Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the human immunodeficiency virus type 1 envelope glycoprotein - PubMed (original) (raw)

Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the human immunodeficiency virus type 1 envelope glycoprotein

M K Gorny et al. Proc Natl Acad Sci U S A. 1991.

Abstract

Cell lines secreting IgG1 human monoclonal antibodies (mAb) to the envelope glycoprotein, gp120, of human immunodeficiency virus (HIV) have been produced by transformation of peripheral blood cells from HIV-infected individuals and by fusion of transformed cells to a human-mouse heteromyeloma cell line (SHM-D33). Two human mAbs were site-selected by means of a 23-mer synthetic peptide spanning a portion of the third variable domain of gp120 from the MN strain of HIV. The two heterohybridomas produce three times more IgG than do their parent lymphoblastoid cell lines. The specificities of these mAbs have been mapped to sequences near the tip of the disulfide loop of the gp120 third variable domain, Lys-Arg-Ile-His-Ile and His-Ile-Gly-Pro-Gly-Arg, respectively. The mAbs have dissociation constants of 3.7 x 10(-6) M and 8.3 x 10(-7) M, neutralize HIVMN in vitro at nanogram levels, and bear the characteristics of antibodies associated with protective immunity in vivo.

PubMed Disclaimer

Cited by

Two immunodominant domains of gp41 bind antibodies which enhance human immunodeficiency virus type 1 infection in vitro.
Robinson WE Jr, Gorny MK, Xu JY, Mitchell WM, Zolla-Pazner S. Robinson WE Jr, et al. J Virol. 1991 Aug;65(8):4169-76. doi: 10.1128/JVI.65.8.4169-4176.1991. J Virol. 1991. PMID: 2072448 Free PMC article.
Molecular characterization of five human anti-human immunodeficiency virus type 1 antibody heavy chains reveals extensive somatic mutation typical of an antigen-driven immune response.
Andris JS, Johnson S, Zolla-Pazner S, Capra JD. Andris JS, et al. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7783-7. doi: 10.1073/pnas.88.17.7783. Proc Natl Acad Sci U S A. 1991. PMID: 1909030 Free PMC article.
Toward effective HIV vaccination: induction of binary epitope reactive antibodies with broad HIV neutralizing activity.
Nishiyama Y, Planque S, Mitsuda Y, Nitti G, Taguchi H, Jin L, Symersky J, Boivin S, Sienczyk M, Salas M, Hanson CV, Paul S. Nishiyama Y, et al. J Biol Chem. 2009 Oct 30;284(44):30627-42. doi: 10.1074/jbc.M109.032185. Epub 2009 Sep 2. J Biol Chem. 2009. PMID: 19726674 Free PMC article.
Preferential use of the VH5-51 gene segment by the human immune response to code for antibodies against the V3 domain of HIV-1.
Gorny MK, Wang XH, Williams C, Volsky B, Revesz K, Witover B, Burda S, Urbanski M, Nyambi P, Krachmarov C, Pinter A, Zolla-Pazner S, Nadas A. Gorny MK, et al. Mol Immunol. 2009 Feb;46(5):917-26. doi: 10.1016/j.molimm.2008.09.005. Epub 2008 Oct 25. Mol Immunol. 2009. PMID: 18952295 Free PMC article.
Design of HIV Coreceptor Derived Peptides That Inhibit Viral Entry at Submicromolar Concentrations.
Bobyk KD, Mandadapu SR, Lohith K, Guzzo C, Bhargava A, Lusso P, Bewley CA. Bobyk KD, et al. Mol Pharm. 2017 Aug 7;14(8):2681-2689. doi: 10.1021/acs.molpharmaceut.7b00155. Epub 2017 Jul 13. Mol Pharm. 2017. PMID: 28494151 Free PMC article.

References

1. J Virol. 1987 Jun;61(6):2024-8 - PubMed
1. Proc Natl Acad Sci U S A. 1988 Dec;85(23):9234-7 - PubMed
1. J Virol. 1987 Oct;61(10):2956-61 - PubMed
1. Mol Immunol. 1987 Jun;24(6):569-76 - PubMed
1. J Immunol. 1987 Dec 15;139(12):4027-33 - PubMed

Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the human immunodeficiency virus type 1 envelope glycoprotein - PubMed (original) (raw)