Influence of the spectrin network on fusion of influenza virus with red blood cells

1995 ◽  
Vol 12 (3) ◽  
pp. 271-276 ◽  
Author(s):  
Torsten Reda ◽  
Robert Blumenthal ◽  
Peter Müller ◽  
Andreas Herrmann
1955 ◽  
Vol 62 (3) ◽  
pp. 342-348
Author(s):  
J. B. BATEMAN ◽  
MARY S. DAVIS ◽  
PATRICIA A. MCCAFFREY

2021 ◽  
Author(s):  
Christian Marco Hadi Nugroho ◽  
Ryan Septa Kurnia ◽  
Simson Tarigan ◽  
Otto Sahat Martua Silaen ◽  
Silvia Tri Widyaningtyas ◽  
...  

Abstract Study on sialidases as antiviral agents has been widely performed, but many types of sialidase had not been tested for their antiviral activity. One of such sialidase is the NanB sialidase of Pasteurella multocida, which has never been isolated for further study. In this study, the activity of NanB sialidase was investigated in silico by docking the NanB sialidase of Pasteurella multocida to the Neu5Acα(2-6)Gal ligand. Additionally, some local isolates of Pasteurella multocida, which had the NanB gene were screened, and the proteins were isolated for further testing regarding their activity in hydrolyzing Neu5Acα(2-6)Gal. In silico studies showed that the NanB sialidase possesses an exceptional affinity towards forming a protein-ligand complex with Neu5Acα(2-6)Gal. This was further confirmed by showing that a dose of 0.258 U/ml (100%) NanB sialidase of Pasteurella multocida B018 can hydrolyze up to 44.28% of Neu5Acα(2-6)Gal in chicken red blood cells and 81.95% in rabbit red blood cells. This study suggested that the NanB sialidase of Pasteurella multocida B018 has a potent antiviral activity that can inhibit avian influenza virus infection.


1956 ◽  
Vol 60 (2) ◽  
pp. 384-391 ◽  
Author(s):  
J.B. Bateman ◽  
Arnold Zellner ◽  
Mary S. Davis ◽  
Patricia A. McCaffrey

2021 ◽  
Author(s):  
Christian Marco Hadi Nugroho ◽  
Ryan Septa Kurnia ◽  
Simson Tarigan ◽  
Otto Sahat Martua Silaen ◽  
Silvia Tri Widyaningtyas ◽  
...  

Abstract Study on sialidases as antiviral agents has been widely performed, but many types of sialidase had not been tested for their antiviral activity. One of such sialidase is the NanB sialidase of Pasteurella multocida, which has never been isolated for further study. In this study, the activity of NanB sialidase was investigated in silico by docking the NanB sialidase of Pasteurella multocida to the Neu5Acα(2-6)Gal ligand. Additionally, some local isolates of Pasteurella multocida, which had the NanB gene were screened, and the proteins were isolated for further testing regarding their activity in hydrolyzing Neu5Acα(2-6)Gal. In silico studies showed that the NanB sialidase possesses an exceptional affinity towards forming a protein-ligand complex with Neu5Acα(2-6)Gal. This was further confirmed by showing that a dose of 0.258 U/ml (100%) NanB sialidase of Pasteurella multocida B018 can hydrolyze up to 44.28% of Neu5Acα(2-6)Gal in chicken red blood cells and 81.95% in rabbit red blood cells. This study suggested that the NanB sialidase of Pasteurella multocida B018 has a potent antiviral activity that can inhibit avian influenza virus infection.


1944 ◽  
Vol 79 (3) ◽  
pp. 301-317 ◽  
Author(s):  
William F. Friedewald ◽  
Edward G. Pickels

