A human pancreatic secretory trypsin inhibitor presenting a hypervariable highly constrained epitope via monovalent phagemid display

Röttgen, Peter; Collins, John

doi:10.1016/0378-1119(95)00441-8

Cited by 46 publications

(17 citation statements)

References 31 publications

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“…Double stranded phagemid DNA was isolated from E. coli WK6λmutS infected with a cloned phagemid and used as a template. We used two primers, #2897: 5′‐GGAGGTCTAGATAACGAGG‐3′ (sense) and #1243a: 5′‐ATGAATTAAGCACGGACC‐3′ (anti‐sense) (both from Amersham Pharmacia Biotech, NJ, USA) [13].…”

Section: Methodsmentioning

confidence: 99%

Selection of peptides that bind to the core oligosaccharide of R-form LPS from a phage-displayed heptapeptide library

Noda

Yamasaki

Hironaka

et al. 2001

FEMS Microbiology Letters

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To characterize common sites within the core oligosaccharide of the R-form lipopolysaccharide (LPS), we screened peptides from a phage-displayed heptapeptide library by using the most truncated form of R-LPS, Re-LPS (S. Typhimurium SL1165) as a ligand. After three rounds of biopanning/amplification and subsequent screening by phagemid enzyme-linked immunosorbent assay (ELISA), we selected three distinct clones that bind to the ligand LPS. We characterized the binding sites of the three clones by ELISA and thin-layer chromatography immunostaining and found that the three clones bind the two Re-LPSs (SL1165 and S. Minnesota Re595) and Rb2-LPS. In addition, one of the clones also bound to S-form LPS (S. Enteritidis). Current data show that those clones bind to common carbohydrate structure(s) expressed in the core oligosaccharides of those LPS samples.

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Section: Methodsmentioning

confidence: 99%

Selection of peptides that bind to the core oligosaccharide of R-form LPS from a phage-displayed heptapeptide library

Noda

Yamasaki

Hironaka

et al. 2001

FEMS Microbiology Letters

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“…This work was partly supported by Grants-in-Aid for Scien- Table 2. Amino acid sequences of the synthetic peptides used in this study GlcNAc-mimicking S F G S G F G G G Y a) The hypervariable heptapeptide region is presented as a loop of 8 amino acids on the surface of the fusion protein by the bracketing Cys covalently bound to internal Cys residues [14]. In other words, 10 amino acids including both Cys residues next to the hypervariable heptapeptide region are exposed on the surface.…”

Section: Discussionmentioning

confidence: 99%

“…A heptapeptide library displayed on M13 filamentous phage (pSKAN8-HyA library [14]) and Escherichia coli WK6λmutS was purchased from MoBiTec GmbH (Göttin-gen, Germany). The biopanning and amplification were essentially performed according to procedures provided by the manufacturer.…”

Section: Affinity Selection and Amplification Of Peptide Librarymentioning

confidence: 99%

Identification and Characterization of Peptides Binding to Newcastle Disease Virus by Phage Display

Ozawa

Ohashi

Onuma

2005

The Journal of Veterinary Medical Science

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ABSTRACT. Three individual peptide sequences, EVSHPKVG, WVTTSNQW, and SGGSNRSP, which have potentials to bind to Newcastle disease virus (NDV), were identified by the biopanning method using phage display technology. The binding specificities of these peptides presented on phages were confirmed by ELISA competition assay using chicken anti-NDV antiserum. The synthetic peptides designed based on these results partially neutralized the infection of NDV in vitro. The peptide-motives identified here have the potential to lead to the identification of novel molecules that inhibit the NDV infection independent of the immune system. KEY WORDS: binding peptide, Newcastle disease virus, phage display.J. Vet. Med. Sci. 67(12): 1237-1241, 2005 Newcastle disease virus (NDV) is an avian enveloped virus belonging to the Paramyxoviridae family, genus Avulavirus, and a pathogen of Newcastle disease (ND). ND is known as one of the most serious avian diseases with a worldwide distribution that can cause severe economic losses in the poultry industry [1]. Several live and inactivated vaccines are available to control the outbreak of ND at present [6]. However, it is known that popular live vaccines, such as the B1 strain, can lead to some loses due to subclinical or acute respiratory disease, resulting in reduced weight gain and chick mortality, respectively [15]. Furthermore, in Japan, the number of small-scale poultry farmers who breed native chickens has increased as a result of the change in food culture. Such farmers tend to avoid vaccinations in consideration of the concerns of consumers over the safety of food, although lack of vaccinations results in a high mortality by NDV in poultry flocks. ND is still an economic problem causing severe losses to farmers and governments in developing countries. NDV can infect numerous kinds of unvaccinated fowl, including wild birds, and such infections seem to play a significant role in the spread of ND [1,11]. For these reasons, the development of novel strategies to control NDV infections is desired.Phage display technology can be used to select for and produce novel peptides that bind to the target molecules of interest. It allows rapid identification and amplification of the peptide ligands for a certain target molecule by the affinity of their specific-binding [3,4,16,18]. Recently, it has been widely used in many fields, such as for identification and characterization of a peptide mimicking the epitope of HIV [5] and HIV-infected cells [10], and identification of enzyme inhibitors [8], immunodepressants [2], and many antigens. This technique is superior to the methods with antibodies, which have been often used to detect such binding peptides, since a peptide displayed on the surface of filamentous bacteriophage is able to bind to the regions in a molecule that the immune system can not recognize. In other words, such a peptide can target a very small epitope: it searches for a binding site with a small amino acid loop while the large antibodies find an epitope of a molecule with ...

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“…Examples are the human pancreatic secretory trypsin inhibitor (PSTI [34]) and Tendamistat [35]. They are small, remarkably stable, and contain an exposed loop structure that can be used for the insertion of a peptide aptamer library.…”

Section: Scaffold Proteins For the Presenta-tion Of Peptide Aptamersmentioning

confidence: 99%

Peptide Aptamer Libraries

Borghouts¹,

Künz²,

Groner³

2008

CCHTS

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Peptide aptamers are molecules that bind to protein targets and are able to interfere with their functions. In the past, important achievements have been made using such peptide aptamers in different approaches and for various purposes. Peptide aptamers are comprised of a variable peptide region of 8 to 20 amino acids in length, which is displayed by a scaffold protein. An overview of the numerous scaffold proteins that have been investigated for their suitability to present peptide aptamers will be given. To identify peptide aptamers efficiently and specifically binding to a predetermined target, two eukaryotic systems have been used in multiple studies: a modified version of the Gal4 yeast-two-hybrid system and the optimized LexA interaction trap system. The two yeast systems are compared and the design of high-complexity peptide aptamer libraries for these systems is described. Although the yeast-two-hybrid system is based on intracellular interactions mammalian screens, performed in cell culture experiments, are sometimes preferred or required. We will give an overview of the mammalian selection systems available, which are based on the expression of peptide aptamers in retroviral or lentiviral vectors. We will show that the isolation and use of peptide aptamers as inhibitors of individual signaling components represents a new challenge for drug development.

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A human pancreatic secretory trypsin inhibitor presenting a hypervariable highly constrained epitope via monovalent phagemid display

Cited by 46 publications

References 31 publications

Selection of peptides that bind to the core oligosaccharide of R-form LPS from a phage-displayed heptapeptide library

Selection of peptides that bind to the core oligosaccharide of R-form LPS from a phage-displayed heptapeptide library

Identification and Characterization of Peptides Binding to Newcastle Disease Virus by Phage Display

Peptide Aptamer Libraries

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