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Arch Virol 2006 Sep;151(9):1841-51

The rubella virus nonstructural protease recognizes itself via an internal sequence present upstream of the cleavage site for trans-activity.

Chen HH, Stark CJ, Atreya CD

Atreya CD, US FDA, Ctr Biol Evaluat & Res, Div Viral Prod, HFM-460,Bldg 29A,2C-11 NIH Campus,8800 Rockville, Bethesda, MD 20892 USA US FDA, Ctr Biol Evaluat & Res, Div Viral Prod, Bethesda, MD 20892 USA

Abstract

The substrate requirement for rubella virus protease trans-activity is unknown. Here, we analyzed the cleavability of RV P200-derived substrates varying in their N-terminal lengths (72-475 amino acids) from the cleavage site by the RV protease trans-activity. Only substrates with at least 309 amino acid residues N-terminal to the cleavage site were able to undergo cleavage. Further, rubella sequence was found to be necessary in the N-terminal region of the substrate, whereas a heterologous sequence C-terminal to the cleavage site was tolerated. These results demonstrated a requirement for residues located between amino acids 994-1102 of the RV P200 polyprotein, besides its cleavage site for RV protease trans-activity. This region overlaps with the starting site of the essential cis-protease activity of RV P200 polyprotein. This is a novel observation for a viral protease of the family Togaviridae.


Category: Journal Article
PubMed ID: #16570206
Includes FDA Authors from Scientific Area(s): Biologics
Entry Created: 2011-10-04 Entry Last Modified: 2012-08-29
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