Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9289380 | Virus Research | 2005 | 16 Pages |
Abstract
Both full-length and subgenomic negative-strand RNAs are initiated at the 3â² terminus of the positive-strand genomic RNA of the arterivirus, simian hemorrhagic fever virus (SHFV). The SHFV 3â²(+) non-coding region (NCR) is 76 nts in length and forms a stem loop (SL) structure that was confirmed by ribonuclease structure probing. Two cell proteins, p56 and p42, bound specifically to a probe consisting of the SHFV 3â²(+)NCR RNA. The 3â²(+)NCR RNAs of two additional members of the arterivirus genus specifically interacted with two cell proteins of the same size. p56 was identified as polypyrimidine tract-binding protein (PTB) and p42 was identified as fructose bisphosphate aldolase A. PTB binding sites were mapped to a terminal loop and to a bulged region of the SHFV 3â²SL structure. Deletion of either of the PTB binding sites in the viral RNA significantly reduced PTB binding activity, suggesting that both sites are required for efficient binding of this protein. Changes in the top portion of the SHFV 3â²SL structure eliminated aldolase binding, suggesting that the binding site for this protein is located near the top of the SL. These cell proteins may play roles in regulating the functions of the genomic 3â² NCR.
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Virology
Authors
Taronna R. Maines, Mary Young, Nikita Nhu-Nguyen Dinh, Margo A. Brinton,