Immunoaffinity purification of baculovirus-expressed rubella virus E1 for diagnostic purposes

Christer Lindqvist, Michel Schmidt, Johanna Heinola, Risto Jaatinen, Monica Österblad, Aimo Salmi, Sirkka Keränen, Karl Åkerman, Christian Oker-Blom

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Abstract

Three monoclonal antibodies, termed 4E10, 1E11:10, and 2D9:1, were generated against rubella virus. Immunoblot analysis with purified authentic rubella virus or recombinant baculovirus-expressed rubella virus structural proteins E1, E2, and C demonstrated that they were directed against the E1 envelope glycoprotein of the rubella virus particle. By using the yeast Ty virus-like particle system, it was possible to map the binding site of 1E11:10 within amino acids 236 to 286 of the E1 protein and the binding sites of 2D9:1 and 4E10 outside this region. Immunoaffinity purification with these monoclonal antibodies made it evident that they are useful for obtaining large quantities of pure baculovirus-expressed rubella virus envelope protein E1. The diagnostic potential of this immunoaffinity-purified recombinant rubella virus E1 protein compared with that of authentic rubella virus is demonstrated.

Original languageEnglish
Pages (from-to)2192-2196
Number of pages5
JournalJournal of Clinical Microbiology
Volume32
Issue number9
Publication statusPublished - 1994
MoE publication typeA1 Journal article-refereed

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Rubella virus
Baculoviridae
Virion
Binding Sites
Viral Structural Proteins
Protein Binding
Glycoproteins
Yeasts
Monoclonal Antibodies
Amino Acids

Cite this

Lindqvist, C., Schmidt, M., Heinola, J., Jaatinen, R., Österblad, M., Salmi, A., ... Oker-Blom, C. (1994). Immunoaffinity purification of baculovirus-expressed rubella virus E1 for diagnostic purposes. Journal of Clinical Microbiology, 32(9), 2192-2196.
Lindqvist, Christer ; Schmidt, Michel ; Heinola, Johanna ; Jaatinen, Risto ; Österblad, Monica ; Salmi, Aimo ; Keränen, Sirkka ; Åkerman, Karl ; Oker-Blom, Christian. / Immunoaffinity purification of baculovirus-expressed rubella virus E1 for diagnostic purposes. In: Journal of Clinical Microbiology. 1994 ; Vol. 32, No. 9. pp. 2192-2196.
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title = "Immunoaffinity purification of baculovirus-expressed rubella virus E1 for diagnostic purposes",
abstract = "Three monoclonal antibodies, termed 4E10, 1E11:10, and 2D9:1, were generated against rubella virus. Immunoblot analysis with purified authentic rubella virus or recombinant baculovirus-expressed rubella virus structural proteins E1, E2, and C demonstrated that they were directed against the E1 envelope glycoprotein of the rubella virus particle. By using the yeast Ty virus-like particle system, it was possible to map the binding site of 1E11:10 within amino acids 236 to 286 of the E1 protein and the binding sites of 2D9:1 and 4E10 outside this region. Immunoaffinity purification with these monoclonal antibodies made it evident that they are useful for obtaining large quantities of pure baculovirus-expressed rubella virus envelope protein E1. The diagnostic potential of this immunoaffinity-purified recombinant rubella virus E1 protein compared with that of authentic rubella virus is demonstrated.",
author = "Christer Lindqvist and Michel Schmidt and Johanna Heinola and Risto Jaatinen and Monica {\"O}sterblad and Aimo Salmi and Sirkka Ker{\"a}nen and Karl {\AA}kerman and Christian Oker-Blom",
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Lindqvist, C, Schmidt, M, Heinola, J, Jaatinen, R, Österblad, M, Salmi, A, Keränen, S, Åkerman, K & Oker-Blom, C 1994, 'Immunoaffinity purification of baculovirus-expressed rubella virus E1 for diagnostic purposes', Journal of Clinical Microbiology, vol. 32, no. 9, pp. 2192-2196.

Immunoaffinity purification of baculovirus-expressed rubella virus E1 for diagnostic purposes. / Lindqvist, Christer; Schmidt, Michel; Heinola, Johanna; Jaatinen, Risto; Österblad, Monica; Salmi, Aimo; Keränen, Sirkka; Åkerman, Karl; Oker-Blom, Christian.

In: Journal of Clinical Microbiology, Vol. 32, No. 9, 1994, p. 2192-2196.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Immunoaffinity purification of baculovirus-expressed rubella virus E1 for diagnostic purposes

AU - Lindqvist, Christer

AU - Schmidt, Michel

AU - Heinola, Johanna

AU - Jaatinen, Risto

AU - Österblad, Monica

AU - Salmi, Aimo

AU - Keränen, Sirkka

AU - Åkerman, Karl

AU - Oker-Blom, Christian

N1 - Project code: BEL4301

PY - 1994

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N2 - Three monoclonal antibodies, termed 4E10, 1E11:10, and 2D9:1, were generated against rubella virus. Immunoblot analysis with purified authentic rubella virus or recombinant baculovirus-expressed rubella virus structural proteins E1, E2, and C demonstrated that they were directed against the E1 envelope glycoprotein of the rubella virus particle. By using the yeast Ty virus-like particle system, it was possible to map the binding site of 1E11:10 within amino acids 236 to 286 of the E1 protein and the binding sites of 2D9:1 and 4E10 outside this region. Immunoaffinity purification with these monoclonal antibodies made it evident that they are useful for obtaining large quantities of pure baculovirus-expressed rubella virus envelope protein E1. The diagnostic potential of this immunoaffinity-purified recombinant rubella virus E1 protein compared with that of authentic rubella virus is demonstrated.

AB - Three monoclonal antibodies, termed 4E10, 1E11:10, and 2D9:1, were generated against rubella virus. Immunoblot analysis with purified authentic rubella virus or recombinant baculovirus-expressed rubella virus structural proteins E1, E2, and C demonstrated that they were directed against the E1 envelope glycoprotein of the rubella virus particle. By using the yeast Ty virus-like particle system, it was possible to map the binding site of 1E11:10 within amino acids 236 to 286 of the E1 protein and the binding sites of 2D9:1 and 4E10 outside this region. Immunoaffinity purification with these monoclonal antibodies made it evident that they are useful for obtaining large quantities of pure baculovirus-expressed rubella virus envelope protein E1. The diagnostic potential of this immunoaffinity-purified recombinant rubella virus E1 protein compared with that of authentic rubella virus is demonstrated.

M3 - Article

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Lindqvist C, Schmidt M, Heinola J, Jaatinen R, Österblad M, Salmi A et al. Immunoaffinity purification of baculovirus-expressed rubella virus E1 for diagnostic purposes. Journal of Clinical Microbiology. 1994;32(9):2192-2196.