scholarly journals Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR

2013 ◽  
Vol 22 (11) ◽  
pp. 1623-1638 ◽  
Author(s):  
Shu Yu Liao ◽  
Keith J. Fritzsching ◽  
Mei Hong
Keyword(s):  
Solid State ◽  
Conformational Analysis ◽  
Influenza A Virus ◽  
Solid State Nmr ◽  
Influenza A ◽  
Full Length ◽  
M2 Protein

scholarly journals Transmembrane Domain of M2 Protein from Influenza A Virus Studied by Solid-State 15N Polarization Inversion Spin Exchange at Magic Angle NMR

2000 ◽  
Vol 79 (2) ◽  
pp. 767-775 ◽  
Author(s):  
Zhiyan Song ◽  
F.A. Kovacs ◽  
J. Wang ◽  
Jeffrey K. Denny ◽  
S.C. Shekar ◽  
...  
Keyword(s):  
Solid State ◽  
Influenza A Virus ◽  
Influenza A ◽  
Spin Exchange ◽  
Transmembrane Domain ◽  
Magic Angle ◽  
M2 Protein

Expression and Initial Structural Insights from Solid-State NMR of the M2 Proton Channel from Influenza A Virus†

Biochemistry ◽  
2002 ◽  
Vol 41 (37) ◽  
pp. 11294-11300 ◽  
Author(s):  
Changlin Tian ◽  
Kurt Tobler ◽  
Robert A. Lamb ◽  
Lawrence H. Pinto ◽  
T. A. Cross
Keyword(s):  
Solid State ◽  
Influenza A Virus ◽  
Solid State Nmr ◽  
Influenza A ◽  
Proton Channel ◽  
M2 Proton Channel ◽  
Structural Insights

scholarly journals Magic Angle Spinning and Oriented Sample Solid-State NMR Structural Restraints Combine for Influenza A M2 Protein Functional Insights

2012 ◽  
Vol 134 (22) ◽  
pp. 9022-9025 ◽  
Author(s):  
Thach V. Can ◽  
Mukesh Sharma ◽  
Ivan Hung ◽  
Peter L. Gor’kov ◽  
William W. Brey ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Influenza A ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
M2 Protein ◽  
Oriented Sample ◽  
Angle Spinning ◽  
Structural Restraints

scholarly journals Oligomeric States of Full Length Influenza a Virus M2 Proteins on Biological Membranes

2013 ◽  
Vol 104 (2) ◽  
pp. 277a
Author(s):  
Ken-ichi Kawano ◽  
Sayaka Matsuzaki ◽  
Kaoru Oomae ◽  
Yoshiaki Yano ◽  
Katsumi Matsuzaki
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Biological Membranes ◽  
Full Length

scholarly journals EPR Spectroscopy of the C-terminal Domain of the M2 Protein from Influenza A Virus

2009 ◽  
Vol 96 (3) ◽  
pp. 432a
Author(s):  
Emily Brown ◽  
Phuong Nguyen ◽  
Kathleen P. Howard
Keyword(s):  
Influenza A Virus ◽  
Epr Spectroscopy ◽  
Influenza A ◽  
M2 Protein ◽  
Terminal Domain

Physicochemical study of the influenza A virus M2 protein and aluminum salt adjuvant interaction as a vaccine candidate model

2019 ◽  
Vol 14 (8) ◽  
pp. 523-536
Author(s):  
Maryam Saleh ◽  
Jamileh Nowroozi ◽  
Fatemeh Fotouhi ◽  
Behrokh Farahmand
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Structural Changes ◽  
Vaccine Candidate ◽  
Human Influenza ◽  
M2 Protein ◽  
Physicochemical Methods ◽  
Α Helix ◽  
High Level ◽  
Β Sheet

Aim: The present study evaluated the structural changes resulting from the interaction between a recombinant influenza A virus M2 protein and aluminum hydroxide adjuvant to investigate the antigen for further immunological studies. Materials & methods: Membrane protein II was produced from the H1N1 subtype of human influenza A virus. The interaction between M2 protein and alum inum hydroxide adjuvant was evaluated by physicochemical techniques including scanning electron microscope, UV-Vis spectra, Fourier-transform infrared spectroscopy and circular dichroism spectroscopy. Results: Physicochemical methods showed high-level protein adsorption and accessibility to the effective parts of the protein. Conclusion: It was concluded that M2 protein secondary structural perturbations, including the α-helix-to-β-sheet transition, enhanced its mechanical properties toward adsorption.

scholarly journals (In)validating experimentally derived knowledge about influenza A defective interfering particles

2016 ◽  
Vol 13 (124) ◽  
pp. 20160412 ◽  
Author(s):  
Laura E. Liao ◽  
Shingo Iwami ◽  
Catherine A. A. Beauchemin
Keyword(s):  
Mathematical Model ◽  
Experimental Method ◽  
Influenza A Virus ◽  
Influenza A ◽  
Infectious Virus ◽  
Full Length ◽  
Prior Work ◽  
Defective Interfering Particles ◽  
A Cell ◽  
Eclipse Phase

A defective interfering particle (DIP) in the context of influenza A virus is a virion with a significantly shortened RNA segment substituting one of eight full-length parent RNA segments, such that it is preferentially amplified. Hence, a cell co-infected with DIPs will produce mainly DIPs, suppressing infectious virus yields and affecting infection kinetics. Unfortunately, the quantification of DIPs contained in a sample is difficult because they are indistinguishable from standard virus (STV). Using a mathematical model, we investigated the standard experimental method for counting DIPs based on the reduction in STV yield (Bellett & Cooper, 1959, Journal of General Microbiology 21 , 498–509 ( doi:10.1099/00221287-21-3-498 )). We found the method is valid for counting DIPs provided that: (i) an STV-infected cell's co-infection window is approximately half its eclipse phase (it blocks infection by other virions before it begins producing progeny virions), (ii) a cell co-infected by STV and DIP produces less than 1 STV per 1000 DIPs and (iii) a high MOI of STV stock (more than 4 PFU per cell) is added to perform the assay. Prior work makes no mention of these criteria such that the method has been applied incorrectly in several publications discussed herein. We determined influenza A virus meets these criteria, making the method suitable for counting influenza A DIPs.

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