the maltose-binding protein as a scaffold for monovalent display of peptides derived from phage libraries.

NLM AIDSLINE The maltose-binding protein as a scaffold for monovalent display of peptides derived from phage libraries. Zwick MB; Bonnycastle LL; Noren KA; Venturini S; Leong E; Barbas CF 3rd;
February 28, 1999

Anal Biochem. 1998 Nov 1;264(1):87-97. Unique Identifier : AIDSLINE Random peptide libraries are displayed on filamentous bacteriophage as fusions to either the minor coat protein, pIII, or the major coat protein, pVIII. We have devised a means of isolating the peptide displayed on a phage clone by transferring it to the N-terminus of the maltose-binding protein (MBP) of Escherichia coli encoded by malE. Transfer of a peptide sequence to monomeric MBP eliminates phage-encoded amino acids downstream of the insert peptide as well as avidity effects caused by multivalent display on phage. Peptide:MBP fusions are also easily affinity purified on amylose columns. The pMal-p2 vector was engineered to accept phage DNA encoding pIII- and pVIII-displayed peptides fused to their respective leader sequences. Both types of leader sequence were shown to target the peptide:MBP fusions to the periplasm of E. coli. A streamlined procedure for transferring peptides to MBP was applied to clones that had been isolated from a panel of pVIII-displayed peptide libraries by screening with an HIV-1-specific monoclonal antibody (Ab). By enzyme-linked immunosorbent assay, the Ab bound each of the peptide:MBP fusions and required the presence of a disulfide bridge within each peptide. Some of the peptide:MBP fusions were also analyzed using surface plasmon resonance. Thus, our study shows the value of malE fusion vectors in characterizing phage-displayed peptides. Copyright 1998 Academic Press. JOURNAL ARTICLE Amino Acid Sequence Bacteriophages/GENETICS Base Sequence Carrier Proteins/GENETICS/METABOLISM/SECRETION Cloning, Molecular DNA, Recombinant Escherichia coli Genetic Vectors Human HIV Antibodies/IMMUNOLOGY HIV-1/IMMUNOLOGY Molecular Sequence Data Peptide Library Polymerase Chain Reaction Protein Processing, Post-Translational Recombinant Fusion Proteins/GENETICS Signal Peptides/GENETICS/METABOLISM Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S.

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Information in this article was accurate in February 28, 1999. The state of the art may have changed since the publication date. This material is designed to support, not replace, the relationship that exists between you and your doctor. Always discuss treatment options with a doctor who specializes in treating HIV.