Abstract |
Hemagglutinin (HA) protein plays an important role in binding the influenza virus to infected cells and therefore mediates infection. Deposited HA sequences of 86 Asian strains of influenza A (H1N1) viruses during the first outbreak were obtained from the NCBI database and compared. Interaction of the HA protein of influenza A (H1N1) virus with the human sialic acid receptor was also studied using bioinformatics. Overall, not more than three single-point amino acid variants/changes were observed in the HA protein region of influenza A (H1N1) virus from Asian countries when a selected group sequence comparison was made. The bioinformatics study showed that the HA protein of influenza A (H1N1) binds to the sialic acid receptor in human airway receptors, possibly key to air-borne infection in humans.
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Authors | K H Chua, H C Chai |
Journal | Genetics and molecular research : GMR
(Genet Mol Res)
Vol. 11
Issue 1
Pg. 636-43
(Mar 16 2012)
ISSN: 1676-5680 [Electronic] Brazil |
PMID | 22535399
(Publication Type: Journal Article)
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Chemical References |
- Hemagglutinin Glycoproteins, Influenza Virus
- Receptors, Virus
- N-Acetylneuraminic Acid
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Topics |
- Amino Acid Substitution
- Asia
- Binding Sites
- Hemagglutinin Glycoproteins, Influenza Virus
(chemistry, genetics, metabolism)
- Humans
- Hydrogen Bonding
- Influenza A Virus, H1N1 Subtype
(genetics, metabolism)
- Models, Molecular
- Mutation
- N-Acetylneuraminic Acid
(chemistry, metabolism)
- Protein Binding
- Receptors, Virus
(metabolism)
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