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HIV-1 consensus envelope-induced broadly binding antibodies.

HIV-1 consensus envelope-induced broadly binding antibodies.
Author Information (click to view)

Meyerhoff RR, Scearce RM, Ogburn DF, Lockwood B, Pickeral J, Kuraoka M, Anasti K, Eudailey J, Eaton A, Cooper M, Wiehe K, Montefiori DC, Tomaras GD, Ferrari G, Alam SM, Liao HX, Korber B, Gao F, Haynes BF,


Meyerhoff RR, Scearce RM, Ogburn DF, Lockwood B, Pickeral J, Kuraoka M, Anasti K, Eudailey J, Eaton A, Cooper M, Wiehe K, Montefiori DC, Tomaras GD, Ferrari G, Alam SM, Liao HX, Korber B, Gao F, Haynes BF, (click to view)

Meyerhoff RR, Scearce RM, Ogburn DF, Lockwood B, Pickeral J, Kuraoka M, Anasti K, Eudailey J, Eaton A, Cooper M, Wiehe K, Montefiori DC, Tomaras GD, Ferrari G, Alam SM, Liao HX, Korber B, Gao F, Haynes BF,

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AIDS research and human retroviruses 2017 03 17() doi 10.1089/AID.2016.0294

Abstract

Antibodies that cross-react with multiple HIV-1 envelopes (Envs) are useful reagents for characterizing Env proteins and for soluble Env capture and purification assays. We previously reported ten murine monoclonal antibodies induced by group M consensus Env, CON-6 immunization. Each demonstrated broad cross-reactivity to recombinant Envs. Here we characterized the Env epitopes to which they bind. Seven mapped to linear epitopes in gp120, five at the Env N-terminus and two at the Env C-terminus. One antibody, 13D7, bound at the gp120 N-terminus (aa 30-42), reacted with HIV-1-infected CD4+ T cells, and when expressed in a human IgG1 backbone, mediated ADCC. Antibody 18F11 bound at the gp120 C-terminus (aa 445-459) and reactivity was glycan-dependent. Antibodies 13D7, 3B3, and 16H3 bound to 100 percent of HIV-1 Envs tested in ELISA and SDS-PAGE/Western blot analysis. These data define the epitopes of monoclonal antibody reagents for characterization of recombinant Envs, one epitope of which is also expressed on the surface of HIV-1 infected CD4+ T cells.

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