H5N1 chicken influenza viruses display a high binding affinity for Neu5Acα2-3Galβ1-4(6-HSO3)GlcNAc-containing receptors

Gambaryan, Alexandra; Tuzikov, Alexander; Pazynina, Galina V.; Webster, Robert G.; Matrosovich, Mikhail; Bovin, Nicolai V.

doi:10.1016/j.virol.2004.06.002

Cited by 82 publications

(70 citation statements)

References 32 publications

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“…Consistent with our findings, these studies have shown that an H3N2 virus binds to the ciliated cells of the human trachea (52). Complex variations in carbohydrate structures may also contribute to binding of viruses and account for differences in infection of human and avian strains; however, this work is still evolving (14).…”

Section: Discussionsupporting

confidence: 89%

Influenza Virus Receptor Specificity and Cell Tropism in Mouse and Human Airway Epithelial Cells

Ibricevic¹,

Pekosz

Walter³

et al. 2006

J Virol

348

324

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Recent human infections caused by the highly pathogenic avian influenza virus H5N1 strains emphasize an urgent need for assessment of factors that allow viral transmission, replication, and intra-airway spread. Important determinants for virus infection are epithelial cell receptors identified as glycans terminated by an ␣2,3-linked sialic acid (SA) that preferentially bind avian strains and glycans terminated by an ␣2,6-linked SA that bind human strains. The mouse is often used as a model for study of influenza viruses, including recent avian strains; however, the selectivity for infection of specific respiratory cell populations is not well described, and any relationship between receptors in the mouse and human lungs is incompletely understood. Here, using in vitro human and mouse airway epithelial cell models and in vivo mouse infection, we found that the ␣2,3-linked SA receptor was expressed in ciliated airway and type II alveolar epithelial cells and was targeted for cell-specific infection in both species. The ␣2,6-linked SA receptor was not expressed in the mouse, a factor that may contribute to the inability of some human strains to efficiently infect the mouse lung. In human airway epithelial cells, ␣2,6-linked SA was expressed and functional in both ciliated and goblet cells, providing expanded cellular tropism. Differences in receptor and cell-specific expression in these species suggest that differentiated human airway epithelial cell cultures may be superior for evaluation of some human strains, while the mouse can provide a model for studying avian strains that preferentially bind only the ␣2,3-linked SA receptor.

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Section: Discussionsupporting

confidence: 89%

Influenza Virus Receptor Specificity and Cell Tropism in Mouse and Human Airway Epithelial Cells

Ibricevic¹,

Pekosz

Walter³

et al. 2006

J Virol

348

324

View full text Add to dashboard Cite

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“…The strong preference observed for α2,3-linked over α2,6-linked sialosides is in agreement with previously reported results for equine viruses (17). Similarly, the greater avidities of equine viruses for analogs containing sulfated GlcNAc3 residues have been reported before (18)(19)(20). Ef virus binds 3′ sialylactosamine (3′SLN) with about 1/3rd the avidity of Ee and the other three analogs, Sialyl Lewis X (SLe x ), sulfated Sialyl Lewis X (Su-SLe x ), and Su-3′SLN, with about 1/10th the avidity of Ee (Fig.…”

Section: Significancesupporting

confidence: 93%

Recent evolution of equine influenza and the origin of canine influenza

Collins¹,

Vachieri²,

Haire³

et al. 2014

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

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Significance Equine influenza viruses of the H3N8 subtype have caused outbreaks of respiratory disease in horses throughout the world since their discovery in 1963 in Florida. In 2004 an equine virus in circulation was transmitted to dogs and subsequently spread throughout the United States and to Europe. Comparative analyses of the structures of hemagglutinin glycoproteins of equine and canine viruses by X-ray crystallography locate the sites of variation on the molecules, indicate a role in determining binding specificity for an amino acid sequence difference in the receptor binding site, and describe a unique structural difference in the membrane fusion region in recent equine and canine virus HAs by comparison with all other known HAs. These differences are proposed to have facilitated cross-species transfer.

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“…There is evidence that some chicken and mammalian influenza A viruses display a high binding affinity for sulfated sialylglycan receptor, and this binding affinity is decreased after treatment of cells with sulfatase [50]. The presence of sulfated Neu5Ac(α2→6)Gal in CAM and AM cells (1.3% and 3.8%, respectively, Table 1) may facilitate human influenza virus infection of AM cells.…”

Section: Methodsmentioning

confidence: 99%

Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses

et al. 2008

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The initial step essential in influenza virus infection is specific binding of viral hemagglutinin to host cell-surface glycan receptors. Influenza A virus specificity for the host is mediated by viral envelope hemagglutinin, that binds to receptors containing glycans with terminal sialic acids. Human viruses preferentially bind to α2→6 linked sialic acids on receptors of host cells, whereas avian viruses are specific for the α2→3 linkage on the target cells. Human influenza virus isolates more efficiently infect amniotic membrane (AM) cells than chorioallantoic membrane (CAM) cells. N-glycans were isolated from AM and CAM cells of 10-day-old chicken embryonated eggs and their structures were analyzed by multi-dimensional HPLC mapping and MALDI-TOF-MS techniques. Terminal Nacetylneuraminic acid contents in the two cell types were similar. However, molar percents of α2→3 linkage prefer- Glycoconj J (2009) 26:433-443

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H5N1 chicken influenza viruses display a high binding affinity for Neu5Acα2-3Galβ1-4(6-HSO3)GlcNAc-containing receptors

Cited by 82 publications

References 32 publications

Influenza Virus Receptor Specificity and Cell Tropism in Mouse and Human Airway Epithelial Cells

Influenza Virus Receptor Specificity and Cell Tropism in Mouse and Human Airway Epithelial Cells

Recent evolution of equine influenza and the origin of canine influenza

Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses

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