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Mol Biochem Parasitol. 2012 Sep;185(1):66-9. doi: 10.1016/j.molbiopara.2012.06.003. Epub 2012 Jun 16.

Interleukin-8-like activity in a filarial asparaginyl-tRNA synthetase.

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Department of Medicine, Biotechnology and Bioengineering Center, Medical College of Wisconsin, Milwaukee, WI 53092, USA.


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.

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