Functionality of chimeric E2 glycoproteins of BVDV and CSFV in virus replication

H.G.P. van Gennip, G.K.W. Miedema, R.J.M. Moormann, P.A. van Rijn

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

An intriguing difference between the E2 glycoprotein of CSFV and the other groups of pestiviruses (nonCSFV) is a lack of two cysteine residues on positions cysteine 751 and 798. Other groups of pestivirus are not restricted to one species as swine, whereas CSFV is restricted to swine and wild boar. We constructed chimeric CSFV/BVDV E2 genes based on a 2D model of E2 proposed by van Rijn et al. (van Rijn et al. 1994, J Virol 68, 3934¿42) and confirmed their expression by immunostaining of plasmid-transfected SK6 cells. No equivalents for the antigenic units B/C and A were found on E2 of BVDVII. This indicates major structural differences in E2. However, the immunodominant BVDVII domain A, containing epitopes with essential amino acids between position 760¿764, showed to be dependent on the presence of the region defined by amino acids 684 to 796. As for the A domain of CSFV, the BVDVII A-like domain seemed to function as a separate unit. These combined domains in E2 proved to be the only combination which was functional in viral background of CSFV C-strain. The fitness of this virus (vfl c36BVDVII 684¿796) seemed to be reduced compared to vfl c9 (with the complete antigenic region of BVDVII).
Original languageEnglish
Pages (from-to)29-40
JournalVirology: Research and Treatment
Volume1
DOIs
Publication statusPublished - 2008

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Pestivirus
Virus Replication
Cysteine
Swine
Immunodominant Epitopes
Sus scrofa
Essential Amino Acids
Epitopes
Plasmids
Viruses
Amino Acids
Genes
bovine viral diarrhea virus gp53

Cite this

van Gennip, H.G.P. ; Miedema, G.K.W. ; Moormann, R.J.M. ; van Rijn, P.A. / Functionality of chimeric E2 glycoproteins of BVDV and CSFV in virus replication. In: Virology: Research and Treatment. 2008 ; Vol. 1. pp. 29-40.
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abstract = "An intriguing difference between the E2 glycoprotein of CSFV and the other groups of pestiviruses (nonCSFV) is a lack of two cysteine residues on positions cysteine 751 and 798. Other groups of pestivirus are not restricted to one species as swine, whereas CSFV is restricted to swine and wild boar. We constructed chimeric CSFV/BVDV E2 genes based on a 2D model of E2 proposed by van Rijn et al. (van Rijn et al. 1994, J Virol 68, 3934¿42) and confirmed their expression by immunostaining of plasmid-transfected SK6 cells. No equivalents for the antigenic units B/C and A were found on E2 of BVDVII. This indicates major structural differences in E2. However, the immunodominant BVDVII domain A, containing epitopes with essential amino acids between position 760¿764, showed to be dependent on the presence of the region defined by amino acids 684 to 796. As for the A domain of CSFV, the BVDVII A-like domain seemed to function as a separate unit. These combined domains in E2 proved to be the only combination which was functional in viral background of CSFV C-strain. The fitness of this virus (vfl c36BVDVII 684¿796) seemed to be reduced compared to vfl c9 (with the complete antigenic region of BVDVII).",
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Functionality of chimeric E2 glycoproteins of BVDV and CSFV in virus replication. / van Gennip, H.G.P.; Miedema, G.K.W.; Moormann, R.J.M.; van Rijn, P.A.

In: Virology: Research and Treatment, Vol. 1, 2008, p. 29-40.

Research output: Contribution to journalArticleAcademicpeer-review

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AU - Miedema, G.K.W.

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AU - van Rijn, P.A.

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N2 - An intriguing difference between the E2 glycoprotein of CSFV and the other groups of pestiviruses (nonCSFV) is a lack of two cysteine residues on positions cysteine 751 and 798. Other groups of pestivirus are not restricted to one species as swine, whereas CSFV is restricted to swine and wild boar. We constructed chimeric CSFV/BVDV E2 genes based on a 2D model of E2 proposed by van Rijn et al. (van Rijn et al. 1994, J Virol 68, 3934¿42) and confirmed their expression by immunostaining of plasmid-transfected SK6 cells. No equivalents for the antigenic units B/C and A were found on E2 of BVDVII. This indicates major structural differences in E2. However, the immunodominant BVDVII domain A, containing epitopes with essential amino acids between position 760¿764, showed to be dependent on the presence of the region defined by amino acids 684 to 796. As for the A domain of CSFV, the BVDVII A-like domain seemed to function as a separate unit. These combined domains in E2 proved to be the only combination which was functional in viral background of CSFV C-strain. The fitness of this virus (vfl c36BVDVII 684¿796) seemed to be reduced compared to vfl c9 (with the complete antigenic region of BVDVII).

AB - An intriguing difference between the E2 glycoprotein of CSFV and the other groups of pestiviruses (nonCSFV) is a lack of two cysteine residues on positions cysteine 751 and 798. Other groups of pestivirus are not restricted to one species as swine, whereas CSFV is restricted to swine and wild boar. We constructed chimeric CSFV/BVDV E2 genes based on a 2D model of E2 proposed by van Rijn et al. (van Rijn et al. 1994, J Virol 68, 3934¿42) and confirmed their expression by immunostaining of plasmid-transfected SK6 cells. No equivalents for the antigenic units B/C and A were found on E2 of BVDVII. This indicates major structural differences in E2. However, the immunodominant BVDVII domain A, containing epitopes with essential amino acids between position 760¿764, showed to be dependent on the presence of the region defined by amino acids 684 to 796. As for the A domain of CSFV, the BVDVII A-like domain seemed to function as a separate unit. These combined domains in E2 proved to be the only combination which was functional in viral background of CSFV C-strain. The fitness of this virus (vfl c36BVDVII 684¿796) seemed to be reduced compared to vfl c9 (with the complete antigenic region of BVDVII).

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