The Ultrastructure of Cell Cultures Infected with Border Disease and Bovine Virus Diarrhoea Viruses

Gray, E. W.; Nettleton, PF

doi:10.1099/0022-1317-68-9-2339

Cited by 33 publications

(33 citation statements)

References 6 publications

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“…Accordingly, the glycoproteins are not integrated into the plasma membrane. In BVDV-infected cells we found virus particles in distended portions of the rough endoplasmic reticulum as already described by Gray & Nettleton (1987). In accordance with these authors, however, we neither detected budding nor any of the stages of virus release.…”

Section: F Weiland and Others F Weiland And Otherssupporting

confidence: 78%

“…This finding was surprising since budding at the cell surface has not been reported for pestiviruses (Gray & Nettleton, 1987 ;Laude, 1987) and in previous studies viral glycoproteins were not detected at the cell surface (GreiserWilke et al, 1991). Further analysis by immune electron microscopy showed that immunogold granules exclusively decorated virions which had accumulated at the cell surface after their release in aggregates.…”

Section: Discussionmentioning

confidence: 39%

“…A prerequisite for virus release by budding from the extracellular membrane is expression of viral glycoproteins. Convincing evidence for a budding process of pestiviruses has so far not been reported (Gray & Nettleton, 1987), and indeed Greiser-Wilke et al (1991) actually reported that viral glycoproteins are not present at the surface of cells infected with pestiviruses.…”

Section: Introductionmentioning

confidence: 99%

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Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles.

Weiland

Unger

et al. 1999

Journal of General Virology

100

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The glycoproteins E rns of classical swine fever virus (CSFV) and E rns and E2 of bovine viral diarrhoea virus (BVDV) are shown to be located at the surface of infected cells by the use of indirect immunofluorescence and by cytofluorometric analysis. The positive immunostaining of the cell surface was further analysed by immunogold electron microscopy and it could be shown that only extracellular virions were labelled. Gold granules were not seen at the cellular plasma membrane. In contrast to BVDV E2, the CSFV E2 of virions sticking to the plasma membrane was not accessible to the respective monoclonal antibodies. However, CSFV particles isolated from culture supernatant were able to bind both monoclonal anti-E rns and anti-E2 antibodies. For CSFV and BVDV, binding of anti-E rns antibodies to the virions was more pronounced than that of anti-E2. This finding was unexpected since E2 is considered to be the immunodominant glycoprotein.

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Section: F Weiland and Others F Weiland And Otherssupporting

confidence: 78%

Section: Discussionmentioning

confidence: 39%

Section: Introductionmentioning

confidence: 99%

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Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles.

Weiland

Unger

et al. 1999

Journal of General Virology

100

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“…Cells infected with poliovirus, a picornavirus, accumulate large numbers of membranous vesicles derived from the endoplasmic reticulum (ER) that range in diameter from 150 to 400 nm (6,7,13,27,(72)(73)(74)76) and that display characteristics similar to those of cellular autophagic vacuoles (18,68,72). Finally, cells infected with bovine viral diarrhea virus (BVDV), a pestivirus, contain tubules and spherical vesicles that are 100 to 200 nm in diameter and that are thought to be derived from the rough ER (33).…”

mentioning

confidence: 99%

Nonstructural Protein Precursor NS4A/B from Hepatitis C Virus Alters Function and Ultrastructure of Host Secretory Apparatus

Konan

Giddings

Ikeda

et al. 2003

J Virol

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“…The virions consist of four structural proteins (C, E rns , E1 and E2). The basic protein C was believed to form a capsid that surrounds the virus genome, but recent studies by Rümenapf et al (2008) have shown that it is dispensable for virus assembly (Gray & Nettleton, 1987;Thiel et al, 1991). The three glycosylated proteins E rns , E1 and E2 are located in the lipid membrane of cellular origin (Chu & Zee, 1984;Coria et al, 1983;Fetzer et al, 2005).…”

mentioning

confidence: 99%

New insights into processing of bovine viral diarrhea virus glycoproteins Erns and E1

Wegelt

Reimann

Zemke

et al. 2009

Journal of General Virology

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Bovine viral diarrhea virus (BVDV) is a member of the genus Pestivirus within the family Flaviviridae. Its single-stranded RNA encodes a polyprotein that is cleaved co-and posttranslationally by viral and cellular proteases. However, the cleavage between the envelope proteins E rns and E1 is still unexplained. In this study, an E rns -E1 protein could be identified and characterized with a new E1-specific antiserum. With bicistronic constructs bearing a deletion in the E rns -encoding region and expressing E rns or the E rns -E1 protein, it could be shown that this protein is not essential for virus replication. Furthermore, two putative cleavage sites were mutated in eukaryotic expression plasmids, as well as in full-length cDNA constructs. The mutation of position P3 of a potential signal peptide peptidase site abolished cleavage completely and no infectious virus progeny could be observed, indicating that cleavage of the E rns -E1 protein is indispensable for virus growth.Bovine viral diarrhea virus (BVDV), the causative agent of an economically important disease of cattle worldwide, belongs, like classical swine fever virus and border disease virus, to the genus Pestivirus within the family Flaviviridae (Collett et al., 1988a;Fauquet et al., 2005;Houe, 1999;Korn, 1977;Pringle, 1998). The genome is a singlestranded RNA of positive polarity with a size of about 12.3 kb. One large open reading frame (ORF) encodes a polyprotein that is cleaved co-and post-translationally by viral and cellular proteases (Collett et al., 1988b; Rümenapf et al., 1993). The ORF is flanked by 59 and 39 untranslated regions (UTRs) that are important for virus replication (Collett et al., 1988a;Yu et al., 1999Yu et al., , 2000. An internal ribosomal entry site (IRES) within the 59 UTR allows capindependent translation of the virus polyprotein (Pestova & Hellen, 1999; Poole et al., 1995;Yu et al., 2000). The virions consist of four structural proteins (C, E rns , E1 and E2). The basic protein C was believed to form a capsid that surrounds the virus genome, but recent studies by Rümenapf et al. (2008) have shown that it is dispensable for virus assembly (Gray & Nettleton, 1987;Thiel et al., 1991). The three glycosylated proteins E rns , E1 and E2 are located in the lipid membrane of cellular origin (Chu & Zee, 1984;Coria et al., 1983;Fetzer et al., 2005). The envelope protein E rns , which lacks a typical membrane anchor, seems to be important for first cell contact by binding to glycosaminoglycans (Fetzer et al., 2005;Iqbal et al., 2000). The cellular receptor for BVDV is the bovine CD46 molecule and it has recently been shown that E1-E2 heterodimers are essential for virus entry (Maurer et al., 2004;Ronecker et al., 2008). The envelope proteins E rns , E1 and E2 are processed from the polyprotein in a hierarchical way, starting with the translocation of the C-terminal signal peptide downstream of the capsid protein into the endoplasmic reticulum (ER), followed by the release of the capsid and E2 protein (Heimann et al., 2006; Rümenap...

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The Ultrastructure of Cell Cultures Infected with Border Disease and Bovine Virus Diarrhoea Viruses

Cited by 33 publications

References 6 publications

Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles.

Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles.

Nonstructural Protein Precursor NS4A/B from Hepatitis C Virus Alters Function and Ultrastructure of Host Secretory Apparatus

New insights into processing of bovine viral diarrhea virus glycoproteins Erns and E1

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