Interleukin-8-like activity in a filarial asparaginyl-tRNA synthetase. Mol Biochem Parasitol 2012 Sep;185(1):66-9
Date
06/20/2012Pubmed ID
22710390DOI
10.1016/j.molbiopara.2012.06.003Scopus ID
2-s2.0-84864277999 (requires institutional sign-in at Scopus site) 19 CitationsAbstract
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 LAAuthor
Michael Kron MD Director, Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
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
