Probing the ability of the coat and vertex protein of the membrane-containing bacteriophage PRD1 to display a meningococcal epitope
| Autor: | Jaana K. H. Bamford, Dennis H. Bamford, Liisa Laakkonen, Juha T. Huiskonen, Matti Sarvas, Maija Toropainen |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Vesicle-associated membrane protein 8
Phage display Capsid protein Recombinant Fusion Proteins Protein subunit Genetic Vectors Porins Neisseria meningitidis Serogroup B Biology Virus Replication Epitope Virus PRD1 Epitopes 03 medical and health sciences Capsid Virology Escherichia coli Bacteriophage PRD1 Amino Acid Sequence Meningococcal epitope 030304 developmental biology Vaccines Synthetic 0303 health sciences 030302 biochemistry & molecular biology Molecular biology Protein tertiary structure 3. Good health Cell biology Mutagenesis Insertional Capsid Proteins Vertex protein Bacterial outer membrane |
| Zdroj: | Virology. 310:267-279 |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/s0042-6822(03)00171-5 |
| Popis: | Bacteriophage PRD1 is an icosahedral dsDNA virus with a diameter of 740 Å and an outer protein shell composed of 720 copies of major coat protein P3. Spike complexes at the vertices are composed of a pentameric base (protein P31) and a spike structure (proteins P5 and P2) where the N-terminal region of the trimeric P5 is associated with the base and the C-terminal region of P5 is associated with receptor-binding protein P2. The functionality of proteins P3 and P5 was investigated using insertions and deletions. It was observed that P3 did not tolerate changes whereas P5 tolerated changes much more freely. These properties support the hypothesis that viruses have core structures and functions, which remain stable over time, as well as other elements, responsible for host interactions, which are evolutionally more fluid. The insertional probe used was the apex of exposed loop 4 of group B meningococcal outer membrane protein PorA, a medically important subunit vaccine candidate. It was demonstrated that the epitope could be displayed on the virus surface as part of spike protein P5. |
| Databáze: | OpenAIRE |
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