A synthetic density gradient technique has been applied to the study of the PR8 and Lee strains of influenza virus in the angle centrifuge. The method counteracted convective disturbances and permitted about a fiftyfold improvement in clearing supernatant fluids of virus. Sedimenting boundaries of infective virus particles, hemagglutinin, and complement-fixing antigen were obtained in the angle centrifuge and correlated with boundaries observed optically in the ultracentrifuge. The sedimentation constant of infective Lee virus particles is approximately 800 Svedberg units, while that of PR8 virus is only about 700. On the assumption of spherical shape, these values correspond to approximate diameters of 85 and 80 mµ respectively. These values agree with those obtained by filtration with graded collodion membranes. The concentration of primary virus particles in untreated allantoic fluid preparations of PR8 or Lee virus is of the order of 0.01 per cent. The primary infective particles are identical with the hemagglutinin and the complement-fixing antigen to a large extent. However, allantoic fluid preparations of PR8 virus also show a slightly inhomogeneous group of particles with an average sedimentation constant of 460 S, which are adsorbed by and eluted from red blood cells yet appear to be non-infective. In addition the virus preparations contain a small amount of "soluble antigen" which sediments more slowly than the virus and is not adsorbed by red blood cells. This soluble antigen is probably associated with material which was observed optically in the ultracentrifuge to sediment at rates ranging from very low values up to that characteristic of the primary virus boundary. This distribution of rate makes it seem likely that the material represents disintegrated virus particles. Calculations based on the experimental results obtained indicate that of the order of 10 influenza virus particles are required to produce infection of chick embryos or mice with the PR8 virus. While a comparable number is required with Lee virus for infection of chick embryos, about 10,000 particles are necessary for infection of mice. The ratio of hemagglutinin to red blood cells required to produce 50 per cent agglutination with dilute virus suspensions in the standard test is roughly 1.


Soft Matter ◽  
2018 ◽  
Vol 14 (30) ◽  
pp. 6278-6289 ◽  
Author(s):  
Masoud Hoore ◽  
François Yaya ◽  
Thomas Podgorski ◽  
Christian Wagner ◽  
Gerhard Gompper ◽  
...  

Red blood cells (RBCs) in plasma or polymer solution interact attractively to form various shapes of RBC doublets. A rich variety of doublet shapes is found, depending on membrane shear and bending elasticity, reduced volumes, and adhesion strength.


1996 ◽  
Vol 104 (10) ◽  
pp. 3774-3781 ◽  
Author(s):  
Ralf Everaers ◽  
Ian S. Graham ◽  
Martin J. Zuckermann ◽  
Erich Sackmann

2000 ◽  
Vol 11 (4) ◽  
pp. 1143-1152 ◽  
Author(s):  
Ruben M. Markosyan ◽  
Fredric S. Cohen ◽  
Grigory B. Melikyan

GPI-linked hemagglutinin (GPI-HA) of influenza virus was thought to induce hemifusion without pore formation. Cells expressing either HA or GPI-HA were bound to red blood cells, and their fusion was compared by patch-clamp capacitance measurements and fluorescence microscopy. It is now shown that under more optimal fusion conditions than have been used previously, GPI-HA is also able to induce fusion pore formation before lipid dye spread, although with fewer pores formed than those induced by HA. The GPI-HA pores did not enlarge substantially, as determined by the inability of a small aqueous dye to pass through them. The presence of 1,1′-dioctadecyl-3,3,3′,3′-tetramethylindocarbocyanine perchlorate or octadecylrhodamine B in red blood cells significantly increased the probability of pore formation by GPI-HA; the dyes affected pore formation to a much lesser degree for HA. This greater sensitivity of pore formation to lipid composition suggests that lipids are a more abundant component of a GPI-HA fusion pore than of an HA pore. The finding that GPI-HA can induce pores indicates that the ectodomain of HA is responsible for all steps up to the initial membrane merger and that the transmembrane domain, although not absolutely required, ensures reliable pore formation and is essential for pore growth. GPI-HA is the minimal unit identified to date that supports fusion to the point of pore formation.


1948 ◽  
Vol 88 (5) ◽  
pp. 503-514 ◽  
Author(s):  
Herbert R. Morgan ◽  
John F. Enders ◽  
Philip F. Wagley

1. A factor capable of causing the hemolysis of the erythrocytes of man, chicken, and sheep occurs in the amniotic and allantoic fluids of chick embryos infected with the virus of mumps. 2. The hemolysin has not been found in normal fluids or in those infected with PR8 or Lee B strains of influenza virus. 3. The hemolysin is definitely inhibited by the serum of man and monkey convalescent from mumps, but only slightly by the serum of the acute phase. 4. The hemolysin is almost completely inactivated at 50°C. after 10 minutes. It exhibits maximal activity at 37°C. and is completely inactive at 4°C. A pH range from about 7.0 to 8.0 allows for maximum activity. 5. Adsorption and elution of the hemolysin with red blood cells has been demonstrated. After elution of the hemolysin, the red blood cells exhibit an increased osmotic fragility. Similar treatment of red cells with influenza virus did not alter this property. 6. The relationship of the hemolysin to the hemagglutinin and the enzyme-like behavior of the former have been discussed.


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