Expression of foreign epitopes in P-fimbriae of Escherichia coli
Autor: | Irma van Die, Simon Barteling, Ingrid van Megen, Hans Bergmans, Betty E. Enger-Valk, Wiel Hoekstra, Frits Mooi, Joost A.W.M. van Oosterhout |
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Rok vydání: | 1990 |
Předmět: |
DNA
Bacterial Protein subunit Fimbria Genetic Vectors Molecular Sequence Data Restriction Mapping Peptide Enzyme-Linked Immunosorbent Assay Biology medicine.disease_cause Antibodies Viral Epitope Microbiology Epitopes Mice Two-Hybrid System Techniques Genetics medicine Escherichia coli Animals Amino Acid Sequence Cloning Molecular Site-directed mutagenesis Molecular Biology Antigens Viral chemistry.chemical_classification Antigens Bacterial Mice Inbred BALB C Base Sequence biochemical phenomena metabolism and nutrition biology.organism_classification Molecular biology Enterobacteriaceae Hypervariable region chemistry Fimbriae Bacterial DNA Viral Mutation bacteria Protein Multimerization |
Zdroj: | Moleculargeneral genetics : MGG. 222(2-3) |
ISSN: | 0026-8925 |
Popis: | Hypervariable regions (HRs) of the major subunit of F11 fimbriae were exploited for insertion of foreign epitopes. Two insertion vectors were created that contain a unique cloning site in HR1 or HR4 respectively. Several oligonucleotides, coding for antigenic determinants derived from different pathogens, were cloned in both insertion vectors. Hybrid fimbrial subunits were generally shown to be assembled in fimbriae when the length of the inserted peptide did not exceed 14 amino acids. The inserted peptides appeared to be exposed in the fimbrial filament. One hybrid fimbrial protein induced detectable levels of antibodies against the inserted epitope if injected into mice. |
Databáze: | OpenAIRE |
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