Cellular libraries of peptide sequences (CLiPS) and methods...

Combinatorial chemistry technology: method – library – apparatus – Method specially adapted for identifying a library member – Identifying a library member by means of a tag – label – or...

Reexamination Certificate

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C506S001000, C506S002000, C506S003000, C506S014000, C506S018000, C435S007200, C435S007370, C435S007400, C435S004000

Reexamination Certificate

active

07666817

ABSTRACT:
The present invention provides compositions including peptide display scaffolds that present at least one candidate peptide and at least one detectable moiety in at least one of the N-terminal and C-terminal candidate peptide presenting domains that when expressed in a cell are accessible at a surface of the cell outermembrane. In addition, the present invention also provides kits and methods for screening a library of cells presenting the candidate peptides in peptide display scaffolds to identify a ligand for an enzyme.

REFERENCES:
patent: 5571698 (1996-11-01), Ladner et al.
patent: 5962255 (1999-10-01), Griffiths et al.
patent: 6300065 (2001-10-01), Kieke et al.
patent: 6303344 (2001-10-01), Patten et al.
patent: 6423538 (2002-07-01), Wittrup et al.
patent: 6492160 (2002-12-01), Griffiths et al.
patent: 6548249 (2003-04-01), Anderson et al.
patent: 6660257 (2003-12-01), McWherter et al.
patent: 6660843 (2003-12-01), Feige et al.
patent: 6696251 (2004-02-01), Wittrup et al.
patent: 6699658 (2004-03-01), Wittrup et al.
patent: 6723512 (2004-04-01), Larocca et al.
patent: 2003/0013150 (2003-01-01), Manosroi et al.
patent: 2003/0049729 (2003-03-01), Manosroi et al.
patent: 2003/0082575 (2003-05-01), Schultz et al.
patent: 2004/0146976 (2004-07-01), Wittrup et al.
patent: 2005/0196406 (2005-09-01), Daugherty et al.
patent: 2006/0003387 (2006-01-01), Peelle et al.
patent: 2006/0029947 (2006-02-01), Georgiou et al.
patent: 2007/0020678 (2007-01-01), Ault-Riche et al.
patent: 0474894 (1992-03-01), None
patent: 0922957 (1999-06-01), None
patent: WO 2005/047461 (2005-05-01), None
Taschner et al,Biochem. J. 2002, 367, 393-402.
Lee et al, Trends in Biotechnology, 21(1), Jan. 2003, 46-52.
Ascheim, et al. Clipping away at protease substrates. Nature Biothnology, 2006, vol. 24, No. 6, pp. 665.
Bessette et al., Rapid Isolation of High-Affinity Protein Binding Peptides Using Bacterial Display. Prot. Eng., Design & Sel. 17(10):731-739 (2004).
Bessette et al., Flow Cytometric Screening of cDNA Expression Libraries for Fluorescent Proteins. Biotechnol. Prog. 20:963-967 (2004).
Boulware et al., Protease Specificity Determination by Using Cellular Libraries of Peptide Substrates (CLiPS). PNAS 103(20):7583-7588 (2006).
Deperthes et al., Phage Display Substrate: A Blind Method for Determining Protease Specificity. Biol. Chem., 383:1107-1112 (2002).
Daugherty et al., Sorting Out the Best Targets. Nature Methods, 2006 vol. 3, No. 7, p. 498.
Daugherty et al., Flow Cytometric Screening of Cell-Based Libraries. J. Immunol. Meth., 243:211-227 (2000).
Daugherty et al., Development of an Optimized Expression System for the Screening of Antibody Libraries Displayed on theEscherichia coliSurface. Protein. Eng., 12(7):613-621 (1999).
Choo & Klug. Designing DNA-binding proteins on the surface of filamentous phage. Curr Opin Biotecluml. Aug. 1995;6(4):431-6. Review.
Hoogenboom,et al. Designing and optimizing library selection strategies for generating high-affinity antibodies. Trends Biotechnol. Feb. 1997;15(2):62-70. Review.
Ladner, et al. Constrained Peptides as Binding Entities, Trends Biotechnol. Oct. 1995;13(10):426-30.
Lowman et al. Selecting High-Affinity Binding Proteins by Monovalent Phage Display, 1991, Biochem. 30(45):10832-10838.
Markland et al., 1996, Selection for Protease Inhibitors Using Bacteriophage Display, Methods of Enzymology, vol. 267, p. 28-51.
