Influenza viruses differ in recognition of 4-O-acetyl substitution of sialic acid receptor determinant

Matrosovich, Mikhail; Gambaryan, Alexandra; Chumakov, M. P.

doi:10.1016/0042-6822(92)90541-v

Cited by 24 publications

(20 citation statements)

References 15 publications

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“…Horse serum proteins are enriched in 4-O-acetylated sialic acids, which are well bound by the virus's HA but hydrolyzed poorly by its NA. The virus can successfully escape from this inhibition by increasing the activity of its NA against 4-O-acetylated decoy receptors or decreasing the binding of HA to these receptors, both of which restore the HA-NA balance (18)(19)(20). Our results suggest that changes in the avidity of viral binding to host cells (due to, e.g., changes in the cells' repertoires of glycosylation enzymes) might be another important factor affecting the intricate balance between HA and NA.…”

Section: Discussionmentioning

confidence: 99%

Influenza A virus entry into cells lacking sialylated N-glycans

Vries

Wienholts

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Influenza A virus (IAV) enters host cells after attachment of its hemagglutinin (HA) to surface-exposed sialic acid. Sialylated Nlinked glycans have been reported to be essential for IAV entry [Chu VC, Whittaker GR (2004) Proc Natl Acad Sci USA 102:18153-18158], thereby implicating the requirement for proteinaceous receptors in IAV entry. Here we show, using different N-acetylglucosaminyl transferase 1 (GnT1)-deficient cells, that N-linked sialosides can mediate, but are not required for, entry of IAV. Entry into GnT1-deficient cells was fully dependent on sialic acid. Although macropinocytic entry appeared to be affected by the absence of sialylated N-glycans, dynamin-dependent entry was not affected at all. However, binding of HA to GnT1-deficient cells and subsequent entry of IAV were reduced by the presence of serum, which could be reversed by back-transfection of a GnT1-encoding plasmid. The inhibitory effect of serum was significantly increased by inhibition of the viral receptor-destroying enzyme neuraminidase (NA). Our results indicate that decoy receptors on soluble serum factors compete with cell surface receptors for binding to HA in the absence of sialylated N-glycans at the cell surface. This competition is particularly disturbed by the additional presence of NA inhibitors, resulting in strongly reduced IAV entry. Our results indicate that the balance between HA and NA is important not only for virion release, but also for entry into cells. (IAV) is an enveloped, negative-strand RNA virus that causes respiratory and/or intestinal infections in a variety of animal hosts, including birds and mammals. The IAV envelope contains two glycoproteins: the hemagglutinin (HA) protein, which is responsible for virus cell attachment and fusion, and the neuraminidase (NA) protein, which is the receptordestroying enzyme essential for release of the virus from the host cell after budding. IAV attaches to host cells by binding of HA to sialic acids (SIA) present on the host cell surface. Attachment is followed by entry via endocytic routes delivering the virus to the acidic environment of the late endosome that triggers HA-mediated fusion. The interactions of HA with SIA likely are important determinants not only of attachment, but also of virus uptake, intracellular trafficking, and fusion.Cell surface glycan composition is complex and varies between host and cell type. Sialylated glycans are attached to membrane phospolipids or to membrane proteins via asparagine (N-linked glycans) or serine/threonine (O-linked glycans) residues. How and to what extent binding of IAV to specific sialoglycans determines subsequent endocytosis remains unclear. N-linked glycans have been shown to be required for IAV entry, even though O-linked glycans and/or glycolipids permit efficient sialic acid-dependent binding of IAV to cells devoid of sialylated N-linked glycans (2). Thus, it appears that beyond the well-established requirement for binding to either α2-6 SIAs of human IAVs or α2-3 SIAs of avian IAVs, a specific subset of glyc...

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Section: Discussionmentioning

confidence: 99%

Influenza A virus entry into cells lacking sialylated N-glycans

Vries

Wienholts

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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“…The 4-O-acetyl-substituted Sia has been described in various tissues in mice, especially in the gut; its presence has been documented in a number of other animal species and in trace amounts in humans (34,35). The resistance of 4-O-acetyl-substituted Sia toward neuraminidases from V. cholerae and Clostridium perfringens has previously been described (36,37), but the susceptibility of this Sia form to neuraminidases requires further detailed investigation.…”

Section: Discussionmentioning

confidence: 99%

Members of a Novel Protein Family Containing Microneme Adhesive Repeat Domains Act as Sialic Acid-binding Lectins during Host Cell Invasion by Apicomplexan Parasites

