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Human anti-asparaginyl-tRNA synthetase autoantibodies (anti-KS) increase the affinity of the enzyme for its tRNA substrate. FEBS Lett 2001 Apr 13;494(3):170-4

Date

04/20/2001

Pubmed ID

11311235

DOI

10.1016/s0014-5793(01)02340-7

Abstract

Autoantibodies directed against specific human aminoacyl-tRNA synthetases have been associated with a clinical picture including myositis, arthritis, interstitial lung disease and other features that has been referred to as the "anti-synthetase syndrome". Anti-asparaginyl-tRNA synthetase autoantibodies (anti-KS), the most recently described anti-synthetase autoantibodies, are directed against human cytosolic asparaginyl-tRNA synthetase and neutralize specifically its activity. Here we show that these antibodies recognize two epitopes on the human enzyme, an N-terminal epitope reactive in immunoblot experiments and a heat-labile epitope in the catalytic domain. In contrast to the well studied anti-Jo-1 autoantibodies anti-KS when bound to the synthetase increase the affinity of the synthetase for its tRNA substrate and prevent aminoacylation without interfering with the amino acid activation step.

Author List

Beaulande M, Kron M, Hirakata M, Härtlein M

Author

Michael Kron MD Director, Professor in the Medicine department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Acylation
Amino Acyl-tRNA Synthetases
Antibody Specificity
Aspartate-tRNA Ligase
Autoantibodies
Binding, Competitive
Catalytic Domain
Epitope Mapping
Epitopes
Humans
Immune Sera
Molecular Sequence Data
Mutation
Neutralization Tests
RNA, Transfer, Amino Acyl
RNA, Transfer, Asp
Recombinant Proteins
jenkins-FCD Prod-388 89e904233d719332173309c68ab82b0b2a78a3a7