|Title||Inactivated Salmonella expressing the receptor-binding domain of bacterial adhesins elicit antibodies inhibiting hemagglutination.|
|Publication Type||Journal Article|
|Year of Publication||2008|
|Authors||Van Gerven, N., H. De Greve, and J-P. Hernalsteens|
|Date Published||2008 Oct 15|
|Keywords||Adhesins, Bacterial, Animals, Antibodies, Bacterial, Erythrocytes, Escherichia coli, Escherichia coli Proteins, Gene Expression Regulation, Bacterial, Hemagglutination, Mice, Protein Binding, Protein Structure, Tertiary, Recombinant Proteins, Salmonella|
We examined the potential of inactivated Salmonella strains to induce protective antibodies against two adhesins of pathogenic Escherichia coli. The receptor-binding domains of the F17a-G adhesin of F17a fimbriae and of the FimH adhesin of type 1 fimbriae were fused to the translocator domain of the autotransporter AIDA-I. An IgG response against F17a-G or FimH was induced after immunization of mice with acetone-inactivated Salmonella displaying the corresponding fimbrial receptor-binding domain. These sera inhibit in vitro agglutination of erythrocytes by E. coli carrying these fimbriae. Our results demonstrate that induced and subsequently acetone-inactivated Salmonella are useful delivery vehicles for the stimulation of an IgG antibody response against heterologous antigens.
|Alternate Journal||Vet. Microbiol.|