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Infect Immun, May 1998, p. 2060-2064, Vol. 66, No. 5
Lehrstuhl für Mikrobiologie,
Theodor-Boveri-Institut für Biowissenschaften, Am Hubland, 97074 Würzburg, Germany,1 and
International Livestock Research Institute, Nairobi,
Kenya2
Received 5 September 1997/Returned for modification 20 October
1997/Accepted 29 January 1998
The p67 sporozoite antigen of Theileria parva has been
fused to the C-terminal secretion signal of Escherichia
coli hemolysin and expressed in secreted form by attenuated
Salmonella dublin aroA strain SL5631. The recombinant p67
antigen was detected in the supernatant of transformed bacterial
cultures. Immunization trials in cattle revealed that SL5631 secreting
the antigen provoked a 10-fold-higher antibody response to p67 than
recombinant SL5631 expressing but not secreting p67. Immunized calves
were challenged with a 80% lethal dose of T. parva
sporozoites and monitored for the development of infection. Two of
three calves immunized intramuscularly with the p67-secreting SL5631
strain were found to be protected, whereas only one of three animals
immunized with the nonsecreting p67-expressing SL5631 strain was
protected. This is the first demonstration that complete eukaryotic
antigens fused to the C-terminal portion of E. coli
hemolysin can be exported from attenuated Salmonella strains and that such exported antigens can protect cattle against subsequent parasite challenge.
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Delivery of the p67 Sporozoite Antigen of Theileria
parva by Using Recombinant Salmonella dublin: Secretion
of the Product Enhances Specific Antibody Responses in
Cattle
*
Corresponding author. Present address: Institute of
Animal Pathology, Laenggass-Str. 122, 3012 Berne, Switzerland. Phone: 41-31-631 2403. Fax: 41-31-631 2635. E-mail:
heussler{at}itpa.unibe.ch.
ILRI publication no. 9706.
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