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Infection and Immunity, October 2003, p. 5505-5513, Vol. 71, No. 10
0019-9567/03/$08.00+0 DOI: 10.1128/IAI.71.10.5505-5513.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Pi
tek,1 Graz·yna Konopa,2 Bogdan Nowicki,3,4 Stella Nowicki,3,4 and Józef Kur1*
Department of Microbiology, Gda
sk University of Technology, 80-952 Gda
sk,1
Department of Molecular Biology, University of Gda
sk, 80-822 Gda
sk, Poland,2
Departments of Obstetrics and Gynecology,3
Microbiology and Immunology, The University of Texas Medical Branch, Galveston, Texas 77555-10624
Received 14 April 2003/ Returned for modification 3 June 2003/ Accepted 13 July 2003
The potential of the major structural protein DraE of Escherichia coli Dr fimbriae has been used to display an 11-amino-acid peptide of glycoprotein D derived from herpes simplex virus (HSV) type 1. The heterologous sequence mimicking an epitope from glycoprotein D was inserted in one copy into the draE gene in place of a predicted 11-amino-acid sequence in the N-terminal region of surface-exposed domain 2 within the conserved disulfide loop (from Cys21 to Cys53). The inserted epitope was displayed on the surface of the chimeric DraE protein as evidenced by immunofluorescence and was recognized by monoclonal antibodies to the target HSV glycoprotein D antigen. Conversely, immunization of rabbits with purified chimeric Dr-HSV fimbriae resulted in a serum that specifically recognized the 11-amino-acid epitope of HSV glycoprotein D, indicating the utility of the strategy employed.
sk University of Technology, Department of Microbiology, ul. Narutowicza 11/12, 80-952 Gda
sk, Poland. Phone: 45 58 347 16 05. Fax: 48 58 347 18 22. E-mail: kur{at}altis.chem.pg.gda.pl.
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