Membrane Glycoproteins of Enveloped Viruses

Compans, Richard W.; Kemp, Maurice C.

doi:10.1016/s0070-2161(08)60750-9

Cited by 10 publications

(5 citation statements)

References 172 publications

(134 reference statements)

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“…attachment and recognition of host cell receptors, haemagglutinating activity, and stability and incorporation into membranes of the glycoproteins (Compans & Kemp, 1978). Clearly, previous analyses of these assumed functions may require re-examination.…”

Section: Discussionmentioning

confidence: 99%

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: Discussionmentioning

confidence: 99%

Envelope Protein of the Flavivirus Kunjin is Apparently Not Glycosylated

Wright

1982

Journal of General Virology

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“…Glycopeptides commonly associated with glycoproteins isolated from various RNA viruses rarely exceed a molecular weight of 3,500 (7,8); nevertheless G1 glycopeptides with an approximate molecular weight of 5,100 have been isolated from three different ecotropic viruses. In addition to their larger size, the labeling pattern of G, is urnusual in that mannose is not incorporated in detectable amounts.…”

Section: Fig 6 Analysis Of the [3h]glucosamine-labeledmentioning

confidence: 99%

Glycopeptides of murine leukemia viruses. II. Comparison of xenotropic and dual-tropic viruses

Kemp

Famulari

O’Donnell

et al. 1980

J Virol

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The glycosylation patterns of the gp70 glycoproteins of xenotropic and dualtropic murine leukemia virus (MuLV) were compared with those of ecotropic viruses. Ecotropic viruses contain a large glycopeptide size class designated G1 (molecular weight, approximately 5100), and such glycopeptides were not detected in xenotropic viruses grown in mink cells nor in dual-tropic viruses grown in mouse or mink lung cells. Both xenotropic and dual-tropic MuLV had glycopeptide size classes designated G2, G3, and G4 (molecular weights, approximately 2900, 2,200, and 1,500, respectively). G2 glycopeptides of xenotropic and dual-tropic MuLV were shown to be resistant to endo-beta-N-acetylglucosaminidase H, whereas G3 and G4 glycopeptides were susceptible. The relative abudance of glycopeptide G3 was increased in xenotropic and dual-tropic viruses as compared with ecotropic viruses, whereas the relative amount of G4 was decreased in xenotropic viruses. The similarity in the glycosylation patterns of a number of xenotropic and dual-tropic viruses suggests that glycosylation sites are highly conserved within the env gene products of each of these classes of viruses.

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“…The resulting virions contain lipids which closely reflect those of the host plasma membrane, whereas most cellular membrane proteins are effectively excluded from the viral envelope. Thus, the maturation process requires specific interactions among the viral proteins which are incorporated into the cellular plasma membrane (1)(2)(3). Reports of the packaging of cellular actin within virions of several groups of enveloped viruses (4), as well as electron microscopic evidence of microfilaments in close association with budding virions (5), have suggested that the cytoskeletal network may be actively involved in the assembly and budding of these viruses.…”

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confidence: 99%

Effect of cytochalasin B on the maturation of enveloped viruses.

Griffin¹,

Compans²

1979

The Journal of Experimental Medicine

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The maturation of two enveloped viruses, influenza and vesicular stomatitis, occurs in cells treated with cytochalasin B. Virions produced in the presence of 50 microgram/ml cytochalasin B (CB) appear to be as infectious as those from control cells, indicating that polymerized actin is not required for the assembly of functional viral components. CB inhibits the release of influenza virus from treated cells, a phenomenon which appears to be a result of the synthesis of an aberrant neuraminidase (NA) glycoprotein; virions grown in CB-treated cells had a 90% reduction in specific enzymatic activity. We found that both influenza viral glycoproteins (NA and Hemagglutinin glycoprotein) had faster electrophoretic mobilities and were more heterogeneous in CB-treated cells as compared with controls. We also observed complete inhibition of incorporation of labeled glucosamine into viral glycoproteins in the presence of the drug. It was of interest that CB-induced inhibition of glycosylation appeared to cause loss of neuraminidase function, whereas hemagglutinating activity was not noticeably impaired. The presence of altered glycoproteins did not significantly diminish the infectivity of either influenza virus or vesicular stomatitis virus. Our results indicate that no step in the maturation of enveloped viruses is dependent upon an intact cytoskeletal network.

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Membrane Glycoproteins of Enveloped Viruses

Cited by 10 publications

References 172 publications

Envelope Protein of the Flavivirus Kunjin is Apparently Not Glycosylated

Envelope Protein of the Flavivirus Kunjin is Apparently Not Glycosylated

Glycopeptides of murine leukemia viruses. II. Comparison of xenotropic and dual-tropic viruses

Effect of cytochalasin B on the maturation of enveloped viruses.

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