Sialic Acid Dependence and Independence of Group A Rotaviruses

Kuhlenschmidt, Theresa B.; Hanafin, William P.; Gelberg, Howard B.; Kuhlenschmidt, Mark S.

doi:10.1007/978-1-4615-4143-1_33

Cited by 20 publications

(58 citation statements)

References 10 publications

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“…In the previous studies, the viral particles were purified by metrizamide gradients rather than CsCl gradients. However, CsCl gradients give better separation of DLP and TLP than metrizamide gradients (13,42). A probable substantial DLP contamination in their TLP preparation might account for the strong GA1 and GA2 binding.…”

Section: Discussionmentioning

confidence: 99%

“…Other studies with rhesus rotavirus showed binding to a glycoprotein on murine enterocytes, with O-linked sialic acid residues being required for virus binding (2). It has recently been suggested that gangliosides are also involved in infection by the so-called neuraminidase-insensitive human rotaviruses (24,42). To clarify these conflicting results, the glycosphingolipid binding specificities of two neuraminidase-sensitive (simian SA11, bovine NCDV) and one neuraminidase-insensitive (bovine UK) rotavirus strain were investigated using the TLC binding assay (26,38,39).…”

mentioning

confidence: 99%

“…The chemical nature of the rotavirus receptors is a topical area of rotavirus research, but no consensus has yet emerged (2,24,42,53,54). For example, infection of cell culture by the simian rotavirus strain SA11 is neuraminidase sensitive, suggesting the involvement of sialic acid on the cell surface in the infection process (14,19).…”

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confidence: 99%

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Glycosphingolipid Binding Specificities of Rotavirus: Identification of a Sialic Acid-Binding Epitope

Delorme

Brüssow

Sidoti

et al. 2001

J Virol

127

143

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The glycosphingolipid binding specificities of neuraminidase-sensitive (simian SA11 and bovine NCDV) and neuraminidase-insensitive (bovine UK) rotavirus strains were investigated using the thin-layer chromatogram binding assay. Both triple-layered and double-layered viral particles of SA11, NCDV, and UK bound to nonacid glycosphingolipids, including gangliotetraosylceramide (GA1; also called asialo-GM1) and gangliotriaosylceramide (GA2; also called asialo-GM2). Binding to gangliosides was observed with triple-layered particles but not with double-layered particles. The neuraminidase-sensitive and neuraminidase-insensitive rotavirus strains showed distinct ganglioside binding specificities. All three strains bound to sialylneolactotetraosylceramide and GM2 and GD1a gangliosides. However, NeuAc-GM3 and the GM1 ganglioside were recognized by rotavirus strain UK but not by strains SA11 and NCDV. Conversely, NeuGc-GM3 was bound by rotaviruses SA11 and NCDV but not by rotavirus UK. Thus, neuraminidase-sensitive strains bind to external sialic acid residues in gangliosides, while neuraminidase-insensitive strains recognize gangliosides with internal sialic acids, which are resistant to neuraminidase treatment. By testing a panel of gangliosides with triple-layered particles of SA11 and NCDV, the terminal sequence sialyl-galactose (NeuGc/NeuAc␣3-Gal␤) was identified as the minimal structural element required for the binding of these strains. The binding of triple-layered particles of SA11 and NCDV to NeuGc-GM3, but not to NeuAc-GM3, suggested that the sequence NeuGc␣3Gal␤ is preferred to NeuAc␣3Gal␤. Further dissection of this binding epitope showed that the carboxyl group and glycerol side chain of sialic acid played an important role in the binding of such triple-layered particles.

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Section: Discussionmentioning

confidence: 99%

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Glycosphingolipid Binding Specificities of Rotavirus: Identification of a Sialic Acid-Binding Epitope

Delorme

Brüssow

Sidoti

et al. 2001

J Virol

127

143

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“…Rotavirus entry into a host cell is a complex process using interactions with surface molecules as the initial basis for viral attachment (2,22). Sialic acid residues on cell-surface glycoproteins and other proteins may contribute to the mechanistic basis for how RRV infects a cholangiocyte (7,20). In Fig.…”

Section: Discussionmentioning

confidence: 99%

Cholangiocyte expression of α₂β₁-integrin confers susceptibility to rotavirus-induced experimental biliary atresia

