DESTRUCTION OF INFLUENZA VIRUS RECEPTORS IN THE MOUSE LUNG BY AN ENZYME FROM V. CHOLERAE

1948 ◽  
Vol 26 (1) ◽  
pp. 29-36 ◽  
Author(s):  
S Fazekas de St. Groth
Intervirology ◽  
1976 ◽  
Vol 7 (4-5) ◽  
pp. 201-210 ◽  
Author(s):  
Bertram Flehmig ◽  
Angelika Vallbracht ◽  
Hans-Joachim Gerth

1948 ◽  
Vol 87 (4) ◽  
pp. 315-328 ◽  
Author(s):  
George K. Hirst

Evidence has been offered that influenza virus which has been heated at 56°C. for 30 or more minutes loses some of its capacity to agglutinate red cells and may completely lose its power to elute from cells on which it has been adsorbed. Such heat-inactivated virus does not possess the capacity to destroy the virus inhibitor in normal rabbit serum and this appears to be the explanation of the higher agglutinin inhibitory levels obtained with serum and heated virus as compared with serum and untreated virus. The heat-inactivated virus can be used to measure the inhibitor substance in normal rabbit serum. By two different methods it has been demonstrated that the inhibitor is destroyed in the presence of unheated influenza virus, as measured by inhibition titrations with virus inactivated at 56°C. The destruction of inhibitor by virus of either type A or B can be measured by virus of either type with similar results.


2009 ◽  
Vol 33 (8) ◽  
pp. 895-903 ◽  
Author(s):  
Zhang-Yong Ning ◽  
Min-Yi Luo ◽  
Wen-Bao Qi ◽  
Bo Yu ◽  
Pei-Rong Jiao ◽  
...  

Vaccines ◽  
2020 ◽  
Vol 8 (2) ◽  
pp. 207 ◽  
Author(s):  
Shelby Landreth ◽  
Yao Lu ◽  
Kannupriya Pandey ◽  
Yan Zhou

Avian influenza H7N9 viruses continue to pose a great threat to public health, which is evident by their high case-fatality rates. Although H7N9 was first isolated in humans in China in 2013, to date, there is no commercial vaccine available against this particular strain. Our previous studies developed a replication-defective influenza virus through mutation of the hemagglutinin (HA) cleavage site from a trypsin-sensitive to an elastase-sensitive motif. In this study, we report the development of a reassortant mutant influenza virus derived from the human isolate A/British Columbia/01/2015 (H7N9) [BC15 (H7N9)], which is the QVT virus. The HA gene of this virus possesses three mutations at the cleavage site, Lys-Gly-Arg were mutated to Gln-Thr-Val at amino acid (aa) positions 337, 338, and 339, respectively. We report this virus to rely on elastase in vitro, possess unaltered replication abilities when elastase was provided compared to the wild type virus in vitro, and to be non-virulent and replication-defective in mice. In addition, we report this virus to induce significant levels of antibodies and IFN-γ and IL-5 secreting cells, and to protect mice against a lethal challenge of the BC15 (H7N9) virus. This protection is demonstrated through the lack of body weight loss, 100% survival rate, and the prevention of BC15 (H7N9) viral replication as well as the reduction of proinflammatory cytokines induced in the mouse lung associated with the influenza disease. Therefore, these results provide strong evidence for the use of this reassortant mutant H7N9 virus as a replication-defective virus vaccine candidate against H7N9 viruses.


1949 ◽  
Vol 89 (2) ◽  
pp. 233-243 ◽  
Author(s):  
George K. Hirst

Influenza virus, treated with sodium periodate, was adsorbed well on red cells but lacked the capacity for spontaneous elution. Heated virus was eluted from red cells by the action of cholera vibrio filtrate, unheated influenza virus, and to a small extent by heating at 56°C. Periodate-treated virus was not elutable by these methods but was liberated by exposure of the adsorbing cells to concentrations of sodium chloride of 5 to 10 per cent. This treatment had no effect on elution of heated virus.


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