A comprehensive analysis of filamentous phage display vectors for cytoplasmic proteins: an analysis with different fluorescent proteins

Velappan, Nileena; Fisher, Hugh E.; Pesavento, Emanuele; Chasteen, Leslie; D'Angelo, Sara; Kiss, Csaba; Longmire, Michelle; Pavlik, Peter; Bradbury, Andrew R.  M.

doi:10.1093/nar/gkp809

Title: A comprehensive analysis of filamentous phage display vectors for cytoplasmic proteins: an analysis with different fluorescent proteins

Journal Article · 02 December 2009 · Nucleic Acids Research

DOI: https://doi.org/10.1093/nar/gkp809 · OSTI ID:1625467

Velappan, Nileena ^[1]; Fisher, Hugh E. ^[2]; Pesavento, Emanuele ^[2]; Chasteen, Leslie ^[2]; D'Angelo, Sara ^[2]; Kiss, Csaba ^[2]; Longmire, Michelle ^[2]; Pavlik, Peter ^[2]; Bradbury, Andrew R. M. ^[2]

Los Alamos National Lab. (LANL), Los Alamos, NM (United States); DOE/OSTI
Los Alamos National Lab. (LANL), Los Alamos, NM (United States)

Filamentous phage display has been extensively used to select proteins with binding properties of specific interest. Although many different display platforms using filamentous phage have been described, no comprehensive comparison of their abilities to display similar proteins has been conducted. This is particularly important for the display of cytoplasmic proteins, which are often poorly displayed with standard filamentous phage vectors. In this article, we have analyzed the ability of filamentous phage to display a stable form of green fluorescent protein and modified variants in nine different display vectors, a number of which have been previously proposed as being suitable for cytoplasmic protein display. Correct folding and display were assessed by phagemid particle fluorescence, and with anti-GFP antibodies. The poor correlation between phagemid particle fluorescence and recognition of GFP by antibodies, indicates that proteins may fold correctly without being accessible for display. The best vector used a twin arginine transporter leader to transport the displayed protein to the periplasm, and a coil-coil arrangement to link the displayed protein to g3p. This vector was able to display less robust forms of GFP, including ones with inserted epitopes, as well as fluorescent proteins of the Azami green series. It was also functional in mock selection experiments.

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Research Organization:: Los Alamos National Laboratory (LANL), Los Alamos, NM (United States)

Sponsoring Organization:: USDOE Laboratory Directed Research and Development (LDRD) Program; USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

Grant/Contract Number:: AC52-06NA25396

OSTI ID:: 1625467

Journal Information:: Nucleic Acids Research, Journal Name: Nucleic Acids Research Journal Issue: 4 Vol. 38; ISSN 0305-1048

Publisher:: Oxford University PressCopyright Statement

Country of Publication:: United States

Language:: English

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