Synthetic Peptides: Prospects for a Pili (Fimbriae)-Based Synthetic Vaccine

Schmidt, Michael

doi:10.1007/978-3-642-74703-8_10

Cited by 5 publications

(3 citation statements)

References 114 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…protecting animals and humans from bacteria expressing heterologous fimbriae (53)(54)(55)(56). Most of the antibodies evoked with the purified fimbrial preparation were directed primarily at the structural FimA subunit (which constitutes over 95% of the total fimbrial proteins), but none appeared to be directed at the minor FimH adhesive component.…”

Section: Discussionmentioning

confidence: 99%

Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection.

Thankavel

Madison²,

Ikeda³

et al. 1997

J. Clin. Invest.

136

View full text Add to dashboard Cite

The FimH subunit of type 1-fimbriated Escherichia coli has been implicated as an important determinant of bacterial adherence and colonization of the urinary tract. Here, we sought to localize the functionally important domain(s) within the FimH molecule and to determine if antibodies against this domain would block adherence of type 1-fimbriated E. coli to the bladder mucosa in situ and in vivo in an established mouse model of cystitis. We generated translational fusion proteins of disparate regions of the FimH molecule with an affinity tag MalE, and tested each of the fusion products in vitro for functional activity. The minimum region responsible for binding mouse bladder epithelial cells and a soluble mannoprotein, horseradish peroxidase, was contained within residues 1-100 of the FimH molecule. We validated and extended these findings by demonstrating that antibodies directed at the putative binding region of

show abstract

Section: Discussionmentioning

confidence: 99%

Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection.

Thankavel

Madison²,

Ikeda³

et al. 1997

J. Clin. Invest.

136

View full text Add to dashboard Cite

show abstract

“…These cell surface components may play important roles in colonization and pathogenicity. Antifimbrial antibodies are considered to inhibit the colonization of many bacterial species (14), and fimbriae of periodontopathic bacteria such as Porphyromonas gingivalis (6) and A. actinomycetemcomitans may constitute good candidates for vaccines to prevent these colonizations.…”

mentioning

confidence: 99%

Relative avidity of serum immunoglobulin G antibody for the fimbria antigen of Actinobacillus actinomycetemcomitans in patients with adult periodontitis

et al. 1993

View full text Add to dashboard Cite

The relative avidity of serum immunoglobulin G antibody for the fimbria antigen of Actinobacillus actinomycetemcomitans was assessed by diethylamine dissociation enzyme-linked immunosorbent assay in patients with adult periodontitis. High-titer sera from patients not harboring A. actinomycetemcomitans had significantly higher avidities for the fimbria antigen than did high-titer sera from patients with A. actinomycetemcomitans in their periodontal pockets. The elicited antibodies against the fimbria antigen may afford protection against A. actinomycetemcomitans infection.

show abstract

“…This limitation led to development of synthetic vaccines which consist of synthetic peptides corresponding to conserved regions of an adhesin (124). This approach was successful with the P fimbriae of E. coli, but failed with the fimbriae of gonococci (124). The M protein of streptococci is highly variable at the N-terminal, while the surface exposed C-terminal is conserved.…”

Section: Prevention Of Diseases By Interfering Witii Adherencementioning

confidence: 99%

Molecular mechanisms of Mycoplasma hyopneumoniae adherence to swine respiratory epithelial cells

Zhang

View full text Add to dashboard Cite

A microtiter plate adherence assay for Mycoplasma hyopneumoniae was established by using purified swine tracheal cilia which contained receptors for the mycoplasma. M. hyopneumoniae bound specifically to plates coated with solubilized cilia. The binding was dependent on both the concentration of cilia and the number of mycoplasmas. Dextran sulfate, heparin, chondroitin sulfate, laminin, mucin, and fucoidan significantly inhibited binding of the mycoplasma. The six inhibitors also disrupted the adherence of the mycoplasma to intact ciliated cells. Preincubation with either mycoplasmas or cilia indicated that heparin, mucin, fucoidan and chondroitin sulfate interacted with the adhesive molecules on the surface of mycoplasmas, whereas laminin blocked the receptors in cilia. The basis for inhibition induced by dextran sulfate was unknown. Treatment of cilia with

show abstract

Synthetic Peptides: Prospects for a Pili (Fimbriae)-Based Synthetic Vaccine

Cited by 5 publications

References 114 publications

Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection.

Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection.

Relative avidity of serum immunoglobulin G antibody for the fimbria antigen of Actinobacillus actinomycetemcomitans in patients with adult periodontitis

Molecular mechanisms of Mycoplasma hyopneumoniae adherence to swine respiratory epithelial cells

Contact Info

Product

Resources

About