Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2009-6-8
pubmed:abstractText
In this work, we study the consequences of sequence variations of the "2009 H1N1" (swine or Mexican flu) influenza A virus strain neuraminidase for drug treatment and vaccination. We find that it is phylogenetically more closely related to European H1N1 swine flu and H5N1 avian flu rather than to the H1N1 counterparts in the Americas. Homology-based 3D structure modeling reveals that the novel mutations are preferentially located at the protein surface and do not interfere with the active site. The latter is the binding cavity for 3 currently used neuraminidase inhibitors: oseltamivir (Tamiflu), zanamivir (Relenza) and peramivir; thus, the drugs should remain effective for treatment. However, the antigenic regions of the neuraminidase relevant for vaccine development, serological typing and passive antibody treatment can differ from those of previous strains and already vary among patients. REVIEWERS: This article was reviewed by Sandor Pongor and L. Aravind.
pubmed:commentsCorrections
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pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1745-6150
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18; discussion 18
pubmed:dateRevised
2011-8-1
pubmed:meshHeading
pubmed-meshheading:19457254-Amino Acid Sequence, pubmed-meshheading:19457254-Antibodies, Viral, pubmed-meshheading:19457254-Antiviral Agents, pubmed-meshheading:19457254-Binding Sites, pubmed-meshheading:19457254-Conserved Sequence, pubmed-meshheading:19457254-Genetic Variation, pubmed-meshheading:19457254-Humans, pubmed-meshheading:19457254-Influenza A Virus, H1N1 Subtype, pubmed-meshheading:19457254-Models, Molecular, pubmed-meshheading:19457254-Molecular Sequence Data, pubmed-meshheading:19457254-Mutation, pubmed-meshheading:19457254-Neuraminidase, pubmed-meshheading:19457254-Phylogeny, pubmed-meshheading:19457254-Protein Processing, Post-Translational, pubmed-meshheading:19457254-Protein Structure, Tertiary, pubmed-meshheading:19457254-Sequence Alignment, pubmed-meshheading:19457254-Sequence Analysis, Protein, pubmed-meshheading:19457254-Surface Properties
pubmed:year
2009
pubmed:articleTitle
Mapping the sequence mutations of the 2009 H1N1 influenza A virus neuraminidase relative to drug and antibody binding sites.
pubmed:affiliation
Biomolecular Function Discovery Division, Bioinformatics Institute (BII), Agency for Science Technology and Research (A*STAR), Singapore. sebastianms@bii.a-star.edu.sg
pubmed:publicationType
Journal Article