Unexpected Altered Specificity Is Responsible for St. Louis Encephalitis Virus Recombinant Protease Autoproteolysis

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We report herein the study of the cleavage fragments generated by autoproteolysis of the St. Louis encephalitis virus recombinant protease. The cleavage sites leading to truncated forms were identified by microsequencing, which revealed an unexpected altered specificity of the recombinant proteinase towards unusual sequences.

Keywords: Altered specificity; NS3; autoproteolysis; flavivirin; trypsin-like serine protease

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986607779117146

Affiliations: Unite de virologie tropicale, IMTSSA, BP 46, 13 998 Marseille armees, France.

Publication date: January 1, 2007

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.



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