Friedrich

Santos

Liu

et al. 2010

Journal of Biological Chemistry

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Numerous intracellular pathogens exploit cell surface glycoconjugates for host cell recognition and entry. Unlike bacteria and viruses, Toxoplasma gondii and other parasites of the phylum Apicomplexa actively invade host cells, and this process critically depends on adhesins (microneme proteins) released onto the parasite surface from intracellular organelles called micronemes (MIC). The microneme adhesive repeat (MAR) domain of T. gondii MIC1 (TgMIC1) recognizes sialic acid (Sia), a key determinant on the host cell surface for invasion by this pathogen. By complementation and invasion assays, we demonstrate that TgMIC1 is one important player in Sia-dependent invasion and that another novel Sia-binding lectin, designated TgMIC13, is also involved. Using BLAST searches, we identify a family of MAR-containing proteins in enteroparasitic coccidians, a subclass of apicomplexans, including T. gondii, suggesting that all these parasites exploit sialylated glycoconjugates on host cells as determinants for enteric invasion. Furthermore, this protein family might provide a basis for the broad host cell range observed for coccidians that form tissue cysts during chronic infection. Carbohydrate microarray analyses, corroborated by structural considerations, show that TgMIC13, TgMIC1, and its homologue Neospora caninum MIC1 (NcMIC1) share a preference for ␣2-3-over ␣2-6-linked sialyl-N-acetyllactosamine sequences. However, the three lectins also display differences in binding preferences. Intense binding of TgMIC13 to ␣2-9-linked disialyl sequence reported on embryonal cells and relatively strong binding to 4-O-acetylated-Sia found on gut epithelium and binding of NcMIC1 to 6sulfo-sialyl Lewis x might have implications for tissue tropism. Sialic acids (Sias)6 occur abundantly in glycoproteins and glycolipids on the cell surface and are exploited by many viruses and bacteria for attachment and host cell entry. Recognition of carbohydrates and in particular sialylated glycoconjugates is important also for host cell invasion by the Apicomplexa (1-4), a phylum that includes several thousand species of obligate intracellular parasites, among them the Plasmodium spp. causing malaria. Enteroparasitic coccidians are a subclass of Apicomplexa comprising Eimeria spp. responsible for coccidiosis in poultry, Neospora spp. causing neosporosis in cattle, and Toxoplasma, the causative agent of toxoplasmosis in warmblooded animals and humans.The host range and cell type targeted by these parasites vary widely across the phylum. Whereas Plasmodium falciparum merozoites exclusively invade erythrocytes of humans and great apes (5), Toxoplasma gondii tachyzoites (the form of the parasite associated with acute infection) invade an extremely broad range of cell types in humans and virtually all warmblooded animals, enabling rapid establishment of infection in the host and dissemination into deep tissues (6). Information is emerging on the involvement of carbohydrate-protein interactions in this broad host cell recognition (1).Many intracellular...

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“…Typically, H3 subtype viruses mainly interact with the terminal Neu5Ac moiety of 6 0 SLN, whereas H1 strains and type B viruses, in addition to binding to Neu5Ac, bind to GlcNAc and Gal residues, respectively [13,22,25]. In contrast to generally good binding of human influenza viruses to 6 0 SLN, a much higher variation has been observed in the virus recognition of other sialic acid species, such as Neu5Gc or Neu4,5Ac 2 , as well as of synthetic sialic acid analogues [22,[25][26]. A lack of such sialosides in humans suggests that this variation is either incidental or reflects differences in the evolution of human virus precursors in their animal hosts.…”

Section: Influenza Virus Ha and Its Cellular Receptorsmentioning

confidence: 99%

Natural and synthetic sialic acid‐containing inhibitors of influenza virus receptor binding

Matrosovich

Klenk²

2003

Reviews in Medical Virology

137

120

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Influenza viruses attach to susceptible cells via multivalent interactions of their haemagglutinins with sialyloligosaccharide moieties of cellular glycoconjugates. Soluble macromolecules containing sialic acid from animal sera and mucosal fluids can act as decoy receptors and competitively inhibit virus-mediated haemagglutination and infection. Although a role for these natural inhibitors in the innate anti-influenza immunity is still not clear, studies are in progress on the design of synthetic sialic acid-containing inhibitors of receptor binding which could be used as anti-influenza drugs.

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Influenza viruses differ in recognition of 4-O-acetyl substitution of sialic acid receptor determinant

Cited by 24 publications

References 15 publications

Influenza A virus entry into cells lacking sialylated N-glycans

Influenza A virus entry into cells lacking sialylated N-glycans

Members of a Novel Protein Family Containing Microneme Adhesive Repeat Domains Act as Sialic Acid-binding Lectins during Host Cell Invasion by Apicomplexan Parasites

Natural and synthetic sialic acid‐containing inhibitors of influenza virus receptor binding

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