Please use this identifier to cite or link to this item: https://doi.org/10.1186/1745-6150-4-18
Title: Mapping the sequence mutations of the 2009 H1N1 influenza A virus neuraminidase relative to drug and antibody binding sites
Authors: Maurer-Stroh, S 
Ma, J
Lee, R.T.C
Sirota, F.L
Eisenhaber, F 
Keywords: Aves
Influenza A virus
Influenzavirus A
Suidae
antivirus agent
sialidase
virus antibody
amino acid sequence
article
binding site
chemical structure
chemistry
drug effect
enzymology
genetic variability
genetics
human
immunology
Influenza virus A H1N1
molecular genetics
mutation
nucleotide sequence
phylogeny
protein processing
protein tertiary structure
sequence alignment
sequence analysis
surface property
Amino Acid Sequence
Antibodies, Viral
Antiviral Agents
Binding Sites
Conserved Sequence
Genetic Variation
Humans
Influenza A Virus, H1N1 Subtype
Models, Molecular
Molecular Sequence Data
Mutation
Neuraminidase
Phylogeny
Protein Processing, Post-Translational
Protein Structure, Tertiary
Sequence Alignment
Sequence Analysis, Protein
Surface Properties
Issue Date: 2009
Citation: Maurer-Stroh, S, Ma, J, Lee, R.T.C, Sirota, F.L, Eisenhaber, F (2009). Mapping the sequence mutations of the 2009 H1N1 influenza A virus neuraminidase relative to drug and antibody binding sites. Biology Direct 4 : 18. ScholarBank@NUS Repository. https://doi.org/10.1186/1745-6150-4-18
Abstract: 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. © 2009 Maurer-Stroh et al; licensee BioMed Central Ltd.
Source Title: Biology Direct
URI: https://scholarbank.nus.edu.sg/handle/10635/174182
ISSN: 17456150
DOI: 10.1186/1745-6150-4-18
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