Abstract: Disclosed are modified HCV E2 glycoproteins. Disclosed are modified HCV E2 glycoproteins comprising an antigenic domain D, wherein the modified HCV E2 glycoproteins comprise one or more amino acid alterations in the antigenic domain D, wherein at least one amino acid alteration is a proline substitution. In some aspects, the proline substitution occurs at position 445 based on the amino acid numbering of HCV strain H77. Disclosed are modified HCV E2 glycoproteins comprising an antigenic domain A, wherein the antigenic domain A comprises an N-glycan sequon substitution. In some aspects, the N-glycan sequon substitution results in an Asn-Xaa-Ser or Asn-Xaa-Thr substitution, wherein Xaa is any amino acid except proline. Also disclosed are methods of using the disclosed modified HCV E2 glycoproteins, such as methods of inducing an immune response in a subject, methods of treating a subject, and methods of increasing antigenicity of HCV E2 glycoprotein.

Abstract: The present invention relates to a Yeast Surface Display (YSD) vector for expression of VLR proteins by yeast, wherein the vector includes nucleotide sequences encoding segments of yeast flocculation proteins Flo1p, such as the leader and C-terminal segments, a homologous recombinant cassette and a geneticin/kanamycin resistance gene. The vector can be used for expression of VLR that may be effective in diagnostic applications (e.g., protein chip, immunohistochemistry, flow cytometry), immunoaffinity purification, and for engineering novel fusion proteins.

Abstract: The present invention relates to a Yeast Surface Display (YSD) vector for expression of VLR proteins by yeast, wherein the vector includes nucleotide sequences encoding segments of yeast flocculation proteins FloIp, such as the leader and C-terminal segments, a homologous recombinant cassette and a geneticin/kanamycin resistance gene. The vector can be used for expression of VLR that may be effective in diagnostic applications (e.g., protein chip, immunohistochemistry, flow cytometry), immunoaffinity purification, and for engineering novel fusion proteins.