Proteins and glycoproteins specified by the flavivirus Kunjin

Westaway, E. G.; Shew, Marilyn

doi:10.1016/s0042-6822(77)80007-x

Cited by 38 publications

(27 citation statements)

References 16 publications

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“…Shapiro et al (1972) originally suggested that GP19 is cleaved to produce M (V1) during virion morphogenesis, but peptide mapping of [35S]methionine-labelled GP19 and M protein did not support this suggested relationship . Considerable heterogeneity in the migration during electrophoresis of GP 19 of several flaviviruses has been reported (Shapiro et al, 1973;Westaway & Shew, 1977) and the results presented in Fig. 5 support these earlier observations.…”

Section: Discussionsupporting

confidence: 82%

“…5), our previous analyses of Kunjin virus-specified proteins in 13 % acrylamide gels using a discontinuous buffer system showed that the second fastest moving band in lane 1 is GP19 . Heterogeneity in the migration of GP 19 following electrophoresis and the incorporation of GP19 into virions have been previously reported (Shapiro et al, 1972(Shapiro et al, , 1973Boulton & Westaway, 1976;Westaway & Shew, 1977). The [3H]glucosamine was not converted to labelled amino acid before incorporation into GP 19 of virions, demonstrated by the lack of label in E, C and M proteins in lane 3, Fig.…”

Section: Gp19 Associated With Purified Virussupporting

confidence: 62%

“…Wright, unpublished results). In addition, '[3H]glucosamine-labelled' E co-migrated on electrophoresis with E containing 14C-labelled mixed amino acids (Westaway & Shew, 1977) and the high ratio of GPI9 to E (NV2 to V3) observed by Boulton & Westaway (1976) in [3H]glucosamine-labelled Kunjin virions probably resulted from the presence of [3Hlglucosamine in GP 19 both as converted amino acids and in its original chemical form. In both the preceeding reports the incorporation of [3H]glucosamine into virions was so low that detection of the two small structural proteins C and M labelled with converted amino acids would not have been possible.…”

Section: Discussionmentioning

confidence: 99%

“…Using [2-3Hlmannose, a radioactive carbohydrate that is not metabolized to other labelled sugars or amino acids (Schwarz et al, 1977), E proteins of MVEV, WNV, dengue type 2 virus and SFV were readily labelled, whereas E of Kunjin virus was not. Unsuccessful attempts to label Kunjin virus E with [3Hlmannose, but the successful incorporation of some [3H]glucosamine into E, have been reported (Boulton & Westaway, 1976;Westaway & Shew, 1977). It now seems likely that the radioactivity previously detected in Kunjin virus E following labelling with [3H]glucosamine was in the form of amino acids (Strauss et al, 1970); exhaustive digestion of similar material with Pronase produced small molecules that eluted with monosaccharides and amino acids in Bio-Gel P-6 columns identical to those used in Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The E proteins of several flaviviruses, e.g. dengue type 2 (Stollar, 1969;Shapiro et al, 1972), Japanese encephalitis (JE) (Shapiro et al, 1973), Saint Louis encephalitis (SLE) (Qureshi & Trent, 1973) and Kunjin (Boulton & Westaway, 1976;Westaway & Shew, 1977) have been reported to be glycosylated, usually on the basis of their incorporation of radioactive carbohydrates into the envelope protein. However, the possibility that the radioactive label in the carbohydrate may have been incorporated into proteins and 0022-1317/82/0000-4838 $02.00 © 1982 SGM Purification of radioactively labelled viruses.…”

Section: Introductionmentioning

confidence: 99%

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Envelope Protein of the Flavivirus Kunjin is Apparently Not Glycosylated

Wright

1982

Journal of General Virology

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SUMMARYThe envelope protein E (formerly designated V3) of the flavivirus Kunjin was not labelled with radioactive galactose, mannose or glucosamine during virus growth in Vero cells. On electrophoresis through polyacrylamide gels containing SDS, the envelope (E) protein migrated more rapidly than related intracellular virus-specified glycoproteins. Furthermore, E had a density in CsC1 solution consistent with that of a protein lacking carbohydrate, and did not bind to concanavalin A-agarose. In contrast, the envelope glycoprotein of Murray Valley encephalitis virus (MVEV) did bind to concanavalin A under similar conditions and was readily labelled with radioactive mannose. These results suggested that the E protein of Kunjin virus was not glycosylated, a feature not shared with MVEV and West Nile virus (WNV), whose properties were consistent with the presence of oligosaccharides attached to the envelope proteins. When Kunjin virions were labelled with radioactive glucosamine, the label was contained in GP19 (formerly NV2). The glycopeptides derived by Pronase digestion of GP19 from Kunjin virions were larger than those derived from GP 19 obtained from infected cells.

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Section: Discussionsupporting

confidence: 82%

Section: Gp19 Associated With Purified Virussupporting

confidence: 62%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Envelope Protein of the Flavivirus Kunjin is Apparently Not Glycosylated

Wright

1982

Journal of General Virology

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Animal Viruses, Including Protozoal Viruses

Fraenkel‐Conrat

1985

The Viruses

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The 12 vertex capsomers (pentons) carry strain-characteristic glycoprotein fibers (1O-30-nm long) with knobs at the ends; the rest is made up of hexons. The genome is linear doublestranded DNA of 20-25 x 10 6 daltons in the mammalian and 28-30 x 10 6 daltons in the avian viruses. At least ten proteins of 5-120 x 10 3 daltons make up the virion. Each adenovirus has a narrow host range. Several are oncogenic in newborn nonhosts. Serological relations among the many different adenoviruses usually called "types" are very limited. Two genera have been defined (MASTAOENOVIRUS and AVIADENOVIRUSi subgroups AD or I-IV), and species names for those found in various animals have been proposed with h1-h34 for the (sero)types of the human virus species. Similar differentiation of serotypes are used for the animal adenoviruses (27 simian, ten bovine, eight avian, four porcine, two canine, and one ovine and opossum in 1979). Adenoviruses generally cause only light upper respiratory diseases (Figure 1). Adoxophyses orana(S) Aedes Aedes aegypti Aedes aegypti (Diptera) Aedes can tans nuclear polyhedrosis virus (A) Aedes iridescent: see mosquito iridescent virus Aerocystis agent: see swim bladder inflammation agent of carp African green monkey cytomegalo (AGM-CMV) African green monkey EBV-like (AGM-EBV) cercopi thecine cercopi thecine probably densovirus C probably chloriridovirus (h5) cytomegalovirus (h14) lymphocrytovirus Baculoviridae Togaviridae Parvoviridae Entomopoxvirinae Iridoviridae Betaherpesvirinae Gammaherpesvirinae .p..

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Viral Membranes

Compans

Klenk

1979

Comprehensive Virology Volume 13: Structure and Assembly

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Proteins and glycoproteins specified by the flavivirus Kunjin

Cited by 38 publications

References 16 publications

Envelope Protein of the Flavivirus Kunjin is Apparently Not Glycosylated

Envelope Protein of the Flavivirus Kunjin is Apparently Not Glycosylated

Animal Viruses, Including Protozoal Viruses

Viral Membranes

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