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J Gen Virol. 2017 Jan 27. doi: 10.1099/jgv.0.000721. [Epub ahead of print]
Truncated forms of the PA protein containing only the C-terminal domains are associated with the RNP complex within H1N1 influenza virus particles.
Myaing M1, Jumat R2, Huong T3, Tan BH4, Sugrue RJ5.
Author information
Abstract
We have examined the expression profile of the influenza virus PA protein in pH1N1/2009 virus-infected cells. Immunoblotting analysis of virus-infected MDCK cells revealed the presence of full-length PA protein from 8 hrs post-infection, together with the simultaneous appearance of PA protein species of approximately 50 kDa, 35/39 kDa and 20/25 kDa (collectively referred to as PA*). PA* was also detected in H1N1/WSN virus-infected cells indicating that its presence was not virus-specific, and PA* was also observed in virus-infected A549 and CEF cells indicating that its presence was not cell type-specific. PA* was detected in cells expressing the recombinant PA protein, indicating that the PA* formation occurred in the absence of virus infection. These data collectivity indicated that PA* formation is an intrinsic property of PA gene expression. The association of PA* with purified influenza virus particles was demonstrated by immunoblotting, and a protease protection assay provided evidence that PA* was packaged into virus particles. The ribonucleoprotein (RNP) complex was isolated from purified influenza virus particles using glycerol gradient centrifugation, which demonstrated that PA* was associated with the RNP complex. To the best of our knowledge this is the first report to demonstrate that PA protein species containing only segments of the C-terminal domain form during influenza virus infection. Furthermore, these truncated PA protein species are subsequently packaged into virus particles as part of the functional RNP complex.
PMID: 28141511 DOI: 10.1099/jgv.0.000721
[PubMed - as supplied by publisher]
Truncated forms of the PA protein containing only the C-terminal domains are associated with the RNP complex within H1N1 influenza virus particles.
Myaing M1, Jumat R2, Huong T3, Tan BH4, Sugrue RJ5.
Author information
Abstract
We have examined the expression profile of the influenza virus PA protein in pH1N1/2009 virus-infected cells. Immunoblotting analysis of virus-infected MDCK cells revealed the presence of full-length PA protein from 8 hrs post-infection, together with the simultaneous appearance of PA protein species of approximately 50 kDa, 35/39 kDa and 20/25 kDa (collectively referred to as PA*). PA* was also detected in H1N1/WSN virus-infected cells indicating that its presence was not virus-specific, and PA* was also observed in virus-infected A549 and CEF cells indicating that its presence was not cell type-specific. PA* was detected in cells expressing the recombinant PA protein, indicating that the PA* formation occurred in the absence of virus infection. These data collectivity indicated that PA* formation is an intrinsic property of PA gene expression. The association of PA* with purified influenza virus particles was demonstrated by immunoblotting, and a protease protection assay provided evidence that PA* was packaged into virus particles. The ribonucleoprotein (RNP) complex was isolated from purified influenza virus particles using glycerol gradient centrifugation, which demonstrated that PA* was associated with the RNP complex. To the best of our knowledge this is the first report to demonstrate that PA protein species containing only segments of the C-terminal domain form during influenza virus infection. Furthermore, these truncated PA protein species are subsequently packaged into virus particles as part of the functional RNP complex.
PMID: 28141511 DOI: 10.1099/jgv.0.000721
[PubMed - as supplied by publisher]