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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 |
| Appears in Collections: | Elements Staff Publications |
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