Matthews and Wells, Substrate Phage: Selection of Protease Substrates by Monovalent Phage Display, Science. May 21, 1993;260(5111):1113-7.
Wang et al., Phage display of proteases and macromolecular inhibitors. 1996 Methods Enzymol. 1996;267:52-68.
Ley et al. Obtaining a family of high-affinity, high-specificity protein inhibitors of plasmin and plasma kallikrein. Mol Divers. Oct. 1996;2(1-2):119-24.
Markland et al. Iterative optimization of high-affinity protease inhibitors using phage display. 2. Plasma kallikrein and thrombin. Biochemistry. Jun. 18, 1996;35(24):8058-67.
Markland et al. Iterative optimization of high-affinity proteases inhibitors using phage display. 1. Plasmin. Biochemistry. Jun. 18, 1996;35(24):8045-57.
Markland and Ladner. Affinity maturation of proteins displayed on surface of M13 bacteriophage as major coat protein fusions. Methods Enzymol. 1996;267:68-82.
Markland and Ladner. Selection for protease inhibitors using bacteriophage display. Methods Enzymol. 1996;267:28-51.
Rice, et al., Bacterial display using circularly permuted outer membrane protein OmpX yields high affinity peptide ligands, Protein Science, (2006), vol. 15,15:825-836.
Camaj, et al., Ligand-mediated protection against phage lysis as a positive selection strategy for the enrichment of epitopes displayed on the surface ofE. colicells, Biol Chem. Dec. 2001;382(12):1669-1677.
Daugherty, et al., Protein engineering with bacterial display, Curr Opin Struct Biol. Aug. 2007;17(4):474-480.
Etz, et al., Bacterial phage receptors, versatile tools for display of polypeptides on the cell surface, Journal of Bacteriology, Dec. 2001, p. 6924-6935, vol. 183, No. 23.
Fernandez, et al., Solution NMR studies of the integral membrane proteins OmpX and OmpA fromEscherichia coli, FEBS Lett. Aug. 31, 2001;504(3):173-178.
Freudl, Insertion of peptides into cell-surface-exposed areas of theEscherichia coliOmpA protein does not interfere with export and membrane assembly, Gene. Oct. 30, 1989;82(2):229-236.
Graf, et. al., Random circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase, Proc Natl Acad Sci U S A. Oct. 15, 1996;93(21):11591-11596.
Koebnik, Membrane assembly of theEscherichia coliouter membrane protein OmpA: exploring sequence constraints on transmembrane beta-strands, J Mol Biol. Jan. 29, 1999;285(4):1801-1810.
Koebnik, et. al., Membrane assembly of circularly permuted variants of theE. coliouter membrane protein OmpA, J Mol Biol. Jul. 28, 1995;250(5):617-626.
Koebnik, et al.,Structural and functional roles of the surface-exposed loops of the beta-barrel membrane protein OmpA fromEscherichia coli, Journal of Bacteriology, Jun. 1999, p. 3688-3694, vol. 181, No. 12.
Koebnik, et al., Structure and function of bacterial outer membrane proteins:barrels in a nutshell, Molecular Microbiology, (2000), 37(2), 239-253.
Macintyre, et al., The signal sequence of anEscherichia coliouter membrane protein can mediate translocation of a not normally secreted protein across the plasma membrane, J. Biol. Chem., vol. 262, Issue 17, 8416-8422, 06, 1987.
Mejare, et al., Selection of cadmium specific hexapeptides and their expression as OmpA fusion proteins inEscherichia coli, Protein Engineering, vol. 11, 489-494.
Rice, et al., Directed evolution of a biterminal bacterial display scaffold enhances the display of diverse peptides, Protein Eng Des Sel. Jul. 2008;21(7):435-442.
Takahara, et al., The ompA signal peptide directed secretion of Staphylococcal nuclease A byEscherichia coli,J. Biol. Chem., vol. 260, Issue 5, 2670-2674, 03, 1985.
Vogt, et al.,The structure of the outer membrane protein OmpX fromEscherichia colireveals possible mechanisms of virulence, Structure (London), vol. 7, Issue 10, Oct. 15, 1999, pp. 1301-1309.

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