Size and position of truncations in the carboxy-terminal region of major capsid protein VP1 of hamster polyomavirus expressed in yeast determine its assembly capacity

The hamster polyomavirus major capsid protein VP1 was modified in its carboxy-terminal region by consecutive truncations and single amino acid exchanges. The ability of yeast-expressed VP1 variants to form virus-like particles (VLPs) strongly depended on the size and position of the truncation. VP1...

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Bibliographic Details
Published in:Archives of virology 2006-09, Vol.151 (9), p.1811-1825
Main Authors: Gedvilaite, A, Aleksaite, E, Staniulis, J, Ulrich, R, Sasnauskas, K
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Biological and medical sciences
Capsid Proteins - chemistry
Capsid Proteins - genetics
Capsid Proteins - metabolism
Cloning
Codon, Nonsense
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Microbiology
Microscopy, Electron, Transmission
Miscellaneous
Models, Molecular
Molecular Sequence Data
Mutation
Plasmids
Polyomavirus - genetics
Polyomavirus - physiology
Protein Structure, Tertiary
Proteins
Recombinant Proteins - metabolism
Saccharomyces cerevisiae - genetics
Sequence Deletion
Virology
Virosomes - metabolism
Virosomes - ultrastructure
Virus Assembly
Yeast
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Summary:The hamster polyomavirus major capsid protein VP1 was modified in its carboxy-terminal region by consecutive truncations and single amino acid exchanges. The ability of yeast-expressed VP1 variants to form virus-like particles (VLPs) strongly depended on the size and position of the truncation. VP1 variants lacking 21, 69, and 79 amino acid (aa) residues in their carboxy-terminal region efficiently formed VLPs similar to those formed by the unmodified VP1 (diameter 40-45 nm). In contrast, VP1 derivatives with carboxy-terminal truncations of 35 to 56 aa residues failed to form VLPs. VP1 mutants with a single A336G aa exchange or internal deletions of aa 335 to aa 346 and aa 335 to aa 363 resulted in the formation of VLPs of a smaller size (diameter 20 nm). These data indicate that certain parts of the carboxy-terminal region of VP1 are not essential for pentamer-pentamer interactions in the capsid, at least in the yeast expression system used.
ISSN:0304-8608
1432-8798
DOI:10.1007/s00705-006-0745-8