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Interleukin-8-like activity in a filarial asparaginyl-tRNA synthetase. Mol Biochem Parasitol 2012 Sep;185(1):66-9

Date

06/20/2012

Pubmed ID

22710390

DOI

10.1016/j.molbiopara.2012.06.003

Abstract

A wide range of secondary biological functions have been documented for eukaryotic aminoacyl-tRNA synthetases including roles in transcriptional regulation, mitochondrial RNA splicing, cell growth, and chemokine-like activities. The asparaginyl-tRNA synthetase (AsnRS) of the filarial nematode, Brugia malayi, is a highly expressed excretory-secretory molecule which activates interleukin 8 (IL-8) receptors via extracellular domains that are different from those used by IL-8. Recent success in determining the complete atomic structure of the B. malayi AsnRS provided the opportunity to map its chemokine-like activity. Chemotaxis assays demonstrated that IL-8-like activity is localized in a novel 80 amino acid amino terminal substructure. Structural homology searches revealed similarities between that domain in B. malayi AsnRS and substructures involved in receptor binding by human IL-8. These observations provide important new insights into how parasite-derived molecules may play a role in the modulation of immune cell function.

Author List

Kron MA, Wang C, Vodanovic-Jankovic S, Howard OM, Kuhn LA

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

Amino Acid Sequence
Animals
Aspartate-tRNA Ligase
Brugia malayi
Chemotaxis
Computational Biology
Enzyme Activation
Helminth Proteins
Humans
Immunologic Factors
Interleukin-8
Molecular Sequence Data
Neutrophils
Protein Structure, Tertiary
RNA, Transfer, Amino Acyl
Receptors, Interleukin-8
Sequence Homology, Amino Acid
jenkins-FCD Prod-388 89e904233d719332173309c68ab82b0b2a78a3a7