Molecular characterization of hog cholera virus

Rümenapf, T.; Meyers, Gregor; Stark, Robert; Thiel, Heinz-Jürgen

doi:10.1007/978-3-7091-9153-8_2

Cited by 45 publications

(29 citation statements)

References 33 publications

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“…The virus, 40-60 nm in diameter, is surrounded by a 5-7 µm thick membrane whose outer surface is lined with radial processes, characterized by helical symmetry [3]. The virus is inactivated at 56 °C for 30 min and is sensitive to lipid solvents, ultraviolet light, and disinfectants [4]. Two biotypes of pestiviruses have been distinguished according to their proliferation in the cell culture as cytopathic (CP) or non-cytopathic (NCP) [5].…”

Section: Introductionmentioning

confidence: 99%

Comparative Investigation of Border Disease Virus Infection in Sheep Flocks with Abortion Problems in Konya Province

Avcı

Yavru

2014

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Abstract:The aim of the present study was to determine the serological and virological status of animals persistently infected (PI) with border disease virus (BDV), with focus on the prevalence of pestiviruses in sheep and lambs. This study is the first to our knowledge, to investigate the role of viral infections in abortions in the sheep population of Konya province. The prevalence of antibodies against BDV was as follows: sheep, 79%; lambs, 43.4%; and rams, 6%. Of 1000 leukocyte (sheep) samples examined with a direct ELISA, 11 (1.1%) (first sampling) were antibody-positive. Three sheep were determined to be PI and were sacrificed. Of 1011 sheep leukocyte samples, 14 were examined using a direct immunoperoxidase (IP) assay for BDV antigen, and 11 of 327 (3.36%) tissue samples were positive. The BDV genome was detected in 14 of 63 (22.2%) sheep leukocyte samples and 11 of 327 (3.36%) tissue samples by one-step RT-PCR. The BDV genome could not be detected in any vaginal swab samples. The sensitivity and specificity rates between direct ELISA and direct IP were respectively 100% and 98.8% and the values were, respectively, 78.57% and 98.6% between direct ELISA and one-step RT-PCR and 100% and 97.5% between one-step RT-PCR and direct IP. In conclusion it was determinate that BDV has an important role as an etiologic agent in abortion causes in sheep population in Konya.

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Section: Introductionmentioning

confidence: 99%

Comparative Investigation of Border Disease Virus Infection in Sheep Flocks with Abortion Problems in Konya Province

Avcı

Yavru

2014

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“…E1 has been implicated (21), along with E rns and E2 (4), in viral adsorption to host cells. Importantly, different modifications introduced into these glycoproteins appear to have an important effect on CSFV virulence (3,6,9,10,11,12,15,20).In lysates of CSFV-infected cells, E2 glycoprotein forms homodimers and heterodimers with E1 glycoprotein (14,22) via disulfide bridges between cysteine residues. Formation of these disulfide-linked heterodimers also occurs in CSFV virions (19), suggesting that the interaction between envelope proteins plays an important role in virus assembly, virion maturity, and consequently in efficiency of viral infection.…”

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confidence: 99%

“…In lysates of CSFV-infected cells, E2 glycoprotein forms homodimers and heterodimers with E1 glycoprotein (14,22) via disulfide bridges between cysteine residues. Formation of these disulfide-linked heterodimers also occurs in CSFV virions (19), suggesting that the interaction between envelope proteins plays an important role in virus assembly, virion maturity, and consequently in efficiency of viral infection.…”

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confidence: 99%

Substitution of Specific Cysteine Residues in the E1 Glycoprotein of Classical Swine Fever Virus Strain Brescia Affects Formation of E1-E2 Heterodimers and Alters Virulence in Swine

