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) |
|---|---|
| Pages (from-to) | 1807-1809 |
| Number of pages | 3 |
| Journal | Journal of General Virology |
| Volume | 75 |
| Issue number | 7 |
| State | Published - 1994 |
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ASJC Scopus subject areas
- Immunology
- Virology
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Sequence and expression of a baculovirus protein with antigenic similarity to telokin. / Raynes, D. A.; Hartshorne, D. J.; Guerriero, Vincent.
In: Journal of General Virology, Vol. 75, No. 7, 1994, p. 1807-1809.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Sequence and expression of a baculovirus protein with antigenic similarity to telokin
AU - Raynes, D. A.
AU - Hartshorne, D. J.
AU - Guerriero, Vincent
PY - 1994
Y1 - 1994
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0028336814&partnerID=8YFLogxK
M3 - Article
C2 - 7517434
AN - SCOPUS:0028336814
VL - 75
SP - 1807
EP - 1809
JO - Journal of General Virology
JF - Journal of General Virology
SN - 0022-1317
IS - 7
ER -