The reassortment in proteins from influenza A viruses among human, swine, and Eurasian avian strains formed a new influenza A virus leading to the first pandemic in this century, which suggests that the barrier between species and between subtypes would not be strong enough to prevent the cross-species infection and cross-subtype reassortment from occurring. In this study, we intensively used the ANOVA including its model I and model II to analyze 2430 polymerase basic proteins 2 (PB2) of influenza A viruses in order to determine whether there is a barrier between species and between subtypes. The results show that (i) there is a barrier between HA subtypes, between NA subtypes and between hosting species in some cases, however, there is no barrier in most cases, which can lead to cross-species infection and crosssubtype reassortment, and (ii) the intra-subtype/species variation is larger than the inter-subtype/species variation in most cases, which can lead mutations/reassortments in PB2 to easily jump from species to species or from subtype to subtype. These results are in agreement with our previous studies along this research line in the hemagglutinin, neuraminidase, matrix protein 1 and 2 from influenza A virus, and provide further explanations for the possible reason for cross-subtype reassortment and cross-species infection.
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influenza A virus;
polymerase basic protein 2;
Document Type: Research Article
Publication date: 2011-05-01
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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.