Abstract
Interactions among the three adenovirus core polypeptides V, VII, and μ were examined, using the reversible chemical cross-linker dithiobis(succinimidyl propionate) and two-dimensional polyacrylamide gel electrophoresis. Cross-linked species obtained from gradient-purified adenovirus type 2 cores were well represented among the cross-linked products of pentonless virions and crude core preparations. The more efficiently formed cross-linked core species were also identified with the arginine-specific cross-linker, p-azidophenyl glyoxal. In addition to dimers of polypeptides V and VII, efficient cross-linking of V to VII, V to μ, and VII to V to μ was detected in adenovirus cores. Notably absent were cross-linked species corresponding to higher multimers of polypeptide VII. A major core-capsid interaction appeared to be via the association of polypeptide V with a dimer of polypeptide VI.
Original language | English (US) |
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Pages (from-to) | 379-386 |
Number of pages | 8 |
Journal | Journal of virology |
Volume | 55 |
Issue number | 2 |
DOIs | |
State | Published - 1985 |
All Science Journal Classification (ASJC) codes
- Microbiology
- Immunology
- Insect Science
- Virology