Attachment of an oligopeptide epitope to the C-terminus of recombinant SIV gp160 facilitates the construction of SMAA complexes while preserving CD4 binding
| Autor: | C. Doyle, Tomáš Hanke, Richard E. Randall, Ian M. Jones, D. F. Young |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Glycosylation
medicine.medical_treatment Recombinant Fusion Proteins viruses Antigen-Antibody Complex Biology complex mixtures Epitope law.invention chemistry.chemical_compound Epitopes law Virology medicine Animals Furin chemistry.chemical_classification Oligopeptide Protease C-terminus Gene Products env Amino acid Biochemistry chemistry CD4 Antigens Recombinant DNA biology.protein Baculoviridae Oligopeptides Protein Processing Post-Translational Protein Binding |
| DOI: | 10.1016/0166-0934(95)00003-d |
| Popis: | A small 14 amino acid oligopeptide tag (termed SV5-Pk) was fused onto the carboxy-terminus of simian immunodeficiency virus gp160 expressed from a recombinant baculovirus. The presence of the Pk tag had no obvious effect on the expression and glycosylation of gp160 and did not interfere either with CD4 binding or with cleavage at its maturation site by the protease furin. The presence of the Pk tag did, however, facilitate the simplified purification of full-length gp160 and its incorporation into immunogenic solid matrix-antibody-antigen (SMAA) complexes. |
| Databáze: | OpenAIRE |
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