HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Zalewska, B. Articles by Piatek, R. Search for Related Content PubMed PubMed Citation Articles by Zalewska, B. Articles by Piatek, R. Agricola Articles by Zalewska, B. Articles by Piatek, R.

DAF- and collagen-binding properties of chimeric Dr fimbriae

Rafa Pitek¹

¹ Department of Microbiology, Gdask University of Technology, ul. G. Narutowicza 11/12, 80-952 Gdask, Poland
² Department of Physical Chemistry, Gdask University of Technology, ul. G. Narutowicza 11/12, 80-952 Gdask, Poland
³ Department of Pharmaceutical Technology and Biochemistry, Gdask University of Technology, ul. G. Narutowicza 11/12, 80-952 Gdask, Poland

Correspondence
Rafa Pitek
wejraf{at}o2.pl

Display of heterologous proteins on the surface of micro-organisms has become an increasingly used strategy for a range of applications in microbiology, biotechnology and vaccinology. In this study, the potential of the major structural protein DraE of Escherichia coli Dr fimbriae as a display system for heterologous sequences was tested. One copy of a heterologous sequence mimicking a small P_k epitope of simian virus 5 was inserted into the draE gene, replacing the N-terminal region of the surface-exposed domain 2 as previously done with the glycoprotein D of herpes simplex virus type 1. The exposure of chimeric proteins on the bacterial surface was detected by immunofluorescence microscopy. Insertion of the heterogenic peptides had no detectable effect on the Ig-barrel structure of the DraE fimbrial subunits, as confirmed by FTIR spectroscopy. Additionally, the affinity of the chimeric fimbriae for DAF and type IV collagen was similar to that of the wild-type Dr fimbriae.