Characterization of a murine monoclonal antibody to the transmembrane glycoprotein of human immunodeficiency virus type 2.

Important note: Information in this article was accurate in 1992. The state of the art may have changed since the publication date.

Characterization of a murine monoclonal antibody to the transmembrane glycoprotein of human immunodeficiency virus type 2.

Abstr Annu Meet Am Soc Microbiol. 1991 May 5-9;91:336 (abstract no. T-16). Unique Identifier : AIDSLINE ASM91/0290292
Granade T; Parekh B; Phillips S; Pau C; George JR; Centers for Disease Control, Atlanta, GA.

Abstract: Monoclonal antibodies (MAB) were developed to study the viral proteins of human immunodeficiency virus type 2 (HIV-2). Mabs were produced with standard techniques using whole viral lysate as immunogens. One MAB (1H5) displayed strong reactivity to the transmembrane glycoprotein gp41 by EIA and by Western blot analysis. Mapping of the antibody binding site was preformed using synthetic peptides in direct capture and competition based EIAs and was identified as the immunodominant region of the gp41 (amino acids 592-603). The 1H5 MAB recognized truncated glycoprotein (gp36) and bound to all five HIV-2 viral isolates tested. The 1H5 identified trimeric forms of gp41 and gp36 in HIV-2 Western blots but no dimers or tetramers of these glycoproteins were detected. The 1H5 MAB may prove useful in studying additional strains of HIV-2 and in establishing appropriate HIV-2 Western blot criteria.

Keywords: Animal Antibodies, Monoclonal/*IMMUNOLOGY Blotting, Western Enzyme-Linked Immunosorbent Assay Gene Products, env/*IMMUNOLOGY HIV Envelope Protein gp41/IMMUNOLOGY HIV-2/*IMMUNOLOGY Mice ABSTRACT
920830
M9281054

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