scholarly journals Optimization of cell culture-derived influenza A virus particles purification using sulfated cellulose membrane adsorbers

2017 ◽  
Vol 18 (1) ◽  
pp. 29-39 ◽  
Author(s):  
Ana Raquel Fortuna ◽  
Florian Taft ◽  
Louis Villain ◽  
Michael W. Wolff ◽  
Udo Reichl
Keyword(s):  
Cell Culture ◽  
Influenza A Virus ◽  
Influenza A ◽  
Cellulose Membrane ◽  
Virus Particles ◽  
Membrane Adsorbers

Direct capture of influenza A virus from cell culture supernatant with Sartobind anion-exchange membrane adsorbers

2007 ◽  
Vol 299 (1-2) ◽  
pp. 251-260 ◽  
Author(s):  
Bernd Kalbfuss ◽  
Michael Wolff ◽  
Liane Geisler ◽  
Alexander Tappe ◽  
Ranil Wickramasinghe ◽  
...  
Keyword(s):  
Cell Culture ◽  
Anion Exchange ◽  
Influenza A Virus ◽  
Influenza A ◽  
Culture Supernatant ◽  
Anion Exchange Membrane ◽  
Cell Culture Supernatant ◽  
Direct Capture ◽  
Membrane Adsorbers ◽  
Exchange Membrane

Evidence for specific packaging of the influenza A virus genome from conditionally defective virus particles lacking a polymerase gene

Vaccine ◽  
2006 ◽  
Vol 24 (44-46) ◽  
pp. 6647-6650 ◽  
Author(s):  
Emmie de Wit ◽  
Monique I.J. Spronken ◽  
Guus F. Rimmelzwaan ◽  
Albert D.M.E. Osterhaus ◽  
Ron A.M. Fouchier
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Virus Genome ◽  
Polymerase Gene ◽  
Virus Particles ◽  
Defective Virus

scholarly journals Deep Mutational Scan of the Highly Conserved Influenza A Virus M1 Matrix Protein Reveals Substantial Intrinsic Mutational Tolerance

2019 ◽  
Vol 93 (13) ◽  
Author(s):  
Nancy Hom ◽  
Lauren Gentles ◽  
Jesse D. Bloom ◽  
Kelly K. Lee
Keyword(s):  
Cell Culture ◽  
Influenza Virus ◽  
Amino Acid ◽  
Viral Replication ◽  
Influenza A Virus ◽  
Influenza A ◽  
Matrix Protein ◽  
Influenza Virus Infection ◽  
Sequence Diversity ◽  
Virus Protein

ABSTRACTInfluenza A virus matrix protein M1 is involved in multiple stages of the viral infectious cycle. Despite its functional importance, our present understanding of this essential viral protein is limited. The roles of a small subset of specific amino acids have been reported, but a more comprehensive understanding of the relationship between M1 sequence, structure, and virus fitness remains elusive. In this study, we used deep mutational scanning to measure the effect of every amino acid substitution in M1 on viral replication in cell culture. The map of amino acid mutational tolerance we have generated allows us to identify sites that are functionally constrained in cell culture as well as sites that are less constrained. Several sites that exhibit low tolerance to mutation have been found to be critical for M1 function and production of viable virions. Surprisingly, significant portions of the M1 sequence, especially in the C-terminal domain, whose structure is undetermined, were found to be highly tolerant of amino acid variation, despite having extremely low levels of sequence diversity among natural influenza virus strains. This unexpected discrepancy indicates that not all sites in M1 that exhibit high sequence conservation in nature are under strong constraint during selection for viral replication in cell culture.IMPORTANCEThe M1 matrix protein is critical for many stages of the influenza virus infection cycle. Currently, we have an incomplete understanding of this highly conserved protein’s function and structure. Key regions of M1, particularly in the C terminus of the protein, remain poorly characterized. In this study, we used deep mutational scanning to determine the extent of M1’s tolerance to mutation. Surprisingly, nearly two-thirds of the M1 sequence exhibits a high tolerance for substitutions, contrary to the extremely low sequence diversity observed across naturally occurring M1 isolates. Sites with low mutational tolerance were also identified, suggesting that they likely play critical functional roles and are under selective pressure. These results reveal the intrinsic mutational tolerance throughout M1 and shape future inquiries probing the functions of this essential influenza A virus protein.

scholarly journals The Influenza A Virus M2 Cytoplasmic Tail Is Required for Infectious Virus Production and Efficient Genome Packaging

2005 ◽  
Vol 79 (6) ◽  
pp. 3595-3605 ◽  
Author(s):  
Matthew F. McCown ◽  
Andrew Pekosz
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Infectious Virus ◽  
Virus Production ◽  
Cytoplasmic Tail ◽  
Host Cells ◽  
Wild Type Virus ◽  
Type Virus ◽  
Wild Type ◽  
Virus Particles

ABSTRACT The M2 integral membrane protein encoded by influenza A virus possesses an ion channel activity that is required for efficient virus entry into host cells. The role of the M2 protein cytoplasmic tail in virus replication was examined by generating influenza A viruses encoding M2 proteins with truncated C termini. Deletion of 28 amino acids (M2Stop70) resulted in a virus that produced fourfold-fewer particles but >1,000-fold-fewer infectious particles than wild-type virus. Expression of the full-length M2 protein in trans restored the replication of the M2 truncated virus. Although the M2Stop70 virus particles were similar to wild-type virus in morphology, the M2Stop70 virions contained reduced amounts of viral nucleoprotein and genomic RNA, indicating a defect in vRNP packaging. The data presented indicate the M2 cytoplasmic tail plays a role in infectious virus production by coordinating the efficient packaging of genome segments into influenza virus particles.

scholarly journals Relevance of Influenza A Virus Detection by PCR, Shell Vial Assay, and Tube Cell Culture to Rapid Reporting Procedures

2006 ◽  
Vol 44 (9) ◽  
pp. 3366-3367 ◽  
Author(s):  
N. L. Zitterkopf ◽  
S. Leekha ◽  
M. J. Espy ◽  
C. M. Wood ◽  
P. Sampathkumar ◽  
...  
Keyword(s):  
Cell Culture ◽  
Influenza A Virus ◽  
Influenza A ◽  
Virus Detection ◽  
Shell Vial ◽  
Tube Cell ◽  
Reporting Procedures ◽  
Shell Vial Assay
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