Inactivated Salmonella expressing the receptor-binding domain of bacterial adhesins elicit antibodies inhibiting hemagglutination.

TitleInactivated Salmonella expressing the receptor-binding domain of bacterial adhesins elicit antibodies inhibiting hemagglutination.
Publication TypeJournal Article
Year of Publication2008
AuthorsVan Gerven, N., H. De Greve, and J-P. Hernalsteens
JournalVet Microbiol
Volume131
Issue3-4
Pagination369-75
Date Published2008 Oct 15
ISSN0378-1135
KeywordsAdhesins, Bacterial, Animals, Antibodies, Bacterial, Erythrocytes, Escherichia coli, Escherichia coli Proteins, Gene Expression Regulation, Bacterial, Hemagglutination, Mice, Protein Binding, Protein Structure, Tertiary, Recombinant Proteins, Salmonella
Abstract

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.
DOI10.1016/j.vetmic.2008.04.001
Alternate JournalVet. Microbiol.
PubMed ID18502056