Delineation of interfaces on human alpha-defensins critical for human adenovirus and human papillomavirus inhibition.
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ABSTRACT: Human α-defensins are potent anti-microbial peptides with the ability to neutralize bacterial and viral targets. Single alanine mutagenesis has been used to identify determinants of anti-bacterial activity and binding to bacterial proteins such as anthrax lethal factor. Similar analyses of α-defensin interactions with non-enveloped viruses are limited. We used a comprehensive set of human α-defensin 5 (HD5) and human neutrophil peptide 1 (HNP1) alanine scan mutants in a combination of binding and neutralization assays with human adenovirus (AdV) and human papillomavirus (HPV). We have identified a core of critical hydrophobic residues that are common determinants for all of the virus-defensin interactions that were analyzed, while specificity in viral recognition is conferred by specific s
SUBMITTER: Tenge VR
PROVIDER: S-EPMC4154873 | biostudies-literature | 2014 Sep
REPOSITORIES: biostudies-literature
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