Work

Chimeric Dr Fimbriae with a Herpes Simplex Virus Type 1 Epitope as a Model for a Recombinant Vaccine

Year: 2003

Type: article

Abstract: 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.

Source: Infection and Immunity

DOI: 10.1128/iai.71.10.5505-5513.2003

Authors: Beata Zalewska, Rafał Piątek, Graz˙yna Konopa, Bogdan Nowicki, Stella Nowicki, Józef Kur

Institutions: Gdańsk University of Technology, University of Gdańsk, The University of Texas Medical Branch at Galveston

Language: English

Topic: Biochemical and Structural Characterization

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: National Institutes of Health, National Institute of Child Health and Human Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development