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Characterization and selectivity of catalytic antibodies from human serum with RNase activity

IgG purified from sera of several patients with systemic lupus erythematosus and hepatitis B are shown to present RNA hydrolyzing activities that are different from the weak RNase A-type activities found in the sera of healthy donors. Further investigation brings evidence for two intrinsic activitie...

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Bibliographic Details
Published in:Nucleic acids research 1998-12, Vol.26 (23), p.5243-5250
Main Authors: Vlassov, Alexander, Florentz, Catherine, Helm, Mark, Naumov, Valerii, Buneva, Valentina, Nevinsky, Georgy, Giegé, Richard
Format: Article
Language:English
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Summary:IgG purified from sera of several patients with systemic lupus erythematosus and hepatitis B are shown to present RNA hydrolyzing activities that are different from the weak RNase A-type activities found in the sera of healthy donors. Further investigation brings evidence for two intrinsic activities, one observed in low salt conditions and another specifically stimulated by Mg2+ ions and distinguishable from human sera RNases. Cleavage of RNA substrates by the latter activity is not sequence-specific but sensitive to both subtle conformational and/or drastic folding changes, as evidenced by comparative analysis of couples of structurally well-studied RNA substrates. These include yeast tRNAAsp and its in vitro transcript and human mitochondrial tRNALys-derived in vitro transcripts. The discovery of catalytic antibodies with RNase activities is a first step towards creation of a new generation of tools for the investigation of RNA structure.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/26.23.5243