Identification of antigenic regions of the Erns protein for pig antibodies elicited during classical swine fever virus infection.

@article{Lin2004IdentificationOA,
  title={Identification of antigenic regions of the Erns protein for pig antibodies elicited during classical swine fever virus infection.},
  author={Min Lin and Erin Trottier and J Pasick and Marta Iris Sabara},
  journal={Journal of biochemistry},
  year={2004},
  volume={136 6},
  pages={
          795-804
        }
}
The structural glycoprotein E(rns) of classical swine fever virus (CSFV) is one of the major antibody targets upon infection of pigs with the virus. Molecular dissection of the structure of E(rns) would define the minimal immunodominant regions that induce antibody responses after infection and may thus help design an effective diagnostic reagent or vaccine. In this study, deletion analysis was made within amino acids (aa) 297 to 776 of the CSFV Alfort/187 polyprotein containing the large C… 
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Classical swine fever virus: Antigenic architecture of the E2 glycoprotein elucidated by epitope mapping using synthetic peptides
TLDR
Mapping of five linear, nonoverlapping B-cell epitopes that use a set of synthetic peptides, which encompass the full sequence of the CSFV E2 protein (Shimen strain), and the effects of aminoacid substitutions in E2 on its antigenic properties are investigated.
New insights into the antigenic structure of the glycoprotein E(rns) of classical swine fever virus by epitope mapping.
High-resolution epitope mapping for monoclonal antibodies to the structural protein Erns of classical swine fever virus using peptide array and random peptide phage display approaches.
TLDR
New insights are provided into the structure and organization of epitopes on theCSFV E(rns) and valuable epitope information is provided for the rational design of vaccines, drugs and diagnostic immunoassays for CSFV.
Enzyme-Linked Immunosorbent Assay Based on a Chimeric Antigen Bearing Antigenic Regions of Structural Proteins Erns and E2 for Serodiagnosis of Classical Swine Fever Virus Infection
TLDR
The data suggest that use of the chimeric antigen C21ErnsE2 would improve serodiagnostic sensitivity and allow for the detection of CSFV infection as early as 7 dpi.
Fusion Proteins Cpn10-Erns with Properties of Generating CSFV-Neutralized Antibodies1
Identification of a conserved linear B-cell epitope at the N-terminus of the E2 glycoprotein of Classical swine fever virus by phage-displayed random peptide library.
Generation and immunogenicity analysis of recombinant classical swine fever virus glycoprotein E2 and Erns expressed in baculovirus expression system
TLDR
While the E rns could not confer protection against CSFV, E2 and E2 + E rnscould not only elicit humoral and cell-mediated immune responses but also confer complete protection againstCSFV C-strain in rabbits.
Molecular cloning and expression of a fragment of the gene codifying for the protein ERNS of classical swine fever virus
TLDR
A synthetic fragment of the Erns gene (codifying for aa 109- 160) was subcloned into pET28a vector and a 90% pure recombinant product was obtained, potential use of this antigen for detection of CSFV antibodies should be further evaluated.
Prokaryotic Expression and Purification of Highly Soluble Partial Glycoprotein Erns of Indian Strain of Classical Swine Fever Virus
TLDR
The described methodology of producing a highly soluble recombinant protein with native conformation would likely to assist in development of differential diagnostic test as well as its application in raising hyperimmune sera for detection of CSFV antigen either in tissue materials or infected cell lines.
Co-expression of Erns and E2 genes of classical swine fever virus by replication-defective recombinant adenovirus completely protects pigs against virulent challenge with classical swine fever virus.
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References

SHOWING 1-10 OF 49 REFERENCES
Deletions of Structural Glycoprotein E2 of Classical Swine Fever Virus Strain Alfort/187 Resolve a Linear Epitope of Monoclonal Antibody WH303 and the Minimal N-Terminal Domain Essential for Binding Immunoglobulin G Antibodies of a Pig Hyperimmune Serum
TLDR
The N-terminal region of 221 amino acids covering Alfort/187 E2, expressed as a fusion product in Escherichia coli, was shown to contain the epitope recognized by a monoclonal antibody with affinity for various CSFV strains but not for the other members of the pestivirus genus, bovine viral diarrhea virus (BVDV) and border disease virus (BDV).
Classical swine fever virus (CSFV) envelope glycoprotein E2 containing one structural antigenic unit protects pigs from lethal CSFV challenge.
TLDR
The vaccinated pigs were protected against an intranasal lethal CSFV challenge, indicating that the immune response induced by one structural antigenic unit of E2 can protect pigs against classical swine fever.
Inactivation of the RNase Activity of Glycoprotein Erns of Classical Swine Fever Virus Results in a Cytopathogenic Virus
TLDR
It is concluded that the RNase activity of envelope protein Erns plays an important role in the replication of pestiviruses and speculate that thisRNase activity might be responsible for the persistence of these viruses in their natural host.
Detection of antibodies against classical swine fever virus in swine sera by indirect ELISA using recombinant envelope glycoprotein E2.
Glycoprotein E2 of classical swine fever virus: expression in insect cells and identification as a ribonuclease.
TLDR
Recombinant virus BacCE2 generated a protein which was similar in size to wild-type E2 synthesized in swine kidney cells infected with CSFV, and RNase activity coeluted with the E2 fraction, indicating that ribonuclease activity is an inherent property of E2.
Classical swine fever virus: independent induction of protective immunity by two structural glycoproteins
TLDR
Glycoprotein E0 represents a second determinant for the induction of protective immunity against classical swine fever and is detected on the surfaces of VVR-infected cells.
Identification of T-cell epitopes in the structural and non-structural proteins of classical swine fever virus.
TLDR
It could be shown that peptide 290 (KHKVRNEVMVHWFDD), which corresponds to amino acid residues 1446-1460 of the CSFV non-structural protein NS2-3 could induce interferon-gamma secretion after secondary in vitro restimulation.
Mutations Abrogating the RNase Activity in Glycoprotein Erns of the Pestivirus Classical Swine Fever Virus Lead to Virus Attenuation
TLDR
Infestation of piglets with an RNase-negative mutant containing a deletion of the histidine codon 346 of the open reading frame did not lead to CSF, andalyses of reisolated viruses gave no indication for the presence of revertants in the infected animals.
Antibody Responses of Pigs to Defined Erns Fragments after Infection with Classical Swine Fever Virus
TLDR
Antibody responses of pigs to defined Erns fragments, after classical swine fever virus (CSFV) infection, were studied by using an enzyme-linked immunosorbent assay (ELISA) and indicated that the epitopes within the consensus region are conformational.
Fine mapping of a C-terminal linear epitope highly conserved among the major envelope glycoprotein E2 (gp51 to gp54) of different pestiviruses.
TLDR
The detailed mapping of a novel linear epitope located at the C-terminal part of the molecule, which reacted with a monoclonal antibody (4-9D4) as well as polyclonal animal sera is reported, which can be used as a genus-specific diagnosis tool.
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