Jafri¹,

Donnelly²,

Allen³

et al. 2008

American Journal of Physiology-Gastrointestinal and Liver Physi

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lation of BALB/c mice with rhesus rotavirus (RRV) in the newborn period results in biliary epithelial cell (cholangiocyte) infection and the murine model of biliary atresia. Rotavirus infection of a cell requires attachment, which is governed in part by cell-surface expression of integrins such as ␣2␤1. We hypothesized that cholangiocytes were susceptible to RRV infection because they express ␣2␤1. RRV attachment and replication was measured in cell lines derived from cholangiocytes and hepatocytes. Flow cytometry was performed on these cell lines to determine whether ␣2␤1 was present. Cholangiocytes were blocked with natural ligands, a monoclonal antibody, or small interfering RNA against the ␣2-subunit and were infected with RRV. The extrahepatic biliary tract of newborn mice was screened for the expression of the ␣2␤1-integrin. Newborn mice were pretreated with a monoclonal antibody against the ␣2-subunit and were inoculated with RRV. RRV attached and replicated significantly better in cholangiocytes than in hepatocytes. Cholangiocytes, but not hepatocytes, expressed ␣2␤1 in vitro and in vivo. Blocking assays led to a significant reduction in attachment and yield of virus in RRV-infected cholangiocytes. Pretreatment of newborn pups with an anti-␣2 monoclonal antibody reduced the ability of RRV to cause biliary atresia in mice. Cell-surface expression of the ␣2␤1-integrin plays a role in the mechanism that confers cholangiocyte susceptibility to RRV infection. rhesus rotavirus; bile ducts; cholangiopathy BILIARY ATRESIA (BA) is a unique disease of infancy in which affected children develop fibroinflammatory obliteration of the biliary tract. It is the most common indication for pediatric liver transplantation (24). Because pathogenic viruses have been found in the livers of children afflicted with biliary atresia (10,12,18,26,29), a proposed etiology for biliary atresia is perinatal infection by a virus triggering inflammatory destruction of the biliary epithelium (3,23,32). A murine model of biliary atresia (30) supports a viral pathogenesis where newborn mice infected with rhesus rotavirus (RRV) develop inflammation within the portal tract (31) and extrahepatic bile duct obstruction (9, 27).Recently, it has been shown that in the murine model of biliary atresia, RRV targeted the biliary epithelial cell (cholangiocyte) for infection (1, 31). To determine the basis for cholangiocyte susceptibility to RRV, an in vitro model of RRV infection of the two dominant cell types found within the liver (cholangiocytes and hepatocytes) was established. Consistent with the in vivo findings, RRV was better able to replicate in cholangiocytes than hepatocytes. Because the ability of rotavirus to infect cells appears to be regulated by cell-surface expression of the integrins ␣ 2 ␤ 1 , ␣ 4 ␤ 1 , ␣ v ␤ 3 , and ␣ x ␤ 2 , which serve as viral receptors (8,13,14,16,21), the cholangiocyte was surveyed for integrin expression and found to uniquely express the ␣ 2 ␤ 1 -integrin when compared with hepatocytes. Based on this informat...

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“…The specificity of rotavirus for sialic acid-containing oligosaccharides and sialylmimetics has been examined by using small molecules as competitors of hemagglutination, infection, or binding to cells (15,22,24,27,37,44). The low affinity of rotavirus for monovalent sialosides complicates this approach.…”

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confidence: 99%

Specificity and Affinity of Sialic Acid Binding by the Rhesus Rotavirus VP8* Core

Dormitzer

Sun²,

Blixt³

et al. 2002

J Virol

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Nuclear magnetic resonance spectroscopy demonstrates that the rhesus rotavirus hemagglutinin specifically binds ␣-anomeric N-acetylneuraminic acid with a K d of 1.2 mM. The hemagglutinin requires no additional carbohydrate moieties for binding, does not distinguish 3 from 6 sialyllactose, and has approximately tenfold lower affinity for N-glycolylneuraminic than for N-acetylneuraminic acid. The broad specificity and low affinity of sialic acid binding by the rotavirus hemagglutinin are consistent with this interaction mediating initial cell attachment prior to the interactions that determine host range and cell type specificity.Rotavirus causes approximately 600,000 childhood deaths through dehydrating diarrhea annually (43) and is also an important veterinary pathogen. Understanding early events in cell entry by rotavirus could aid in the development of therapeutic and preventive measures against rotavirus and could help explain the host range and cell type specificity of the virus.

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Sialic Acid Dependence and Independence of Group A Rotaviruses

Cited by 20 publications

References 10 publications

Glycosphingolipid Binding Specificities of Rotavirus: Identification of a Sialic Acid-Binding Epitope

Glycosphingolipid Binding Specificities of Rotavirus: Identification of a Sialic Acid-Binding Epitope

Cholangiocyte expression of α₂β₁-integrin confers susceptibility to rotavirus-induced experimental biliary atresia

Specificity and Affinity of Sialic Acid Binding by the Rhesus Rotavirus VP8* Core

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Sialic Acid Dependence and Independence of Group A Rotaviruses

Cited by 20 publications

References 10 publications

Glycosphingolipid Binding Specificities of Rotavirus: Identification of a Sialic Acid-Binding Epitope

Glycosphingolipid Binding Specificities of Rotavirus: Identification of a Sialic Acid-Binding Epitope

Cholangiocyte expression of α2β1-integrin confers susceptibility to rotavirus-induced experimental biliary atresia

Specificity and Affinity of Sialic Acid Binding by the Rhesus Rotavirus VP8* Core

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Cholangiocyte expression of α₂β₁-integrin confers susceptibility to rotavirus-induced experimental biliary atresia