Cloning and expression of a species-specific early immunogenic 36-kilodalton protein of Mycoplasma hyopneumoniae in Escherichia coli
Autor: | Joachim Frey, M Strasser, Marylène Kobisch, Jacques Nicolet, G Bestetti |
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Rok vydání: | 1991 |
Předmět: |
Swine
Immunology lac operon Molecular cloning medicine.disease_cause Microbiology Mycoplasma Porcine enzootic pneumonia Bacterial Proteins Species Specificity Mycoplasma hyopneumoniae Escherichia coli medicine Animals Cloning Molecular Promoter Regions Genetic Gene biology biology.organism_classification Molecular biology Ribosomal binding site Infectious Diseases Subcloning Genes Bacterial Parasitology Rabbits Research Article |
Zdroj: | Infection and Immunity. 59:1217-1222 |
ISSN: | 1098-5522 0019-9567 |
DOI: | 10.1128/iai.59.4.1217-1222.1991 |
Popis: | Mycoplasma hyopneumoniae, the etiologic agent of porcine enzootic pneumonia, synthesizes a 36-kDa protein which is an early and strong immunogenic factor in experimentally and naturally infected swine. The gene encoding this protein was cloned by screening a gene library of M. hyopneumoniae DNA with rabbit hyperimmune serum made against whole M. hyopneumoniae cells and convalescent-phase swine serum. Analysis of the recombinant protein expressed in Escherichia coli by immunoblot techniques showed that the protein is expressed in E. coli in its full length and does not cross-react with proteins from M. flocculare or M. hyorhinis. Genetic analysis showed that the gene was expressed from the lac promoter of the vector and seems to be translationally initiated from its own ribosome binding site. Subcloning in a transcriptional fusion vector to optimize expression resulted in production of the 36-kDa protein in E. coli at levels up to 30% of total protein. |
Databáze: | OpenAIRE |
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