136. [PubMed] [Google Scholar]
  45. Moore J. P., McCutchan F. E., Poon S. W., Mascola J., Liu J., Cao Y., Ho D. D. Exploration of antigenic variation in gp120 from clades A through F of human immunodeficiency virus type 1 by using monoclonal antibodies. J Virol. 1994 Dec;68(12):8350–8364. doi: 10.1128/jvi.68.12.8350-8364.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Moore J. P., McKeating J. A., Huang Y. X., Ashkenazi A., Ho D. D. Virions of primary human immunodeficiency virus type 1 isolates resistant to soluble CD4 (sCD4) neutralization differ in sCD4 binding and glycoprotein gp120 retention from sCD4-sensitive isolates. J Virol. 1992 Jan;66(1):235–243. doi: 10.1128/jvi.66.1.235-243.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Moore J. P., Trkola A., Korber B., Boots L. J., Kessler J. A., 2nd, McCutchan F. E., Mascola J., Ho D. D., Robinson J., Conley A. J. A human monoclonal antibody to a complex epitope in the V3 region of gp120 of human immunodeficiency virus type 1 has broad reactivity within and outside clade B. J Virol. 1995 Jan;69(1):122–130. doi: 10.1128/jvi.69.1.122-130.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Morgado M. G., Sabino E. C., Shpaer E. G., Bongertz V., Brigido L., Guimaraes M. D., Castilho E. A., Galvão-Castro B., Mullins J. I., Hendry R. M. V3 region polymorphisms in HIV-1 from Brazil: prevalence of subtype B strains divergent from North American/European prototype and detection of subtype F. AIDS Res Hum Retroviruses. 1994 May;10(5):569–576. doi: 10.1089/aid.1994.10.569. [DOI] [PubMed] [Google Scholar]
  49. Muster T., Guinea R., Trkola A., Purtscher M., Klima A., Steindl F., Palese P., Katinger H. Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS. J Virol. 1994 Jun;68(6):4031–4034. doi: 10.1128/jvi.68.6.4031-4034.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Muster T., Steindl F., Purtscher M., Trkola A., Klima A., Himmler G., Rüker F., Katinger H. A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J Virol. 1993 Nov;67(11):6642–6647. doi: 10.1128/jvi.67.11.6642-6647.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Myers G. Tenth anniversary perspectives on AIDS. HIV: between past and future. AIDS Res Hum Retroviruses. 1994 Nov;10(11):1317–1324. doi: 10.1089/aid.1994.10.1317. [DOI] [PubMed] [Google Scholar]
  52. Nakamura G. R., Byrn R., Rosenthal K., Porter J. P., Hobbs M. R., Riddle L., Eastman D. J., Dowbenko D., Gregory T., Fendly B. M. Monoclonal antibodies to the extracellular domain of HIV-1IIIB gp160 that neutralize infectivity, block binding to CD4, and react with diverse isolates. AIDS Res Hum Retroviruses. 1992 Nov;8(11):1875–1885. doi: 10.1089/aid.1992.8.1875. [DOI] [PubMed] [Google Scholar]
  53. Nkengasong J. N., Janssens W., Heyndrickx L., Fransen K., Ndumbe P. M., Motte J., Leonaers A., Ngolle M., Ayuk J., Piot P. Genotypic subtypes of HIV-1 in Cameroon. AIDS. 1994 Oct;8(10):1405–1412. doi: 10.1097/00002030-199410000-00006. [DOI] [PubMed] [Google Scholar]
  54. O'Brien W. A., Mao S. H., Cao Y., Moore J. P. Macrophage-tropic and T-cell line-adapted chimeric strains of human immunodeficiency virus type 1 differ in their susceptibilities to neutralization by soluble CD4 at different temperatures. J Virol. 1994 Aug;68(8):5264–5269. doi: 10.1128/jvi.68.8.5264-5269.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Olshevsky U., Helseth E., Furman C., Li J., Haseltine W., Sodroski J. Identification of individual human immunodeficiency virus type 1 gp120 amino acids important for CD4 receptor binding. J Virol. 1990 Dec;64(12):5701–5707. doi: 10.1128/jvi.64.12.5701-5707.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Ou C. Y., Takebe Y., Weniger B. G., Luo C. C., Kalish M. L., Auwanit W., Yamazaki S., Gayle H. D., Young N. L., Schochetman G. Independent introduction of two major HIV-1 genotypes into distinct high-risk populations in Thailand. Lancet. 1993 May 8;341(8854):1171–1174. doi: 10.1016/0140-6736(93)91001-3. [DOI] [PubMed] [Google Scholar]
  57. Pau C. P., Kai M., Holloman-Candal D. L., Luo C. C., Kalish M. L., Schochetman G., Byers B., George J. R. Antigenic variation and serotyping of HIV type 1 from four World Health Organization-sponsored HIV vaccine sites. WHO Network for HIV Isolation and Characterization. AIDS Res Hum Retroviruses. 1994 Nov;10(11):1369–1377. doi: 10.1089/aid.1994.10.1369. [DOI] [PubMed] [Google Scholar]
  58. Potts K. E., Kalish M. L., Lott T., Orloff G., Luo C. C., Bernard M. A., Alves C. B., Badaro R., Suleiman J., Ferreira O. Genetic heterogeneity of the V3 region of the HIV-1 envelope glycoprotein in Brazil. Brazilian Collaborative AIDS Research Group. AIDS. 1993 Sep;7(9):1191–1197. doi: 10.1097/00002030-199309000-00007. [DOI] [PubMed] [Google Scholar]
