Abstract:
:AWAP IV constitutes the C-terminal domain of the larger 81 kDa protein AWAK [Avian WAP (whey acidic protein) domain- and Kunitz domain-containing], which is predicted, through conserved domain database searching, to contain at least four WAP domains and one Kunitz domain. RT (reverse transcription)-PCR analyses revealed mRNA transcripts encoding AWAP IV in the small intestinal and kidney tissues of 5-day-old Salmonella-infected chicks. Time-kill antimicrobial assays using rAWAP IV (recombinant AWAP IV) cell lysate indicated antimicrobial activity against gram-positive and gram-negative bacteria including Salmonella, Streptococcus and Staphylococcus spp. In addition, permeabilization of the outer membrane of Salmonella, as shown by the NPN (N-phenyl-1-naphthylamine) fluorescent probe assay, supported the ability of rAWAP IV to disrupt prokaryotic membranes. WAP domains can function as inhibitors of serine protease activity, and the microbial serine proteases subtilisin and proteinase K were inhibited by rAWAP IV cell lysate. However, at comparable concentrations, no significant inhibition of the mammalian serine protease elastase was observed. The combined broad-spectrum antibacterial and anti-protease activities of AWAP IV suggest a novel role in the avian innate defence mechanisms operating against microbial infection.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Townes CL,Milona P,Hall Jdoi
10.1042/BST20060267keywords:
subject
Has Abstractpub_date
2006-04-01 00:00:00pages
267-9issue
Pt 2eissn
0300-5127issn
1470-8752pii
BST20060267journal_volume
34pub_type
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