The influenza c virus glycoprotein (HE) exhibits receptor-binding (hemagglutinin) and receptor-destroying (esterase) activities

Vlasak, Reinhard; Krystal, Mark; Nacht, Mariana; Palese, Peter

doi:10.1016/0042-6822(87)90013-4

Cited by 125 publications

(131 citation statements)

References 33 publications

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“…The HEF esterase activity was determined by incubation of transfected cells with pNPA at room temperature as described previously (Vlasak et al, 1987). Hydrolysis of this substrate was monitored by measuring the increase in optical density at 405 nm.…”

Section: Sds-page and Western Blottingmentioning

confidence: 99%

The cytoplasmic tail of the influenza C virus glycoprotein HEF negatively affects transport to the cell surface.

Oeffner¹,

Klenk²,

Herrler³

1999

Journal of General Virology

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Section: Sds-page and Western Blottingmentioning

confidence: 99%

The cytoplasmic tail of the influenza C virus glycoprotein HEF negatively affects transport to the cell surface.

Oeffner¹,

Klenk²,

Herrler³

1999

Journal of General Virology

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“…This glycoprotein, recently designated HE (Vlasak et al, 1987), possesses both receptor-binding and receptor-destroying activities (Sugawara et al, 1985;Vlasak et al, 1987). The nature of the cellular receptor for influenza C virus as well as of the receptor-destroying enzyme (RDE) of the virus remained unclear for a long time.…”

Section: Introductionmentioning

confidence: 99%

Attachment of Influenza C Virus to Human Erythrocytes

Nishimura

Sugawara²,

Kitame³

et al. 1988

Journal of General Virology

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SUMMARYBinding experiments with radioactively labelled influenza C virions were carried out to investigate the interaction of the virus with human erythrocytes. The erythrocytes from any of 35 different individuals were found to contain influenza C virus-binding sites though their number was variable among the individuals and was much less than that on mouse, rat and chicken erythrocytes. Attachment of influenza C virus to human erythrocytes was inhibited completely by prior treatment of the virus with anti-HE monoclonal antibody having a strong haemagglutination inhibition activity. Pretreatment of erythrocytes with neuraminidase or the neuraminate-O-acetylesterase of influenza C virus resulted in a marked reduction in the level of virus binding. Thus it appears that human erythrocytes have a low level of O-acetylated sialic acid-containing glycoconjugates that can interact specifically with the HE glycoprotein of influenza C virus. Proteolytic digestion of erythrocytes with ficin, bromelain or V-8 protease inhibited virus binding almost completely, suggesting that the erythrocyte receptor for influenza C virus is a glycoprotein. In contrast to these enzymes, trypsin treatment of erythrocytes reduced virus binding by only about 50~, and ~-chymotrypsin treatment did not inhibit at all. It was also found that treatment of erythrocytes with monoclonal antibody to the M or N blood group antigen greatly inhibited virus binding to the cells. These results, taken together, suggest that most influenza C virus receptors on human erythrocytes, if not all, reside on glycophorin A which is known to possess the M or N blood group activity.

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“…Influenza C virus contains five internal non-glycosylated proteins including three P proteins (P1, P2, P3), nucleoprotein (NP) and matrix (M) protein in addition to a single surface glycoprotein, haemagglutinin-esterase (HE) (Compans et al, 1977;Petri et al, 1980;Vlasak et al, 1987). Earlier serological studies with polyclonal antiviral sera showed that influenza C virus strains isolated over a long period in different parts of the world were highly cross-reactive in haemagglutination inhibition tests (Chakraverty, 1978;Meier-Ewert et al, 1981 ;Kawamura et al, 1986), suggesting that the antigenicity of HE is much more stable than that of the surface glycoproteins of influenza A and B viruses.…”

Section: Introductionmentioning

confidence: 99%

Antigenic Characterization of the Nucleoprotein and Matrix Protein of Influenza C Virus with Monoclonal Antibodies

Sugawara

Nishimura

Hongō

et al. 1991

Journal of General Virology

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Monoclonal antibodies against the nucleoprotein (NP) and matrix (M) protein of influenza C virus were prepared and characterized. At least two non-overlapping or partially overlapping antigenic sites were delineated on each of the proteins by competitive binding assays. Western blot analysis showed that two antigenic sites on the M protein were highly resistant to conformational changes whereas two sites on NP were sensitive. No antigenic variation was seen in either the NP or the M protein when the reactivity of monoclonal antibodies with 23 different influenza C strain s isolated over a 41 year period was studied by radioimmunoprecipitation and enzyme-linked immunosorbent assay. Immunofluorescence analysis with the monoclonal antibodies revealed that both the NP and M proteins migrated to the cell nucleus during the replication cycle of influenza C virus.

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The influenza c virus glycoprotein (HE) exhibits receptor-binding (hemagglutinin) and receptor-destroying (esterase) activities

Cited by 125 publications

References 33 publications

The cytoplasmic tail of the influenza C virus glycoprotein HEF negatively affects transport to the cell surface.

The cytoplasmic tail of the influenza C virus glycoprotein HEF negatively affects transport to the cell surface.

Attachment of Influenza C Virus to Human Erythrocytes

Antigenic Characterization of the Nucleoprotein and Matrix Protein of Influenza C Virus with Monoclonal Antibodies

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