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

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

VTT Technical Research Centre of Finland

Research output: Contribution to journal › Article › Scientific › peer-review

10 Citations (Scopus)

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 language	English
Pages (from-to)	2192-2196
Journal	Journal of Clinical Microbiology
Volume	32
Issue number	9
Publication status	Published - 1994
MoE publication type	A1 Journal article-refereed

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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",

note = "Project code: BEL4301",

year = "1994",

language = "English",

volume = "32",

pages = "2192--2196",

journal = "Journal of Clinical Microbiology",

issn = "0095-1137",

publisher = "American Society for Microbiology",

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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

Y1 - 1994

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

SN - 0095-1137

VL - 32

SP - 2192

EP - 2196

JO - Journal of Clinical Microbiology

JF - Journal of Clinical Microbiology

IS - 9

ER -

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

Abstract

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