Identification of minor fimbrial subunits involved in biosynthesis of K88 fimbriae
| Autor: | P. T. J. Willemsen, D. Bakker, F Stegehuis, F. R. Mooi, Bauke Oudega, F K de Graaf, T T Huisman, R. H. Willems |
|---|---|
| Předmět: |
Signal peptide
Protein subunit Immunoelectron microscopy Recombinant Fusion Proteins Fimbria Molecular Sequence Data Enzyme-Linked Immunosorbent Assay Biology Microbiology Fimbriae Proteins Bacterial Proteins Escherichia coli Amino Acid Sequence Microscopy Immunoelectron Molecular Biology Peptide sequence Antigens Bacterial Base Sequence Escherichia coli Proteins Nucleic acid sequence Protein primary structure biochemical phenomena metabolism and nutrition Molecular biology Molecular Weight Genes Bacterial Antigens Surface bacteria Nucleic Acid Conformation Research Article Molecular Chaperones Plasmids |
| Zdroj: | ResearcherID |
| Popis: | The nucleotide sequences of the genes faeF, faeH, faeI, and faeJ encoding K88 minor fimbrial subunits were determined. Analysis of the primary structure of the gene products revealed that all four proteins are synthesized with an amino-terminal signal sequence. The molecular masses of the mature FaeF, FaeH, FaeI, and FaeJ proteins were calculated to be 15,161, 25,461, 24,804, and 25,093 Da, respectively. FaeH, FaeI, and FaeJ showed significant homology with FaeG, the major fimbrial subunit of K88 fimbriae. Mutations in the respective genes were constructed. Analysis of the mutants showed that the minor fimbrial subunits FaeF and FaeH play an essential role in the biogenesis but not in the adhesive properties of the K88 fimbriae. Mutations in faeI or faeJ had no significant effect on K88 production or adhesive capacity. Specific antisera against FaeF and FaeH were raised by immunization with hybrid Cro-LacZ-FaeF and Cro-LacZ-FaeH proteins. Immunoblotting and immunoelectron microscopy revealed that FaeF and FaeH are located in or along the K88 fimbrial structure. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|