title: Next generation phage display by use of pVII and pIX as display scaffolds.
abstract: Phage display technology has evolved to become an extremely versatile and powerful platform for protein engineering. The robustness of the phage particle, its ease of handling and its ability to tolerate a range of different capsid fusions are key features that explain the dominance of phage display in combinatorial engineering. Implementation of new technology is likely to ensure the continuation of its success, but has also revealed important short comings inherent to current phage display systems. This is in particular related to the biology of the two most popular display capsids, namely pIII and pVIII. Recent findings using two alternative capsids, pVII and pIX, located to the phage tip opposite that of pIII, suggest how they may be exploited to alleviate or circumvent many of these short comings. This review addresses important aspects of the current phage display standard and then discusses the use of pVII and pIX. These may both complement current systems and be used as alternative scaffolds for display and selection to further improve phage display as the ultimate combinatorial engineering platform.
authors: Centre for Immune Regulation, University of Oslo, N-316 Oslo, Norway. g.a.loset@imbv.uio.no
authors: Geir Åge
authors: GÅ
authors: Løset
authors: Inger
authors: I
authors: Sandlie
mesh_terms: D001435:Bacteriophages; D036022:Capsid Proteins / Q000096:biosynthesis* / Q000235:genetics; D061505:Cell Surface Display Techniques; D019020:Directed Molecular Evolution; D004926:Escherichia coli; D006801:Humans; D019151:Peptide Library; D015202:Protein Engineering; D021382:Protein Sorting Signals; D021381:Protein Transport; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000235:genetics
chemical_list: D036022:Capsid Proteins; D019151:Peptide Library; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins