Chimeric FimH adhesin of type 1 fimbriae: a bacterial surface display system for heterologous sequences
Article Abstract:
The preS2 hepatitis B protein segment and the cholera toxin epitope inserted into the Escherichia coli FimH proteins are effective as a surface display system for heterologous sequences. The conformation of the inserted DNA segments is similar to the sequences in the wild-type proteins. The inserted protein segments contain almost 56 amino acids and has no effect on FimH production or exposure to the cell surface. The adhesive activity of FimH reduces slightly.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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Authentic display of a cholera toxin epitope by chimeric type 1 fimbriae: effects of insert position and host background
Article Abstract:
The effects of insert position and host background on the cholera toxin B fimA gene were determined by utilizing a reporter epitope mimicking a neutralizing epitope of the cholera toxin B. Results reveal that insertion of the wild-type fim gene mediated the production and surface exposure of chimeric FimA proteins in contrast with the mutated MS7 strain. This is secondary to the co-assembly of wild-type and chimeric FimA proteins into the fimbrial organeles.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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Probing the receptor recognition site of the FimH adhesin by fimbriae-displayed FimH-FocH hybrids
Article Abstract:
Fimbriae-displayed FimH-FocH hybrids were utilized to investigate the receptor recognition site of the FimH adhesin. Results revealed that erythrocytes and yeast cells agglutinated following the fusion of the N-terminus of FimH to the complementary sector of FocH. The receptor binding capacity of some of the fusions disappeared. Moreover, the existence of a D-mannose-receptor-binding core domain in FimH was confirmed.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
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