Exposure of HIV-1 gp41 transmembrane protein epitopes on the surface of hepatitis B core antigen capsids

R. Ulrich, G. P. Borisova, R. Möhring, I. Latzsch, V. P. Ose, I. G. Berzins, D. E. Dreilina, P. M. Pushko, V. V. Tsibinogin, P. P. Pumpen, H. A. Rosenthal, E. J. Gren

Institut für medizinische Virologie, Bereich Medizin der Humboldt-Universitat (Charite), Berlin, DDR; Department of Molecular Biology, Institute of Organic Synthesis, Latvian Academy of Sciences, Riga; A. Kirhenstein Institute of Microbiology, Latvian Academy of Sciences, Riga; Experimental Plant, Institute of Organic Synthesis, Riga

Abstract: Insertion of 52 amino acid sequence of transmembrane protein gp41 of human immunodeficiency virus 1 (HIV-1), (amino acid residues 78 to 129 of gp41 or 596 to 647 of Env), at the Pro¹⁴⁴ position of the hepatitis B core antigen (HBcAg) leads to the formation of chimeric capsids which retain morphology of intact HBcAg but expose on their outer surface major HIV-1 epitopes localised in the inserted gp41 fragment. Antigenicity of inserted gp41 epitopes within chimeric capsids remains undisturbed. The localization of gp41 epitopes on the capsids does not depend on the presence or absence of the argi-nine-rich 39 amino acid C-terminus of HBcAg.

Russian Journal of Bioorganic Chemistry 1990, 16 (9):1283-1286

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