title: Protein engineering with biosynthesized libraries from Bordetella bronchiseptica bacteriophage.
abstract: Phage display offers a powerful approach to engineer protein affinity. A naturally occurring analog to phage display, the Bordetella bronchiseptica bacteriophage (BP) employs a highly variable protein termed the major tropism determinant (Mtd) to recognize its dynamic host. Propagation of BP provides a self-made phage library (SMPL) with vast numbers of phage particles, each displaying a single Mtd variant. We report applying the diversity of the BP-SMPL to access a tyrosine-rich library of Mtd variants. Expression of the SMPL-engineered Mtd variant as a GST-bound fusion protein demonstrated specific binding to the target T4 lysozyme with dissociation constants in the sub-micromolar range. The results guide future experiments with SMPLs applied to protein engineering.
authors: Department of Molecular Biology and Biochemistry, University of California Irvine, Irvine, California, USA.
authors: Tom Z
authors: TZ
authors: Yuan
authors: Cathie M
authors: CM
authors: Overstreet
authors: Issa S
authors: IS
authors: Moody
authors: Gregory A
authors: GA
authors: Weiss
mesh_terms: D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000378:metabolism*; D016950:Bordetella bronchiseptica / Q000821:virology*; D008969:Molecular Sequence Data; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
chemical_list: D011994:Recombinant Proteins