Abstract
A protein from baculovirus-infected cells reacted with an antibody against the smooth muscle protein telokin. Because of this unusual similarity, the protein, termed telokin-like protein-20 (TLP20), was isolated and characterized. Its M(r) on denaturing polyacrylamide gels was 28K and the protein contained a high proportion of β structure. A cDNA for TLP20 was isolated and sequenced. The 3' non-coding sequence contained a region of high identity with the 5' end of two other baculovirus genes. The 5' non-coding region contains several baculovirus regulatory elements. Surprisingly, the derived amino acid sequence showed no homologies to telokin. The cDNA was cloned into a bacterial expression vector and the subsequently expressed protein had a slightly lower M(r) than the native protein, but cross-reacted with telokin antibody. This paper reports the characterization of a new baculovirus protein that shares some antigenic similarities to the smooth muscle protein telokin.
Original language | English (US) |
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Pages (from-to) | 1807-1809 |
Number of pages | 3 |
Journal | Journal of General Virology |
Volume | 75 |
Issue number | 7 |
DOIs | |
State | Published - 1994 |
ASJC Scopus subject areas
- Virology