  59. Purtscher M., Trkola A., Gruber G., Buchacher A., Predl R., Steindl F., Tauer C., Berger R., Barrett N., Jungbauer A. A broadly neutralizing human monoclonal antibody against gp41 of human immunodeficiency virus type 1. AIDS Res Hum Retroviruses. 1994 Dec;10(12):1651–1658. doi: 10.1089/aid.1994.10.1651. [DOI] [PubMed] [Google Scholar]
  60. Roben P., Moore J. P., Thali M., Sodroski J., Barbas C. F., 3rd, Burton D. R. Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1. J Virol. 1994 Aug;68(8):4821–4828. doi: 10.1128/jvi.68.8.4821-4828.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Rübsamen-Waigmann H., von Briesen H., Holmes H., Björndal A., Korber B., Esser R., Ranjbar S., Tomlinson P., Galvao-Castro B., Karita E. Standard conditions of virus isolation reveal biological variability of HIV type 1 in different regions of the world. WHO Network for HIV Isolation and Characterization. AIDS Res Hum Retroviruses. 1994 Nov;10(11):1401–1408. doi: 10.1089/aid.1994.10.1401. [DOI] [PubMed] [Google Scholar]
  62. Sattentau Q. J., Moore J. P. Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer. J Exp Med. 1995 Jul 1;182(1):185–196. doi: 10.1084/jem.182.1.185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Sattentau Q. J., Zolla-Pazner S., Poignard P. Epitope exposure on functional, oligomeric HIV-1 gp41 molecules. Virology. 1995 Jan 10;206(1):713–717. doi: 10.1016/s0042-6822(95)80094-8. [DOI] [PubMed] [Google Scholar]
  64. Stamatatos L., Cheng-Mayer C. Structural modulations of the envelope gp120 glycoprotein of human immunodeficiency virus type 1 upon oligomerization and differential V3 loop epitope exposure of isolates displaying distinct tropism upon virion-soluble receptor binding. J Virol. 1995 Oct;69(10):6191–6198. doi: 10.1128/jvi.69.10.6191-6198.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Steimer K. S., Scandella C. J., Skiles P. V., Haigwood N. L. Neutralization of divergent HIV-1 isolates by conformation-dependent human antibodies to Gp120. Science. 1991 Oct 4;254(5028):105–108. doi: 10.1126/science.1718036. [DOI] [PubMed] [Google Scholar]
  66. Sullivan N., Sun Y., Li J., Hofmann W., Sodroski J. Replicative function and neutralization sensitivity of envelope glycoproteins from primary and T-cell line-passaged human immunodeficiency virus type 1 isolates. J Virol. 1995 Jul;69(7):4413–4422. doi: 10.1128/jvi.69.7.4413-4422.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Thali M., Furman C., Ho D. D., Robinson J., Tilley S., Pinter A., Sodroski J. Discontinuous, conserved neutralization epitopes overlapping the CD4-binding region of human immunodeficiency virus type 1 gp120 envelope glycoprotein. J Virol. 1992 Sep;66(9):5635–5641. doi: 10.1128/jvi.66.9.5635-5641.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Thali M., Olshevsky U., Furman C., Gabuzda D., Posner M., Sodroski J. Characterization of a discontinuous human immunodeficiency virus type 1 gp120 epitope recognized by a broadly reactive neutralizing human monoclonal antibody. J Virol. 1991 Nov;65(11):6188–6193. doi: 10.1128/jvi.65.11.6188-6193.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Turner S., Tizard R., DeMarinis J., Pepinsky R. B., Zullo J., Schooley R., Fisher R. Resistance of primary isolates of human immunodeficiency virus type 1 to neutralization by soluble CD4 is not due to lower affinity with the viral envelope glycoprotein gp120. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1335–1339. doi: 10.1073/pnas.89.4.1335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Vanden Haesevelde M., Decourt J. L., De Leys R. J., Vanderborght B., van der Groen G., van Heuverswijn H., Saman E. Genomic cloning and complete sequence analysis of a highly divergent African human immunodeficiency virus isolate. J Virol. 1994 Mar;68(3):1586–1596. doi: 10.1128/jvi.68.3.1586-1596.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Weiss R. A., Clapham P. R., Weber J. N., Dalgleish A. G., Lasky L. A., Berman P. W. Variable and conserved neutralization antigens of human immunodeficiency virus. Nature. 1986 Dec 11;324(6097):572–575. doi: 10.1038/324572a0. [DOI] [PubMed] [Google Scholar]
  72. Wrin T., Loh T. P., Vennari J. C., Schuitemaker H., Nunberg J. H. Adaptation to persistent growth in the H9 cell line renders a primary isolate of human immunodeficiency virus type 1 sensitive to neutralization by vaccine sera. J Virol. 1995 Jan;69(1):39–48. doi: 10.1128/jvi.69.1.39-48.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES