Polymer-bound 6′ sialyl-N-acetyllactosamine protects mice infected by influenza virus

Gambaryan, Alexandra; Boravleva, Elizaveta; Matrosovich, Tatyana; Matrosovich, Mikhail; Klenk, Hans‐Dieter; Моисеева, Е. В.; Tuzikov, Alexander; Chinarev, Alexander; Pazynina, Galina V.; Bovin, Nicolai V.

doi:10.1016/j.antiviral.2005.07.008

Cited by 54 publications

(44 citation statements)

References 36 publications

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“…One study suggested that the mouse lung was preferentially infected by virus strains that bind the ␣2,6-type receptor (13), while another showed that the ␣2,6-type receptor was absent, based on SNA binding (11). Our finding that ␣2,3-linked SA is the only influenza virus receptor in the mouse lung was supported by the use of epithelial cellspecific markers, lectin binding, and functional studies in relevant in vitro and in vivo mouse models.…”

Section: Discussionsupporting

confidence: 61%

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

Ibricevic¹,

Pekosz

Walter³

et al. 2006

J Virol

347

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: 61%

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

Ibricevic¹,

Pekosz

Walter³

et al. 2006

J Virol

347

324

View full text Add to dashboard Cite

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“…Analogously, administration of the probe in conjugation with a nonblocking anti-CD22 Ab, may further increase the rate of internalization of the probe and result in greater B cell killing. Although the polyacrylamide backbone is nontoxic in vivo (72,73), other carrier backbones with the sugar derivative presented in high valency may prove more useful in therapeutic applications. Because other siglecs are expressed in many leukocyte types (e.g., NK cells, macrophages, dendritic cells, eosinophils), and several siglecs have been demonstrated to mediate endocytosis (1)(2)(3)61), it will be of interest to see whether analogous high-affinity ligands of other siglecs can be produced to carry ligand-based payloads into other cell types.…”

Section: Discussionmentioning

confidence: 99%

High-Affinity Ligand Probes of CD22 Overcome the Threshold Set by cis Ligands to Allow for Binding, Endocytosis, and Killing of B Cells

Collins

Blixt

Han

et al. 2006

The Journal of Immunology

146

212

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CD22 (Siglec-2) is a key regulator of B cell signaling whose function is modulated by interaction with extracellular glycan ligands mediated through its N-terminal Ig domain. Its preferred ligand is the sequence Siaα2-6Gal that is abundantly expressed on N-linked glycans of B cell glycoproteins, and by binding to CD22 in cis causes CD22 to appear “masked” from binding to synthetic sialoside probes. Yet, despite the presence of cis ligands, CD22 redistributes to sites of cell contact by binding to trans ligands on neighboring cells. In this study, we demonstrate the dynamic equilibrium that exists between CD22 and its cis and trans ligands, using a high-affinity multivalent sialoside probe that competes with cis ligands and binds to CD22 on native human and murine B cells. Consistent with the constitutive endocytosis reported for CD22, the probes are internalized once bound, demonstrating that CD22 is an endocytic receptor that can carry ligand-decorated “cargo” to intracellular compartments. Conjugation of the sialoside probes to the toxin saporin resulted in toxin uptake and toxin-mediated killing of B lymphoma cell lines, suggesting an alternative approach for targeting CD22 for treatment of B cell lymphomas.

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“…For example, human H3N2 clinical specimens can be the source of different sequence variants when propagated in MDCK cells or in embryonated eggs (17). Similarly, classical swine H1N1 viruses isolated in eggs have changes at positions 187 and/or 222 and modulate their receptor specificity (4,18).…”

Section: Discussionmentioning

confidence: 99%

Substitution in position 222 of haemagglutinin of pandemic influenza A (H1N1) viruses isolated from pigs in Poland

Kowalczyk

Urbaniak

Markowska-Daniel

et al. 2015

Bulletin of the Veterinary Institute in Pulawy

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The aim of the study was to monitor genetic diversity and antigenic changes in the genome of influenza A(H1N1)pdm09 viral isolates detected during the post-pandemic period in Poland. Clinical specimens obtained from three suspected cases of influenza were analysed by sequencing. Among the differences identified in amino acids sequences, nine substitutions were located within the antigenic HA1 sites and in five residues forming receptor-binding pocket. The HA(D222G) mutation was shown in the isolate Swine/Poland/134312/12 obtained from a mild case of the disease. It must be emphasized that, in general, clinically mild cases are caused by the viruses in which that specific mutation, i.e. haemagglutinin (D222G), does not occur.

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Polymer-bound 6′ sialyl-N-acetyllactosamine protects mice infected by influenza virus

Cited by 54 publications

References 36 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

High-Affinity Ligand Probes of CD22 Overcome the Threshold Set by cis Ligands to Allow for Binding, Endocytosis, and Killing of B Cells

Substitution in position 222 of haemagglutinin of pandemic influenza A (H1N1) viruses isolated from pigs in Poland

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