Literature DB >> 12097387

Immunogenically fit subunit vaccine components via epitope discovery from natural peptide libraries.

Leslie J Matthews1, Robert Davis, George P Smith.   

Abstract

Antigenic peptides that bind pathogen-specific Abs are a potential source of subunit vaccine components. To be effective the peptides must be immunogenically fit: when used as immunogens they must elicit Abs that cross-react with native intact pathogen. In this study, antigenic peptides obtained from phage display libraries through epitope discovery were systematically examined for immunogenic fitness. Peptides selected from random peptide libraries, in which the phage-displayed peptides are encoded by synthetic degenerate oligonucleotides, had marginal immunogenic fitness. In contrast, 50% of the peptides selected from a natural peptide library, in which phage display segments of actual pathogen polypeptides, proved very successful. Epitope discovery from natural peptide libraries is a promising route to subunit vaccines.

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Year:  2002        PMID: 12097387     DOI: 10.4049/jimmunol.169.2.837

Source DB:  PubMed          Journal:  J Immunol        ISSN: 0022-1767            Impact factor:   5.422


  14 in total

1.  Selecting open reading frames from DNA.

Authors:  Paola Zacchi; Daniele Sblattero; Fiorella Florian; Roberto Marzari; Andrew R M Bradbury
Journal:  Genome Res       Date:  2003-05       Impact factor: 9.043

2.  Characterizing monoclonal antibody epitopes by filtered gene fragment phage display.

Authors:  Roberto Di Niro; Fortunato Ferrara; Tarcisio Not; Andrew R M Bradbury; Fernando Chirdo; Roberto Marzari; Daniele Sblattero
Journal:  Biochem J       Date:  2005-06-15       Impact factor: 3.857

3.  Exploring peptide mimics for the production of antibodies against discontinuous protein epitopes.

Authors:  Melita B Irving; Lisa Craig; Alfredo Menendez; Beechanahalli P Gangadhar; Marinieve Montero; Nienke E van Houten; Jamie K Scott
Journal:  Mol Immunol       Date:  2009-12-23       Impact factor: 4.407

4.  Anti-idiotypic monobodies derived from a fibronectin scaffold.

Authors:  Mark A Sullivan; Lauren R Brooks; Philip Weidenborner; William Domm; Jonelle Mattiacio; Qingfu Xu; Michael Tiberio; Timothy Wentworth; James Kobie; Peter Bryk; Bo Zheng; Mary Murphy; Ignacio Sanz; Stephen Dewhurst
Journal:  Biochemistry       Date:  2013-03-01       Impact factor: 3.162

5.  The nature and combination of subunits used in epitope-based Schistosoma japonicum vaccine formulations affect their efficacy.

Authors:  Xuefeng Wang; Lei Zhang; Ying Chi; Jason Hoellwarth; Sha Zhou; Xiaoyun Wen; Lei He; Feng Liu; Calvin Wu; Chuan Su
Journal:  Parasit Vectors       Date:  2010-11-19       Impact factor: 3.876

Review 6.  Interaction analysis through proteomic phage display.

Authors:  Gustav N Sundell; Ylva Ivarsson
Journal:  Biomed Res Int       Date:  2014-09-11       Impact factor: 3.411

7.  Purification of polyclonal anti-conformational antibodies for use in affinity selection from random peptide phage display libraries: a study using the hydatid vaccine EG95.

Authors:  A J Read; C G Gauci; M W Lightowlers
Journal:  J Chromatogr B Analyt Technol Biomed Life Sci       Date:  2009-03-28       Impact factor: 3.205

8.  Identification of genes coding for B cell antigens of Mycoplasma mycoides subsp. mycoides Small Colony (MmmSC) by using phage display.

Authors:  Dubravka R Miltiadou; Arshad Mather; Edy M Vilei; Dion H Du Plessis
Journal:  BMC Microbiol       Date:  2009-10-09       Impact factor: 3.605

9.  Shotgun Phage Display - Selection for Bacterial Receptins or other Exported Proteins.

Authors:  Karin Jacobsson; Anna Rosander; Joakim Bjerketorp; Lars Frykberg
Journal:  Biol Proced Online       Date:  2003-05-01       Impact factor: 3.244

Review 10.  Phage display as a promising approach for vaccine development.

Authors:  Leili Aghebati-Maleki; Babak Bakhshinejad; Behzad Baradaran; Morteza Motallebnezhad; Ali Aghebati-Maleki; Hamid Nickho; Mehdi Yousefi; Jafar Majidi
Journal:  J Biomed Sci       Date:  2016-09-29       Impact factor: 8.410

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