RELATIONS ENTRE LES PROPRIÉTÉS CYTOPATHOGÉNIQUES, HÉMADSORBANTES ET HÉMAGGLUTINANTES DU VIRUS DE L'INFLUENZA

1961 ◽  
Vol 7 (3) ◽  
pp. 347-353 ◽  
Author(s):  
A. Boudreault ◽  
V. Pavilanis

Quantitative relations between hemadsorption, hemagglutination, and cytopathogenicity of influenza virus strains have been studied. The influenza virus has been cultivated on monkey kidney, chick kidney, and chick embryo cells.It was shown that hemadsorption can also be used for titration of influenza virus adapted on tissue culture.This technic is a reliable and sensitive one. It was also found that the growth of influenza virus is better in a medium of neutral pH and that chicks' age is not an important factor in the multiplication of the virus on chick kidney cells.

1985 ◽  
Vol 5 (9) ◽  
pp. 2181-2189
Author(s):  
L V Jones ◽  
R W Compans ◽  
A R Davis ◽  
T J Bos ◽  
D P Nayak

We have investigated the site of surface expression of the neuraminidase (NA) glycoprotein of influenza A virus, which, in contrast to the hemagglutinin, is bound to membranes by hydrophobic residues near the NH2-terminus. Madin-Darby canine kidney or primary African green monkey kidney cells infected with influenza A/WSN/33 virus and subsequently labeled with monoclonal antibody to the NA and then with a colloidal gold- or ferritin-conjugated second antibody exhibited specific labeling of apical surfaces. Using simian virus 40 late expression vectors, we also studied the surface expression of the complete NA gene (SNC) and a truncated NA gene (SN10) in either primary or a polarized continuous line (MA104) of African green monkey kidney cells. The polypeptides encoded by the cloned NA cDNAs were expressed on the surface of both cell types. Analysis of [3H]mannose-labeled polypeptides from recombinant virus-infected MA104 cells showed that the products of cloned NA cDNA comigrated with glycosylated NA from influenza virus-infected cells. Both the complete and the truncated glycoproteins were found to be preferentially expressed on apical plasma membranes, as detected by immunogold labeling. These results indicate that the NA polypeptide contains structural features capable of directing the transport of the protein to apical cell surfaces and the first 10 amino-terminal residues of the NA polypeptide are not involved in this process.


Virology ◽  
1970 ◽  
Vol 40 (2) ◽  
pp. 408-410 ◽  
Author(s):  
Yasuji Saito ◽  
Isao Yoshioka ◽  
Yoshiteru Igarashi ◽  
Susumu Nakagawa

1985 ◽  
Vol 5 (9) ◽  
pp. 2181-2189 ◽  
Author(s):  
L V Jones ◽  
R W Compans ◽  
A R Davis ◽  
T J Bos ◽  
D P Nayak

We have investigated the site of surface expression of the neuraminidase (NA) glycoprotein of influenza A virus, which, in contrast to the hemagglutinin, is bound to membranes by hydrophobic residues near the NH2-terminus. Madin-Darby canine kidney or primary African green monkey kidney cells infected with influenza A/WSN/33 virus and subsequently labeled with monoclonal antibody to the NA and then with a colloidal gold- or ferritin-conjugated second antibody exhibited specific labeling of apical surfaces. Using simian virus 40 late expression vectors, we also studied the surface expression of the complete NA gene (SNC) and a truncated NA gene (SN10) in either primary or a polarized continuous line (MA104) of African green monkey kidney cells. The polypeptides encoded by the cloned NA cDNAs were expressed on the surface of both cell types. Analysis of [3H]mannose-labeled polypeptides from recombinant virus-infected MA104 cells showed that the products of cloned NA cDNA comigrated with glycosylated NA from influenza virus-infected cells. Both the complete and the truncated glycoproteins were found to be preferentially expressed on apical plasma membranes, as detected by immunogold labeling. These results indicate that the NA polypeptide contains structural features capable of directing the transport of the protein to apical cell surfaces and the first 10 amino-terminal residues of the NA polypeptide are not involved in this process.


1971 ◽  
Vol 7 (1) ◽  
pp. 59-64 ◽  
Author(s):  
Jeffrey Anderson ◽  
Kenneth J. McCormick ◽  
Wayne A. Stenback ◽  
John J. Trentin

1968 ◽  
Vol 14 (8) ◽  
pp. 867-874 ◽  
Author(s):  
A. Boudreault ◽  
G. Lussier ◽  
V. Pavilanis

Two mouse-adapted influenza virus strains were adapted to growth at 29 °C by a gradual lowering of the temperature of incubation in embryonated eggs. The growth of these two cold variants was completely inhibited at 41 °C. The cold and hot variants showed no significant difference in rise in the infectious titer in the mouse lung but a marked reduction in mortality and pathological response was observed with the cold variants, while good antibody response was stimulated in both cases. The cold variants were better interferon inducers in chick embryo. However, neither cold nor hot variants induced more than detectable amounts of interferon in blood, spleen, or lungs of infected mice. These cold variants possess many characteristics suitable for an effective live virus vaccine.


1981 ◽  
Vol 53 (2) ◽  
pp. 347-351 ◽  
Author(s):  
K. G. Nicholson ◽  
S. P. Bauer ◽  
P. Harrison

1973 ◽  
Vol 19 (1) ◽  
pp. 147-149 ◽  
Author(s):  
R. Dobardzic ◽  
A. Boudreault ◽  
V. Pavilanis

The specific antibodies anti-influenza virus A2/Aichi/68 were combined immunologically with the virus purified by zonal centrifugation, then dissociated by lowering the pH and conjugated with horseradish peroxidase using glutaraldehyde as the coupling agent. With so labeled antibodies it was possible to detect the viral antigen in infected chick embryo kidney cells with the light microscope. This work suggests that the immunoperoxidase technique could be useful for early rhinocytologic diagnosis of influenza virus infections.


1987 ◽  
Vol 262 (4) ◽  
pp. 1876-1881
Author(s):  
G Noël ◽  
L Zollinger ◽  
N Larivière ◽  
C Nault ◽  
P Crine ◽  
...  
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