Fernandez-Sainz

Holinka

Gladue

et al. 2011

J Virol

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E1, along with E rns and E2, is one of the three envelope glycoproteins of classical swine fever virus (CSFV). E1 and E2 are anchored to the virus envelope at their carboxyl termini, and E rns loosely associates with the viral envelope. In infected cells, E2 forms homodimers and heterodimers with E1 mediated by disulfide bridges between cysteine residues. The E1 protein of CSFV strain Brescia contains six cysteine residues at positions 5, 20, 24, 94, 123, and 171. The role of these residues in the formation of E1-E2 heterodimers and their effect on CSFV viability in vitro and in vivo remain unclear. Here we observed that recombinant viruses harboring individual cysteine-to-serine substitutions within the E1 envelope protein still have formation of E1-E2 heterodimers which are functional in terms of allowing efficient virus progeny yields in infected primary swine cells. Additionally, these single cysteine mutant viruses were virulent in infected swine. However, a double mutant harboring Cys24Ser and Cys94Ser substitutions within the E1 protein altered formation of E1-E2 heterodimers in infected cells. This recombinant virus, E1⌬Cys24/94v, showed delayed growth kinetics in primary swine macrophage cultures and was attenuated in swine. Furthermore, despite the observed diminished growth in vitro, infection with E1⌬Cys24/94v protected swine from challenge with virulent CSFV strain Brescia at 3 and 28 days postinfection.Classical swine fever (CSF) is a highly contagious disease of swine. The etiological agent, Classical swine fever virus (CSFV), is a small, enveloped virus with a positive, single-stranded RNA genome and, along with Bovine viral diarrhea virus (BVDV) and Border disease virus (BDV), is classified as a member of the genus Pestivirus within the family Flaviviridae (2). The 12.3-kb CSFV genome contains a single open reading frame that encodes a 3,898-amino-acid polyprotein and ultimately yields 11 to 12 final cleavage products (NH 2 -Npro-C-E rns -E1-E2-p7-NS2-NS3-NS4A-NS4B-NS5A-NS5B-COOH) through co-and posttranslational processing of the polyprotein by cellular and viral proteases (5). Structural components of the CSFV virion include the capsid (C) protein and glycoproteins E rns , E1, and E2. E1 and E2 are anchored to the envelope at their carboxyl termini, and E rns loosely associates with the viral envelope (22, 23). E1 and E2 are type I transmembrane proteins with an N-terminal ectodomain and a C-terminal hydrophobic anchor (19). E1 has been implicated (21), along with E rns and E2 (4), in viral adsorption to host cells. Importantly, different modifications introduced into these glycoproteins appear to have an important effect on CSFV virulence (3,6,9,10,11,12,15,20).In lysates of CSFV-infected cells, E2 glycoprotein forms homodimers and heterodimers with E1 glycoprotein (14,22) via disulfide bridges between cysteine residues. Formation of these disulfide-linked heterodimers also occurs in CSFV virions (19), suggesting that the interaction between envelope proteins plays an important role in virus ...

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“…The nucleocapsid consists of Core protein and the viral RNA genome (13,38,42). While Flaviviridae typically encode Core protein as the first product of the polyprotein, pestiviruses encode the unique N-terminal protease N pro at the analogous position (41).…”

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confidence: 99%

Characterization of Essential Domains and Plasticity of the Classical Swine Fever Virus Core Protein

Riedel

Lamp

Heimann

et al. 2010

J Virol

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genes between two Core genes. Even a Core fusion protein with more than 10-fold-increased molecular mass was integrated into the viral particle and supported the production of infectious progeny virus. The unexpected plasticity of Core protein brings into question the formation of a regular icosahedric particle and supports the idea of a histone-like protein-RNA interaction. All viruses with a duplicated Core gene were unstable and reverted to the wild-type sequence. Interestingly, a nonviable YFP-Core construct was rescued by a mutation within the C-terminal domain of the nonstructural protein NS3.

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Molecular characterization of hog cholera virus

Cited by 45 publications

References 33 publications

Comparative Investigation of Border Disease Virus Infection in Sheep Flocks with Abortion Problems in Konya Province

Comparative Investigation of Border Disease Virus Infection in Sheep Flocks with Abortion Problems in Konya Province

Substitution of Specific Cysteine Residues in the E1 Glycoprotein of Classical Swine Fever Virus Strain Brescia Affects Formation of E1-E2 Heterodimers and Alters Virulence in Swine

Characterization of Essential Domains and Plasticity of the Classical Swine Fever Virus Core Protein

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