Comparison of human, simian, and bovine rotaviruses for requirement of sialic acid in hemagglutination and cell adsorption

Fukudome, Kenji; Yoshie, Osamu; Konno, Tasuke

doi:10.1016/0042-6822(89)90121-9

Cited by 111 publications

(146 citation statements)

References 40 publications

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“…Prior studies have shown that neuraminidase treatment of MA-104 cells reduces the infectivity of RRV up to 90 % (Fukudome et al, 1989 ;Keljo & Smith, 1988 ;Ludert et al, 1996), while the infectivity of the 0001-5176 # 1998 SGM HCF human strains is unaffected (Fukudome et al, 1989 ;Ludert et al, 1996). The infectivity of the reassortant strains in neuraminidase-treated MA-104 cells was tested using an assay described previously (Ludert et al, 1996).…”

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confidence: 99%

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Identification of mutations in the rotavirus protein VP4 that alter sialic-acid-dependent infection.

Ludert

Mason²,

Ángel

et al. 1998

Journal of General Virology

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To explore further the role of VP4 as the rotavirus cell attachment protein, VP7 monoreassortants derived from the sialic-acid-dependent simian strain RRV and from the sialic-acid-independent human strains D, DS-1 and ST-3 were tested for susceptibility of infectivity of neuraminidasetreated MA-104 cells. Infectivity of RRViD VP7 and RRViST-3 VP7 monoreassortants decreased when sialic acid was removed from the cell surface. However, of three separate RRViDS-1 VP7 monoreassortants tested, only one was sialic-aciddependent. Sequence analysis showed that both sialic-acid-independent strains contained a single amino acid change, Lys to Arg, at position 187. In addition, sialic-acid-independent infectivity was seen in one of 14 RRV VP4 neutralization escape mutants tested, and this strain was found to have a Gly to Glu change at amino acid position 150. These results indicate that positions 150 and 187 of VP4 play an important role in early rotavirus-cell interactions.The rotavirus virion is composed of three concentric layers of proteins and 11 segments of double-stranded RNA (Both et al., 1994 ;Estes, 1996). The outermost layer of the virion is comprised of two proteins, VP4 and VP7. VP4 forms dimeric spikes that project from the surface of the virion, which is constituted by VP7 (Shaw et al., 1993 ;Yeager et al., 1994).

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confidence: 99%

“…While most animal rotaviruses require the presence of sialic acid on the cell surface for efficient binding and infectivity, this is not true of the human rotaviruses, nor of a few animal isolates (Fukudome et al, 1989 ;Keljo & Smith, 1988 ;Superti & Donelli, 1991 ;Rolsma et al, 1994). Me!…”

mentioning

confidence: 99%

Identification of mutations in the rotavirus protein VP4 that alter sialic-acid-dependent infection.

Ludert

Mason²,

Ángel

et al. 1998

Journal of General Virology

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“…Sialylated compounds at the cell surface have been pointed out as critical for the binding of several viruses including RV. In fact, the presence of these compounds was shown to be essential for binding and hemagglutin activity for RV (SA-11 and bovine strain), however, it was not true for Wa, KUN and MO strains of human RV (Fukudome et al, 1989). Similarly, Méndez et al (1993) demonstrated that sialic acid was not necessary for the infectivity of certain mutant strains of RV in MA-104 cells.…”

Section: Discussionmentioning

confidence: 98%

The effect of concanavalin A on the replication of rotavirus (SA-11) in cell culture

Hasenack

Botelho

Lauretti

et al. 2002

Braz. arch. biol. technol.

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“…These interactions have been shown to depend on the presence of sialic acid (SA) on the cell (Fukudome et al, 1989 ;Keljo & Smith, 1988 ;Yolken et al, 1987). In contrast, human rotaviruses do not have HA activity and do not require SA to infect the cells.…”

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confidence: 99%

A new cysteine in rotavirus VP4 participates in the formation of an alternate disulfide bond.

Cuadras

Méndez²,

Arias³

et al. 1998

Journal of General Virology

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Most animal rotaviruses bind to a cell surface molecule that contains sialic acid (SA). We have recently isolated variants from simian rotavirus RRV which show an SA-independent phenotype. The VP4 protein of these variants was shown to have three amino acid changes with respect to the wt protein, one of them being Tyr-267 Cys. In this work, we have investigated whether the new cysteine could interfere with the disulfide bond (Cys-318/Cys-380) present in the VP5* subunit of the wt protein. Cysteine residues 318 and 380 were mutagenized in gpr8 and RRV VP4 genes, and the wt and mutant genes were transcribed and translated in vitro. The protein products were analysed by electrophoresis under reducing and non-reducing conditions. This approach showed that, in the VP4 protein synthesized in vitro, Cys-267 is capable of forming an alternate disulfide bond with Cys-318. This alternate bond also seems to occur in the VP4 protein present in the variant gpr8 virus particles.

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Comparison of human, simian, and bovine rotaviruses for requirement of sialic acid in hemagglutination and cell adsorption

Cited by 111 publications

References 40 publications

Identification of mutations in the rotavirus protein VP4 that alter sialic-acid-dependent infection.

Identification of mutations in the rotavirus protein VP4 that alter sialic-acid-dependent infection.

The effect of concanavalin A on the replication of rotavirus (SA-11) in cell culture

A new cysteine in rotavirus VP4 participates in the formation of an alternate disulfide bond.

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