scholarly journals Structure and Function of the Influenza Virus Transcription and Replication Machinery

2019 ◽  
Vol 10 (9) ◽  
pp. a038398 ◽  
Author(s):  
Ervin Fodor ◽  
Aartjan J.W. te Velthuis
Keyword(s):  
Influenza Virus ◽  
Structure And Function ◽  
Replication Machinery ◽  
Virus Transcription ◽  
And Function ◽  
Transcription And Replication

scholarly journals Influenza Virus Neuraminidase: Structure and Function

Acta Naturae ◽  
2009 ◽  
Vol 1 (2) ◽  
pp. 26-32 ◽  
Author(s):  
Y A Shtyrya ◽  
L V Mochalova ◽  
N V Bovin
Keyword(s):  
Influenza Virus ◽  
Structure And Function ◽  
And Function ◽  
Influenza Virus Neuraminidase

scholarly journals Structure and function of the influenza virus genome

1983 ◽  
Vol 211 (2) ◽  
pp. 281-294 ◽  
Author(s):  
J W McCauley ◽  
B W J Mahy
Keyword(s):  
Influenza Virus ◽  
Virus Genome ◽  
Structure And Function ◽  
And Function

The haloarchaeal chromosome replication machinery

2009 ◽  
Vol 37 (1) ◽  
pp. 108-113 ◽  
Author(s):  
Stuart A. MacNeill
Keyword(s):  
Dna Replication ◽  
Replication Fork ◽  
Biochemical Analysis ◽  
Structure And Function ◽  
Haloferax Volcanii ◽  
Eukaryotic Cells ◽  
Replication Machinery ◽  
Chromosomal Dna ◽  
Biochemical Studies ◽  
And Function

The powerful combination of genetic and biochemical analysis has provided many key insights into the structure and function of the chromosomal DNA replication machineries of bacterial and eukaryotic cells. In contrast, in the archaea, biochemical studies have dominated, mainly due to the absence of efficient genetic systems for these organisms. This situation is changing, however, and, in this regard, the genetically tractable haloarchaea Haloferax volcanii and Halobacterium sp. NRC-1 are emerging as key models. In the present review, I give an overview of the components of the replication machinery in the haloarchaea, with particular emphasis on the protein factors presumed to travel with the replication fork.

scholarly journals Oligomerization of the influenza virus polymerase complex in vivo

2008 ◽  
Vol 89 (2) ◽  
pp. 520-524 ◽  
Author(s):  
Núria Jorba ◽  
Estela Area ◽  
Juan Ortín
Keyword(s):  
Influenza Virus ◽  
Virus Infection ◽  
Affinity Purification ◽  
Significant Proportion ◽  
Gel Filtration ◽  
Agarose Gel ◽  
Polymerase Complex ◽  
Virus Transcription ◽  
Transcription And Replication

The influenza virus polymerase is a heterotrimer formed by the PB1, PB2 and PA subunits and is responsible for virus transcription and replication. We have expressed the virus polymerase complex by co-transfection of the subunit cDNAs, one of which was tandem affinity purification (TAP)-tagged, into human cells. The intracellular polymerase complexes were purified by the TAP approach, involving two affinity chromatography steps, IgG–Sepharose and calmodulin–agarose. Gel-filtration analysis indicated that, although most of the purified polymerase behaved as a heterotrimer, a significant proportion of the purified material migrated as polymerase dimers, trimers and higher oligomers. Co-purification of polymerase complexes alternatively tagged in the same subunit confirmed that the polymerase complex might form oligomers intracellularly. The implications of this observation for virus infection are discussed.

scholarly journals The Cellular Factor NXP2/MORC3 Is a Positive Regulator of Influenza Virus Multiplication

2015 ◽  
Vol 89 (19) ◽  
pp. 10023-10030 ◽  
Author(s):  
Lorena S. Ver ◽  
Laura Marcos-Villar ◽  
Sara Landeras-Bueno ◽  
Amelia Nieto ◽  
Juan Ortín
Keyword(s):  
Influenza Virus ◽  
Virus Infection ◽  
Nuclear Matrix ◽  
Influenza Viruses ◽  
Genomic Rna ◽  
Viral Polymerase ◽  
Virus Transcription ◽  
Infected Cells ◽  
Transcription And Replication

ABSTRACTTranscription and replication of influenza A virus are carried out in the nuclei of infected cells in the context of viral ribonucleoproteins (RNPs). The viral polymerase responsible for these processes is a protein complex composed of the PB1, PB2, and PA proteins. We previously identified a set of polymerase-associated cellular proteins by proteomic analysis of polymerase-containing intracellular complexes expressed and purified from human cells. Here we characterize the role of NXP2/MORC3 in the infection cycle. NXP2/MORC3 is a member of the Microrchidia (MORC) family that is associated with the nuclear matrix and has RNA-binding activity. Influenza virus infection led to a slight increase in NXP2/MORC3 expression and its partial relocalization to the cytoplasm. Coimmunoprecipitation and immunofluorescence experiments indicated an association of NXP2/MORC3 with the viral polymerase and RNPs during infection. Downregulation of NXP2/MORC3 by use of two independent short hairpin RNAs (shRNAs) reduced virus titers in low-multiplicity infections. Consistent with these findings, analysis of virus-specific RNA in high-multiplicity infections indicated a reduction of viral RNA (vRNA) and mRNA after NXP2/MORC3 downregulation. Silencing of NXP2/MORC3 in a recombinant minireplicon system in which virus transcription and replication are uncoupled showed reductions incatmRNA and chloramphenicol acetyltransferase (CAT) protein accumulation but no alterations incatvRNA levels, suggesting that NXP2/MORC3 is important for influenza virus transcription.IMPORTANCEInfluenza virus infections appear as yearly epidemics and occasional pandemics of respiratory disease, with high morbidity and occasional mortality. Influenza viruses are intracellular parasites that replicate and transcribe their genomic ribonucleoproteins in the nuclei of infected cells, in a complex interplay with host cell factors. Here we characterized the role of the human NXP2/MORC3 protein, a member of the Microrchidia family that is associated with the nuclear matrix, during virus infection. NXP2/MORC3 associates with the viral ribonucleoproteins in infected cells. Downregulation of NXP2/MORC3 reduced virus titers and accumulations of viral genomic RNA and mRNAs. Silencing of NXP2/MORC3 in an influenza virus CAT minireplicon system diminished CAT protein andcatmRNA levels but not genomic RNA levels. We propose that NXP2/MORC3 plays a role in influenza virus transcription.

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