Journal
MICROBIOLOGY-SGM
Volume 155, Issue -, Pages 468-476Publisher
MICROBIOLOGY SOC
DOI: 10.1099/mic.0.022327-0
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Funding
- Institute for the Promotion of Innovation through Science and Technology in Flanders (IWT-Vlaanderen)
- Fonds voor Wetenschappelijk Onderzoek - Vlaanderen [FWOAL215]
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Surface exposure of antigens on bacterial cells can be critical for eliciting an effective antibody response. Therefore, we investigated the cellular localization of the fimbrial F17a-G receptor-binding domain, fused to the translocator domain of the AIDA-I autotransporter. Synthesis of the fusion protein, under the control of the L-arabinose-inducible P-BAD promoter, was shown to permeabilize Escherichia coli K-12 and Salmonella enterica serovar Typhimurium cells. The presence of permeable cells interfered with several methods that are typically used to determine surface exposure of proteins, such as protease treatment and whole-cell ELISA. Double immunofluorescence microscopy, using a second antibody directed against beta-galactosidase, a bacterial protein expressed in the cytoplasm, allowed the simultaneous detection of antigen expression and permeability in individual cells.
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