A modified polypeptide corresponding to an envelope glycoprotein of a primate lentivirus is described. The polypeptide has been modified from the wild-type structure so that it has cysteine amino acid residues introduced to create disulfide bonds, a cavity is filled with hydrophobic amino acids, a Proresidue is introduced at a defined turn structure of the protein, or the hydrophobicity is increased across the interface between different domains, while retaining the overall 3-dimensional structure of a discontinuous conserved epitope of the wild-type protein. Preferably, the polypeptide has more than one of those characteristics. Preferably, the primate lentivirus is HIV, and the protein is HIV-1 gp120.

 
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< Stimulation of hematopoiesis by ex vivo activated immune cells

< Combination antiviral and interleukin-2 therapy for HIV infection

> Preparation and standardization of immunomodulatory peptide-linked glucans with verifiable oral absorbability from coriolus versicolor

> Diagnostic methods based on human BTG-2 and BTG-3 polypeptides

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