scholarly journals Hemagglutinin and neuraminidase matching patterns of two influenza A virus strains related to the 1918 and 2009 global pandemics

2009 ◽  
Vol 387 (2) ◽  
pp. 405-408 ◽  
Author(s):  
Yonghui Zhang ◽  
Xiaojing Lin ◽  
Fengwei Zhang ◽  
Jia Wu ◽  
Wenjie Tan ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Virus Strains

Analysis of the Receptor Specificity of Influenza A Virus Strains Using the Method of Surface Plasmon Resonance

BIOPHYSICS ◽  
2020 ◽  
Vol 65 (2) ◽  
pp. 222-224
Author(s):  
G. S. Onkhonova ◽  
P. Yu. Torzhkova ◽  
V. Yu. Marchenko ◽  
S. V. Svyatchenko ◽  
A. S. Gudymo ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Influenza A Virus ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Influenza A ◽  
Receptor Specificity ◽  
Virus Strains

scholarly journals QUALITATIVE DIFFERENCES IN THE ANTIGENIC COMPOSITION OF INFLUENZA A VIRUS STRAINS

1944 ◽  
Vol 79 (6) ◽  
pp. 633-647 ◽  
Author(s):  
William F. Friedewald
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Serum Antibody ◽  
Allantoic Fluid ◽  
Influenza B Virus ◽  
Influenza B ◽  
Red Cell ◽  
Homologous Virus ◽  
Cell Adsorption ◽  
Virus Strains

A study of the PR8, Christie, Talmey, W.S., and swine strains of influenza A virus by means of antibody absorption tests revealed the following findings: 1. Serum antibody could be specifically absorbed with allantoic fluid containing influenza virus or, more effectively, with concentrated suspensions of virus obtained from allantoic fluid by high-speed centrifugation or by the red cell adsorption and elution technique. Normal allantoic fluid, or the centrifugalized sediment therefrom, failed to absorb antibodies. Influenza B virus (Lee) caused no detectable absorption of antibody from antisera directed against influenza A virus strains, but it specifically absorbed antibody from Lee antisera. 2. The neutralizing, agglutination-inhibiting, and complement-fixing anti-bodies in ferret antisera were completely absorbed only by the homologous virus strain, even though 2 absorptions were carried out with large amounts of heterologous virus strains. 3. PR8 virus appeared to have the broadest range of specific antigenic components for it completely absorbed the heterologous antibodies in Christie and W.S. antisera and left only those antibodies which reacted with the respective homologous strains. The other virus strains (Christie, Talmey, W.S., swine) were more specific in the absorption of heterologous antibodies and completely removed only those antibodies which reacted with the absorbing virus. 4. The absorption tests revealed a higher degree of specificity and individuality of the virus strains than the various cross reactions previously reported. The strain specificity of PR8 virus was equally manifest in absorption tests with ferret sera and with human sera following vaccination. 5. The amount of homologous antibody remaining in a PR8 ferret serum after absorption with PR8 virus, obtained by the red cell adsorption and elution method, varied inversely as the concentration of virus used for absorption. A given concentration of virus, however, absorbed a greater percentage of neutralizing antibodies than either agglutination-inhibiting or complement-fixing antibodies.

scholarly journals Complete Genomic Sequences of H3N8 Equine Influenza Virus Strains Used as Vaccine Strains in Japan

2018 ◽  
Vol 6 (12) ◽  
Author(s):  
Manabu Nemoto ◽  
Takashi Yamanaka ◽  
Hiroshi Bannai ◽  
Koji Tsujimura ◽  
Hiroshi Kokado
Keyword(s):  
Influenza Virus ◽  
Influenza A Virus ◽  
Influenza A ◽  
Animal Health ◽  
Genomic Sequences ◽  
Equine Influenza Virus ◽  
Equine Influenza ◽  
World Organization ◽  
Virus Strains ◽  
Complete Genomic

ABSTRACT We sequenced the eight segments of influenza A virus strains A/equine/Ibaraki/1/2007 and A/equine/Yokohama/aq13/2010, which are strains of the Florida sublineage clades 1 and 2 of the H3N8 subtype equine influenza virus. These strains have been used as vaccine strains in Japan since 2016 in accordance with World Organization for Animal Health (OIE) recommendations.

Kinetic studies on the sialidase of three influenza B and three influenza A virus strains

1989 ◽  
Vol 6 (2) ◽  
pp. 219-227 ◽  
Author(s):  
Jos� A Cabezas ◽  
Milagros Milicua ◽  
Carmen S Bernal ◽  
Enrique Villar ◽  
Nieves Perez ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Kinetic Studies ◽  
Influenza B ◽  
Virus Strains

scholarly journals Virtual Screening Identifies Chebulagic Acid as an Inhibitor of the M2(S31N) Viral Ion Channel and Influenza A Virus

Molecules ◽  
2020 ◽  
Vol 25 (12) ◽  
pp. 2903
Author(s):  
Maggie C. Duncan ◽  
Pascal Amoa Onguéné ◽  
Ibuki Kihara ◽  
Derrick N. Nebangwa ◽  
Maya E. Naidu ◽  
...  
Keyword(s):  
Ion Channel ◽  
Influenza A Virus ◽  
Influenza A ◽  
Influenza Viruses ◽  
Drug Resistant ◽  
M2 Protein ◽  
Virtual Screen ◽  
Chebulagic Acid ◽  
Virus Strains

The increasing prevalence of drug-resistant influenza viruses emphasizes the need for new antiviral countermeasures. The M2 protein of influenza A is a proton-gated, proton-selective ion channel, which is essential for influenza replication and an established antiviral target. However, all currently circulating influenza A virus strains are now resistant to licensed M2-targeting adamantane drugs, primarily due to the widespread prevalence of an M2 variant encoding a serine to asparagine 31 mutation (S31N). To identify new chemical leads that may target M2(S31N), we performed a virtual screen of molecules from two natural product libraries and identified chebulagic acid as a candidate M2(S31N) inhibitor and influenza antiviral. Chebulagic acid selectively restores growth of M2(S31N)-expressing yeast. Molecular modeling also suggests that chebulagic acid hydrolysis fragments preferentially interact with the highly-conserved histidine residue within the pore of M2(S31N) but not adamantane-sensitive M2(S31). In contrast, chebulagic acid inhibits in vitro influenza A replication regardless of M2 sequence, suggesting that it also acts on other influenza targets. Taken together, results implicate chebulagic acid and/or its hydrolysis fragments as new chemical leads for M2(S31N) and influenza-directed antiviral development.

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