Attachment of Influenza C Virus to Human Erythrocytes

Abstract

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.

Complex signatures of natural selection at GYPA

“…This hypothesis was based on two observations. First, GPA binds multiple infectious agents including viruses and bacteria (Baseman et al 1982; Brooks et al 1989; Nishimura et al 1988; Paul 1987; Saada et al 1991; Tavakkol and Burness 1990; Wybenga et al 1996). Second, the erythrocyte is an optimal decoy because it lacks a nucleus.…”

The in situ distribution of glycoprotein-bound 4-O-Acetylated sialic acids in vertebrates

“…Apart from this, we have so far not been able to identify any common denominator characterizing 4-O-Ac sia positive species. Reports on the cellular distribution of O-Ac sias are scarce, however, Influenza C, which uses 9-O-Ac sias as its cellular receptor [27], has been reported to agglutinate RBCs from a range of species, including humans, mice, rat and chicken [12] suggesting occurrence of this sialic derivative on RBCs. This and the fact that 9-O-Ac sias have been associated with endothelial cells in rat [9] leads us to speculated if the 4-O-Ac sia negative species in the present work contains O-Ac sias at the same location, but with derivatives not detected by our 4-O-Ac sia specific assay.…”

“…Studies demonstrating the distribution of O-Ac sias are few. Most have focused on mucous membranes and mucus producing cells, using biochemical techniques to examine extracts from homogenized organ samples [6][7][8][9][10][11][12][13]. 9-O-Ac sias are commonly found in mammalian species, including in cow (e.g.…”

“…Virus and lectin histochemistry have been used for anatomical studies [22,23], and to identify the cellular distribution of specific sias, such as the receptors for Influenza A and C virus [24,25]. In addition, influenza C virus and ISAV, that both use O-Ac sias as cellular receptors, agglutinate RBCs from a range of species [12,26]. The influenza C virus surface glycoprotein, haemagglutinin-esterase, binds 9-O-Ac sias [27].…”

Characteristics of new Staphylococcus aureus-RBC adhesion mechanism independent of fibrinogen and IgG under hydrodynamic shear conditions

“…RBCs are the most abundant cells in human blood and have been shown to interact with numerous pathogens (2,6,17,21,35,38,43,47,51). These pathogens bind to sugar groups of RBC surface glycoproteins, especially sialic acid residues.…”