Phage pVIII

Huse WD, Stinchcombe TJ, Glaser SM, Starr L, MacLean M, Hellstrom KE, Hellstrom I, Yelton DE. Application of a filamentous phage pVIII fusion protein system suitable for efficient production, screening, and mutagenesis of F(ab) antibody fragments. J. Immunol. 1992 149(12) 3914-3920. 

To achieve surface display, five of the Ml3 coat proteins have been used in fusion to foreign protein fragments. In the most widespread system the antibody is coupled to the N-terminus or second domain of the minor coat protein pill (11,12,14). The naive function of the three to five copies of the pill, in particular their N-terminal domain, is to provide binding of the phage to the f-pili of E. coli to initiate infection (39). The major coat protein (pVIII) has been used as an alternative fusion partner, with only very few successes reported in the past decade (40). This fusion technique is more useful for the display of short peptides (41,42). Fusions to pVI have been tried, but not yet with antibodies (43). pVII and pIX were... 

FIGURE 16.4 Schematic representation of phage (b) and phagemid (c) display of polypeptides fused to pill and pVIII coat proteins, compared to wild-type phage (a). 

The one-gene system display (phage) is a good system for the display of small peptides, which do not alter the structure of the coat protein and do not prevent its assembly into viral particles. For the display of larger peptides the two-gene system (phagemid) is preferred or sometimes required, as for pVIII fusion. 

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