Libraries of Peptides and Proteins Displayed on Filamentous Phage

Smith, Georgep.; Scott, Jamie K.

doi:10.1016/b978-0-12-765561-1.50028-x

Cited by 212 publications

(303 citation statements)

References 26 publications

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“…Phage were concentrated from the cultures by precipitation with polyethylene glycol (PEG) [48] followed by purification by CsCl gradient purification [48]. The phage concentration was determined by absorbance measurement as described in Smith and Scott [49] and re-confirmed by electrophoresis on a 0.8% agarose gel in 4×-GBB buffer.…”

Section: Large-scale Preparation Of F1k Phage and Recombinant B21mentioning

confidence: 99%

Filamentous phage as an immunogenic carrier to elicit focused antibody responses against a synthetic peptide

Houten

Zwick

Menéndez

et al. 2006

Vaccine

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Filamentous bacteriophage are widely used as immunogenic carriers for "phage-displayed" recombinant peptides. Here we report that they are an effective immunogenic carrier for synthetic peptides. The f1.K phage was engineered to have an additional Lys residue near the N-terminus of the major coat protein, pVIII, so as to enhance access to chemical cross-linking agents. The dimeric synthetic peptide, B2

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Section: Large-scale Preparation Of F1k Phage and Recombinant B21mentioning

confidence: 99%

Filamentous phage as an immunogenic carrier to elicit focused antibody responses against a synthetic peptide

Houten

Zwick

Menéndez

et al. 2006

Vaccine

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“…The major problem existed in cell-based selection is that phage displayed peptides can bind to the modified cells nonspecifically. In order to overcome the problem, multirounds of selection were carried out in our experiment according to Smith's method [30]. In addition, before each round of selection, wild type hCD81-deficient NIH/ 3T3 cells were used for preincubation with the library in order to remove the non-specific phages.…”

Section: The Motif-containing Phages Specific To Hcd81 On Cell Membranementioning

confidence: 99%

Phage display selection on whole cells yields a small peptide specific for HCV receptor human CD81

Cao

Zhao

et al. 2003

Cell Res

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The human CD81 (hCD81), the most recently proposed receptor of hepatitis C virus (HCV), can especifically bind to HCV envelope glycoprotein 2 (E2). In this study, hCD81-expressing murine NIH/3T3 cells were used to select hCD81-binding peptides from a phage displayed nonapeptide library (PVIII9aaCys). Eighteen of the 75 clones selected from the library showed specific binding to the hCD81-expressing NIH/3T3 cells by enzyme linked immunosorbent assay (ELISA) and competitive inhibition test. Twelve out of the 18 clones shared the amino acid motif SPQYWTGPA. Sequence comparison of the motif showed no amino acid homology with the native HCV E2. The motif-containing phages could competitively inhibit the ability of HCV E2 binding to native hCD81-expressing MOLT-4 cells, and induce HCV E2 specific immune response in vivo. These results suggest that the selected motif SPQYWTGPA should be a mimotope of HCV E2 to bind to hCD81 molecules. Our findings cast new light on developing HCV receptor antagonists.

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“…Smith, University of Missouri, Columbia. Biopanning and sequencing were performed as reported earlier (Smith & Scott, 1993) with modifications as described below. GCC:BIO purified to homogeneity using protein A Sepharose chromatography was dialyzed against 100 mM NaHC03 buffer pH 8.6.…”

Section: Immunoselection Of Gcc:bio Reactive Phages From a Random Pementioning

confidence: 99%

“…Phage particles ( I O ' I), purified by polyethylene glycol 8000 precipitation of the culture filtrate of Kan91 cells infected with individual phages, were titered spectroscopically (Smith & Scott, 1993). Purified phages were boiled in SDS-PAGE sample buffer.…”

Section: Western Blot Analysis With Gcc:blo-reactive Phage Particlesmentioning

confidence: 99%

Topological mimicry and epitope duplication in the guanylyl cyclase C receptor

et al. 1998

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Guanylyl cyclase C (GCC) is the receptor for the gastrointestinal hormones, guanylin, and uroguanylin, in addition to the bacterial heat-stable enterotoxins, which are one of the major causes of watery diarrhea the world over. GCC is expressed in intestinal cells, colorectal tumor tissue and tumors originating from metastasis of the colorectal carcinoma. We have earlier generated a monoclonal antibody to human GCC, GCC:B 10, which was useful for the immunohistochemical localization of the receptor in the rat intestine (Nandi A et al., 1997, J Cell Biochern 66500-51 I), and identified its epitope to a 63-amino acid stretch in the intracellular domain of GCC. In view of the potential that this antibody has for the identification of colorectal tumors, we have characterized the epitope for GCC:B 10 in this study. Overlapping peptide synthesis indicated that the epitope was contained in the sequence HIPPENIFPLE. This sequence was unique to GCC, and despite a short stretch of homology with serum amyloid protein and pertussis toxin, no cross reactivity was detected. The core epitope was delineated using a random hexameric phage display library, and two categories of sequences were identified, containing either a single, or two adjacent proline residues. No sequence identified by phage display was identical to the epitope present in GCC, indicating that phage sequences represented mimotopes of the native epitope. Alignment of these sequences with HIPPENIFPLE suggested duplication of the recognition motif, which was confirmed by peptide synthesis. These studies allowed us not only to define the requirements of epitope recognition by GCC:B10 monoclonal antibody, but also to describe a novel means of epitope recognition involving topological mimicry and probable duplication of the cognate epitope in the native guanylyl cyclase C receptor sequence.

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Libraries of Peptides and Proteins Displayed on Filamentous Phage

Cited by 212 publications

References 26 publications

Filamentous phage as an immunogenic carrier to elicit focused antibody responses against a synthetic peptide

Filamentous phage as an immunogenic carrier to elicit focused antibody responses against a synthetic peptide

Phage display selection on whole cells yields a small peptide specific for HCV receptor human CD81

Topological mimicry and epitope duplication in the guanylyl cyclase C receptor

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