Hæmagglutinin From Rotavirus

Spence, L.; Fauvel, M.; Petro, R.; Bloch, S.

doi:10.1016/s0140-6736(76)90860-6

Cited by 25 publications

(9 citation statements)

References 6 publications

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“…The recognition that sialic acids play an important role during rotavirus entry comes from early studies in which some strains had hemagglutination activity of red blood cells and neuraminidase treatment of cells reduced virus binding and infection of some strains (e.g., [140–144]). In general, the easily culturable animal rotaviruses bound to host cells in a neuraminidase-sensitive manner while human rotaviruses did not [145].…”

Section: Discussionmentioning

confidence: 99%

Glycosphingolipids as Receptors for Non-Enveloped Viruses

Taube

Jiang

Wobus

2010

Viruses

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Glycosphingolipids are ubiquitous molecules composed of a lipid and a carbohydrate moiety. Their main functions are as antigen/toxin receptors, in cell adhesion/recognition processes, or initiation/modulation of signal transduction pathways. Microbes take advantage of the different carbohydrate structures displayed on a specific cell surface for attachment during infection. For some viruses, such as the polyomaviruses, binding to gangliosides determines the internalization pathway into cells. For others, the interaction between microbe and carbohydrate can be a critical determinant for host susceptibility. In this review, we summarize the role of glycosphingolipids as receptors for members of the non-enveloped calici-, rota-, polyoma- and parvovirus families.

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Section: Discussionmentioning

confidence: 99%

Glycosphingolipids as Receptors for Non-Enveloped Viruses

Taube

Jiang

Wobus

2010

Viruses

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“…Soon after their discovery, it was found that rotaviruses were able to agglutinate human type O erythrocytes [16], and in a short period of time this observation was extended to several other rotavirus strains of animal and human origin [17][18][19][20]. However, despite the original reports of hemagglutination by human rotavirus strains [19,20], these observations were not confirmed, and further studies showed that human rotavirus isolates were only able to agglutinate fixed, one-day old chicken erythrocytes, and that this activity was abolished by trypsin treatment of the viruses [21].…”

Section: Introductionmentioning

confidence: 99%

Role of sialic acids in rotavirus infection

2006

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Rotaviruses are the leading cause of childhood diarrhea. The entry of rotaviruses into the host cell is a complex process that includes several interactions of the outer layer proteins of the virus with different cell surface molecules. The fact that neuraminidase treatment of the cells, or preincubation of the virus with sialic acid-containing compounds decrease the infectivity of some rotavirus strains, suggested that these viruses interact with sialic acid on the cell surface. The infectivity of some other rotavirus strains is not affected by neuraminidase treatment of the cells, and therefore they are considered neuraminidase-resistant. However, the current evidence suggests that even these neuraminidase-resistant strains might interact with sialic acids located in context different from that of the sialic acids used by the neuraminidase-sensitive strains. This review summarizes our current knowledge of the rotavirus-sialic acid interaction, its structural basis, the specificity with which distinct rotavirus isolates interact with sialic acid-containing compounds, and also the potential use of these compounds as therapeutic agents.

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“…For this work, cell culture-adapted rotaviruses of calf (BDV 486) (Spence et al, 1976), simian (SA11) (Malherbe & Strickland-Cholmley, 1967) and human (Wa) (Wyatt et al, 1980) origin were used. In addition, a rotavirus (82-124) passaged in a calf by L. Babiuk was employed to compare gut-derived with culture-grown virus.…”

mentioning

confidence: 99%

Comparison of Bovine, Simian and Human Rotavirus Structural Glycoproteins

Kouvelos¹,

Petric²,

Middleton³

1984

Journal of General Virology

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SUMMARYThe structural glycoproteins of calf (BDV 486), human (Wa) and Simian (SAIl) rotaviruses were compared for sensitivity to endoglycosidase (Endo) H. The calf and human virus glycoproteins were reduced by approximately 5000 molecular weight in two equal stages. The simian rotavirus glycoprotein sustained only one 2500 molecular weight decrease. The effect of the host cell on the viral oligosaccharide composition was examined. Endo H digests of calf rotavirus 82-124 extracted from stool and its progeny propagated and [35S]methionine-labelled in MA104 cells were compared. Endo H had the same effects on the glycoproteins, indicating that the nature of the host cell does not affect the oligosaccharide composition of the virus glycoproteins.

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Hæmagglutinin From Rotavirus

Cited by 25 publications

References 6 publications

Glycosphingolipids as Receptors for Non-Enveloped Viruses

Glycosphingolipids as Receptors for Non-Enveloped Viruses

Role of sialic acids in rotavirus infection

Comparison of Bovine, Simian and Human Rotavirus Structural Glycoproteins

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