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PMID:21431346
| Citation |
Abdel-Moneim, AS, Shehab, GM and Abu-Elsaad, AA (2011) Molecular evolution of the six internal genes of H5N1 equine influenza A virus. Arch. Virol. 156:1257-62 |
|---|---|
| Abstract |
Phylogenetic and evolutionary patterns of the six internal genes of an equine H5N1 influenza A virus isolated in Egypt on 2009 were analyzed using direct sequencing. All of the internal genes of the equine H5N1 strain showed a genetic pattern potentially related to Eurasian lineages. Variable dendrogram topologies revealed an absence of reassortment in the equine strain while confirming its close relatedness to other Egyptian H5N1 strains from human and avian species. The equine strain is characterized by a variety of amino acid substitutions in six internal proteins compared to the available Egyptian H5N1 strains. Interestingly, the equine strain displayed amino acids in the PB2, PA, M2 and NS2 proteins that are unique among the available H5N1 sequences in the flu database, and their potential effect on virulence needs to be further investigated. |
| Links |
PubMed Online version:10.1007/s00705-011-0966-3 |
| Keywords |
Amino Acid Sequence; Animals; Birds; Evolution, Molecular; Horse Diseases/virology; Horses; Humans; Influenza A Virus, H5N1 Subtype/classification; Influenza A Virus, H5N1 Subtype/genetics; Influenza A Virus, H5N1 Subtype/isolation & purification; Influenza in Birds/virology; Influenza, Human/virology; Molecular Sequence Data; Orthomyxoviridae Infections/veterinary; Orthomyxoviridae Infections/virology; Phylogeny; Viral Proteins/genetics; Viral Proteins/metabolism |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0003968: RNA-directed RNA polymerase activity |
ECO:0000316: |
F |
The polymorphic amino acid sites in the protein sequences of the Egyptian human and avian strains in comparison to the equine isolate were examined, as was the distribution of the alternative residues among strains classified as virulent or nonvirulent (Table 2), such residues having functional significance for virulence in H5N1. H5N1 influenza virus isolated from equines and humans in Egypt contained most of the amino acids specific to the avian virus, where the PB2 contained two avian virus-like amino acids (alanine, A 661 and lysine, K 702). These two amino acids are located in the domain of the PB2 gene, which is believed to be responsible for interaction with other polymerase components [30]. One genetic indicator of adaptation and efficient replication in humans is the E627K substitution in the PB2 protein [34, 37]. |
Missing: with/from | ||||
See also
References
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