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The novel avian protein, AWAK, contains multiple domains with homology to protease inhibitory modules

Lookup NU author(s): Dr Christopher NileORCiD, Dr Claire Townes, Emeritus Professor Barry Hirst, Dr Judith Hall

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Abstract

We report the purification of a 3.5 kDa peptide with antimicrobial activity from the mucosa and epithelial cells of chicken intestine. The peptide contains a pattern of cysteines characteristic of a whey acidic protein (WAP) domain and was identified as the carboxy terminal fragment of a novel 767 amino acid avian protein which has a proposed molecular weight of 81 kDa. Using the conserved domain database (CDD) we identified this 81 kDa protein to contain multiple amino acid motifs with homology to WAP domains and an amino acid motif with homology to a Kunitz proteinase inhibitor domain. We propose to call this avian protein AWAK (Avian WAP motif containing, Kunitz domain containing). The presence of WAP and Kunitz modules suggests that AWAK has proteinase inhibitor activity. RT-PCR analyses demonstrated expression of the AWAK gene in the chicken intestine. © 2005 Elsevier Ltd. All rights reserved.


Publication metadata

Author(s): Nile CJ, Townes CL, Hirst BH, Hall J

Publication type: Article

Publication status: Published

Journal: Molecular Immunology

Year: 2006

Volume: 43

Issue: 4

Pages: 388-394

ISSN (print): 0161-5890

ISSN (electronic): 1872-9142

Publisher: Pergamon

URL: http://dx.doi.org/10.1016/j.molimm.2005.02.015

DOI: 10.1016/j.molimm.2005.02.015

PubMed id: 16310052


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