Isolation and structural analysis of influenza C virion glycoproteins

Herrler, Georg; Nagele, Arno; Meier-Ewert, Herbert; Bhown, Ajit S.; Compans, Richard W.

doi:10.1016/0042-6822(81)90173-2

Cited by 75 publications

(47 citation statements)

References 36 publications

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“…In contrast to influenza A and B viruses which contain two distinct glycoproteins, haemagglutinin and neuraminidase, influenza C virions have only a single type of glycoprotein on their surface (Herrler et al, 1979(Herrler et al, , 1981Sugawara et al, 1981). 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).…”

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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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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“…Influenza A, influenza C, and two paramyxoviruses have been found to selectively bud from the apical surface of polarized cells (12,21,25), whereas the basolateral surface is the preferred site of maturation for vesicular stomatitis virus (VSV) (21) and several retroviruses (27). The maturation sites reflect the sites of insertion of the respective viral glycoproteins (11,20).…”

mentioning

confidence: 99%

Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells.

Jones¹,

Compans²,

Davis³

et al. 1985

Mol. Cell. Biol.

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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 (i) the NA polypeptide contains structural features capable of directing the transport of the protein to apical cell surfaces and (ii) the first 10 amino-terminal residues of the NA polypeptide are not involved in this process.

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“…In contrast, only a single type of glycoprotein, gp88, has been identified in influenza C virions (1), which leads one to postulate that this glycoprotein possesses the receptor-binding activity, a penetration function and the receptor-destroying activity. Herrler et al (10) have detected HA activity in purified preparations of gp88. We have also observed that some of the monoclonal antibodies raised against gp88 are able to inhibit efficiently the HA activity of influenza C virus (Sugawara et al, unpublished observations).…”

Section: Discussionmentioning

confidence: 99%

“…Only a single type of glycoprotein designated gp88 has been detected on the surface of influenza C virions (8,10,28). It therefore appears likely that the RDE of influenza C virus is associated with this glycoprotein, as are the hemagglutinating and cell-fusing activities (1).…”

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confidence: 99%

An Assay for the Receptor‐Destroying Activity of Influenza C Virus

Sugawara

Kitame

Homma

et al. 1985

Microbiology and Immunology

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We have developed a convenient method for assaying the receptordestroying enzyme (RDE) activity of influenza C virus. This method measures the ability of the RDE to destroy the hemagglutination-inhibition activity of a potent inhibitor present in rat serum. Some physico-chemical properties of the RDE of influenza C virus were investigated by using this method. The temperature optimum for maximal activity of this enzyme was found to be 45 C to 53 C. There was little difference in thermostability between the RDE and hemagglutinating activities of influenza C virus. When influenza C virions were treated with various concentrations of trypsin, the RDE activity decreased in parallel with the decrease in the amount of residual gp88 glycoprotein, suggesting association of RDE with this glycoprotein.

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Isolation and structural analysis of influenza C virion glycoproteins

Cited by 75 publications

References 36 publications

Attachment of Influenza C Virus to Human Erythrocytes

Attachment of Influenza C Virus to Human Erythrocytes

Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells.

An Assay for the Receptor‐Destroying Activity of Influenza C Virus

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