Defective mutant of Sindbis virus with a smaller-molecular-weight form of the E1 glycoprotein

Leone, Arturo; Colantuoni, Vittorio; Pontarelli, Gianfranco; Cancedda, Ranieri

doi:10.1128/jvi.34.3.598-603.1980

Cited by 9 publications

(3 citation statements)

References 26 publications

(17 reference statements)

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“…CeUl culture and infection. Monolayer cultures of CEF cells grown in 6-cm petri dishes were prepared and infected as described previously (18).…”

mentioning

confidence: 99%

Posttranslational modifications of Sindbis virus glycoproteins: electrophoretic analysis of pulse-chase-labeled infected cells

Bonatti¹,

Cancedda²

1982

J Virol

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Cytoplasmic extracts prepared from Sindbis virus-infected chicken embryo fibroblasts pulse-chase-labeled with [35S]methionine 6 h postinfection were analyzed on a highly resolving sodium dodecyl sulfate-gel either directly or after various treatments. The results we obtained suggest that (i) the proteolytic cleavage which converts PE2 to E2 glycoprotein takes place intracellularly, before or at least during the formation of complex-type oligosaccharide side chains; and (ii) E1 glycoprotein undergoes a complex maturation pattern. Newly synthesized E1 has a molecular weight of 53,000: shortly thereafter, this 53,000 (53K) form was converted to a 50K form. Subsequently, the 50K form decreased its apparent molecular weight progressively and eventually comigrated with E1 glycoprotein present in the extracellular virus, which displays a molecular weight of 51,000 to 52,000. The conversion of the 53K to the 50K form was not the result of a proteolytic processing and did not depend on glycosylation or disulfide bridge formation and exchange. The possible mechanisms of this conversion are discussed. The second conversion step (from the 50K to the 51-52K form) was due to the formation of complex-type oligosaccharide and was reversed by incubating the cellular extracts with neuraminidase before electrophoretic analysis.

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“…CeUl culture and infection. Monolayer cultures of CEF cells grown in 6-cm petri dishes were prepared and infected as described previously (18).…”

mentioning

confidence: 99%

Posttranslational modifications of Sindbis virus glycoproteins: electrophoretic analysis of pulse-chase-labeled infected cells

Bonatti¹,

Cancedda²

1982

J Virol

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“…Cell culture and cell infection. Monolayers of chicken embryo fibroblasts were prepared and infected as described previously (13).…”

Section: Methodsmentioning

confidence: 99%

“…(i) Immunoprecipitation of`Slabeled cellular extracts. Immunoprecipitation of cellular extracts containing ES-labeled viral proteins was performed as described previously (13). Antibodies, clonal anti-El and clonal anti-E2, were gifts of M. J. Schlesinger.…”

Section: Methodsmentioning

confidence: 99%

One extra oligosaccharide chain of the high-mannose class in the E2 protein of a Sindbis virus isolate

Cancedda¹,

Bonatti²,

Leone³

1981

J Virol

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The number and nature of oligosaccharide chains in the E2 envelope protein (and its precursor PE2) from two strains of Sindbis virus, originally derived from the same HR strain, were investigated. The E2 glycoproteins (and the PE2 proteins) of the two strains had different electrophoretic mobilities on a sodium dodecyl sulfate-polyacrylamide gel. We observed that the glycopeptides from the E2 protein of one of the two strains included an extra oligosaccharide chain of the mannose-rich type. The altered pattern of glycosylation does not interfere with the intracellular migration of the protein and the envelopment and budding of the virus.

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The culture of chick embryo chondrocytes and the control of their differentiated functions in vitro *1I. Characterization of the chondrocyte-specific phenotypes

Capasso

1982

Experimental Cell Research

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Defective mutant of Sindbis virus with a smaller-molecular-weight form of the E1 glycoprotein

Cited by 9 publications

References 26 publications

Posttranslational modifications of Sindbis virus glycoproteins: electrophoretic analysis of pulse-chase-labeled infected cells

Posttranslational modifications of Sindbis virus glycoproteins: electrophoretic analysis of pulse-chase-labeled infected cells

One extra oligosaccharide chain of the high-mannose class in the E2 protein of a Sindbis virus isolate

The culture of chick embryo chondrocytes and the control of their differentiated functions in vitro *1I. Characterization of the chondrocyte-specific phenotypes

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