Expression of the envelope antigen F1 of Yersinia pestis is mediated by the product of caf1M gene having homology with the chaperone protein PapD of Escherichia coli
Open Access
- 29 July 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 286 (1-2) , 79-82
- https://doi.org/10.1016/0014-5793(91)80945-y
Abstract
The effective synthesis of the envelope antigen F1 of Y. pestis in E. coli HB101 is mediated by the expression of the caf1M gene. This gene was sequenced, and the protein encoded was found to have a significant homology with the chaperone protein PapD of uropathogenic E. coli. The data presented allow one to suppose Caf1M and PapD proteins perform similar functions in the biogenesis of the Y. pestis capsule and E. coli P‐pili, respectively.Keywords
This publication has 11 references indexed in Scilit:
- Nucleotide sequence of the Yersinia pestis gene encoding F1 antigen and the primary structure of the proteinFEBS Letters, 1990
- Crystal structure of chaperone protein PapD reveals an immunoglobulin foldNature, 1989
- The PapG adhesin of uropathogenic Escherichia coli contains separate regions for receptor binding and for the incorporation into the pilus.Proceedings of the National Academy of Sciences, 1989
- Structural model for interferonsFEBS Letters, 1985
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- A program for prediction of protein secondary structure from nucleotide sequence data: application to histocompatibility antigensNucleic Acids Research, 1984
- REGULATORY SEQUENCES INVOLVED IN THE PROMOTION AND TERMINATION OF RNA TRANSCRIPTIONAnnual Review of Genetics, 1979
- Plague Immunization. VI. Vaccination with the Fraction I Antigen of Yersinia pestisThe Journal of Infectious Diseases, 1974
- Probable domains conformation of human G1(Eu) immunoglobulinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973