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

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.

journal_name

Mol Biochem Parasitol

authors

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

doi

10.1016/j.molbiopara.2012.06.003

subject

Has Abstract

pub_date

2012-09-01 00:00:00

pages

66-9

issue

1

eissn

0166-6851

issn

1872-9428

pii

S0166-6851(12)00175-2

journal_volume

185

pub_type

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