Policy: Adaptations of avian flu virus are a cause for concern.

US National Science Advisory Board for Biosecurity, USA.
Nature (Impact Factor: 38.6). 02/2012; 482(7384):153-4. DOI: 10.1038/482153a
Source: PubMed

ABSTRACT Members of the US National Science Advisory Board for Biosecurity
explain its recommendations on the communication of experimental work on
H5N1 influenza.

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    ABSTRACT: In recent time there has been ample discussion concerning censorship of research conducted in two labs involved in avian influenza virus research. Much of the debate has centered on the question whether the methods and results should reach to open disclosure given the "dual use" nature of this research which can be used for nefarious purposes. This paper reviews the discussion to date but centers on epistemological issues associated with initial justification of this research and what this entails for continuation of this research despite US governmental biosecurity concerns. The question here is whether there was reasonable moral warrant for genetic alteration of the H5N1 influenza virus. The paper concludes with philosophical (ethical) justification for continuation of this research.
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    Frontiers in Bioengineering and Biotechnology 01/2014; 2:35.
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    ABSTRACT: Highly pathogenic avian influenza A virus H5N1 continues to spread among poultry and has frequently broken the species barrier to humans. Recent studies have shown that a laboratory-mutated or reassortant H5N1 virus bearing hemagglutinin (HA) with as few as four or five mutations was capable of transmitting more efficiently via respiratory droplets between ferrets, posing a serious threat to public health and underscoring the priority of effective vaccines and therapeutics. In this study, we identified a novel monoclonal antibody (mAb) named HAb21, that has a broadly neutralizing activity against all tested strains of H5N1 covering clades 0, 1, 2.2, 2.3.4, and Importantly, HAb21 efficiently neutralized diverse H5N1 variants with single or combination forms of mutations capable of airborne transmission. We demonstrated that HAb21 blocked viral entry during the receptor-binding step by targeting a previously uncharacterized epitope at the tip of the HA head. This novel epitope closely neighbors the receptor-binding site (RBS) and the interface of HA trimer and is highly conserved among divergent H5N1 strains. Our studies provide a new tool for use either for therapeutic purposes or as a basis of vaccine development.
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