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Phage and Yeast Display

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  • Authors: Jared Sheehan1, Wayne A. Marasco2
  • Editors: James E. Crowe Jr.3, Diana Boraschi4, Rino Rappuoli5
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02215; 2: Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02215; 3: Vanderbilt University School of Medicine, Nashville, TN; 4: National Research Council, Pisa, Italy; 5: Novartis Vaccines, Siena, Italy
    • Source: microbiolspec February 2015 vol. 3 no. 1 doi:10.1128/microbiolspec.AID-0028-2014
  • Received 05 December 2014 Accepted 06 December 2014 Published 06 February 2015
  • Wayne A. Marasco, [email protected]
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  • Abstract:

    Despite the availability of antimicrobial drugs, the continued development of microbial resistance—established through escape mutations and the emergence of resistant strains—limits their clinical utility. The discovery of novel, therapeutic, monoclonal antibodies (mAbs) offers viable clinical alternatives in the treatment and prophylaxis of infectious diseases. Human mAb-based therapies are typically nontoxic in patients and demonstrate high specificity for the intended microbial target. This specificity prevents negative impacts on the patient microbiome and avoids driving the resistance of nontarget species. The selection of human antibody fragment libraries displayed on phage or yeast surfaces represents a group of well-established technologies capable of generating human mAbs. The advantage of these forms of microbial display is the large repertoire of human antibody fragments present during a single selection campaign. Furthermore, the selection environments of microbial surface display allow for the rapid isolation of antibodies—and their encoding genes—against infectious pathogens and their toxins that are impractical within systems, such as murine hybridomas. This article focuses on the technologies of phage display and yeast display, as these strategies relate to the discovery of human mAbs for the treatment and vaccine development of infectious diseases.

  • Citation: Sheehan J, Marasco W. 2015. Phage and Yeast Display. Microbiol Spectrum 3(1):AID-0028-2014. doi:10.1128/microbiolspec.AID-0028-2014.

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/content/journal/microbiolspec/10.1128/microbiolspec.AID-0028-2014
2015-02-06
2020-07-12

Abstract:

Despite the availability of antimicrobial drugs, the continued development of microbial resistance—established through escape mutations and the emergence of resistant strains—limits their clinical utility. The discovery of novel, therapeutic, monoclonal antibodies (mAbs) offers viable clinical alternatives in the treatment and prophylaxis of infectious diseases. Human mAb-based therapies are typically nontoxic in patients and demonstrate high specificity for the intended microbial target. This specificity prevents negative impacts on the patient microbiome and avoids driving the resistance of nontarget species. The selection of human antibody fragment libraries displayed on phage or yeast surfaces represents a group of well-established technologies capable of generating human mAbs. The advantage of these forms of microbial display is the large repertoire of human antibody fragments present during a single selection campaign. Furthermore, the selection environments of microbial surface display allow for the rapid isolation of antibodies—and their encoding genes—against infectious pathogens and their toxins that are impractical within systems, such as murine hybridomas. This article focuses on the technologies of phage display and yeast display, as these strategies relate to the discovery of human mAbs for the treatment and vaccine development of infectious diseases.

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Figures

Phage and Yeast Display
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Citation: Sheehan J, Marasco W. 2015. Phage and yeast display. microbiolspec 3(1): doi:10.1128/microbiolspec.AID-0028-2014
/content/microbiolspec/10.1128/microbiolspec.AID-0028-2014.fig1
FIGURE 1
Overview of phage antibody library production and selections. (A) The phage antibody library repertoire is derived from the B cells of naïve or immune donors. The amplified and genes are subcloned into a phage display vector for expression and library production. (B) The phage antibody library is selected against an immobilized target antigen. After washing to remove nonbinders, the Ag-reactive phage antibodies are eluted, amplified, and reselected through subsequent rounds. ELISA screens identify monoclonal, Ag-binding phage antibodies, whose heavy and light chain antibody genes are subcloned into mammalian expression vectors.
microbiolspec/3/1/AID-0028-2014-fig1_thmb.gif
microbiolspec/3/1/AID-0028-2014-fig1.gif
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FIGURE 1

Overview of phage antibody library production and selections. (A) The phage antibody library repertoire is derived from the B cells of naïve or immune donors. The amplified and genes are subcloned into a phage display vector for expression and library production. (B) The phage antibody library is selected against an immobilized target antigen. After washing to remove nonbinders, the Ag-reactive phage antibodies are eluted, amplified, and reselected through subsequent rounds. ELISA screens identify monoclonal, Ag-binding phage antibodies, whose heavy and light chain antibody genes are subcloned into mammalian expression vectors.

Source: microbiolspec February 2015 vol. 3 no. 1 doi:10.1128/microbiolspec.AID-0028-2014
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FIGURE 2
Types of phage antibody display. (A) Monovalent display with the scFv or Fab fusion (green circle) to truncated pIII along with wild-type copies of pIII (purple circles). This monovalent mAb display format can also be used with pVII (olive) or pIX (light blue) separately. (B) Multivalent display with the scFv or Fab fusion to all copies of truncated pIII. Multivalent mAb display is also possible with the major coat protein pVIII (black border) separate from pIII. The pVI (red circles) coat proteins are also present in these diagrams.
microbiolspec/3/1/AID-0028-2014-fig2_thmb.gif
microbiolspec/3/1/AID-0028-2014-fig2.gif
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FIGURE 2

Types of phage antibody display. (A) Monovalent display with the scFv or Fab fusion (green circle) to truncated pIII along with wild-type copies of pIII (purple circles). This monovalent mAb display format can also be used with pVII (olive) or pIX (light blue) separately. (B) Multivalent display with the scFv or Fab fusion to all copies of truncated pIII. Multivalent mAb display is also possible with the major coat protein pVIII (black border) separate from pIII. The pVI (red circles) coat proteins are also present in these diagrams.

Source: microbiolspec February 2015 vol. 3 no. 1 doi:10.1128/microbiolspec.AID-0028-2014
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FIGURE 3
Overview of yeast antibody display. The scFv (or Fab) is displayed as a fusion product with the Aga2p protein (light blue). This fusion product can be detected and normalized by fluorescent signaling through the HA tags (orange) and c-Myc tags (dark blue). During FACS selections, the Ag-reactive library variants are detected through the fluorescent avidin tag (pink) on the biotinylated target antigen (red).
microbiolspec/3/1/AID-0028-2014-fig3_thmb.gif
microbiolspec/3/1/AID-0028-2014-fig3.gif
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FIGURE 3

Overview of yeast antibody display. The scFv (or Fab) is displayed as a fusion product with the Aga2p protein (light blue). This fusion product can be detected and normalized by fluorescent signaling through the HA tags (orange) and c-Myc tags (dark blue). During FACS selections, the Ag-reactive library variants are detected through the fluorescent avidin tag (pink) on the biotinylated target antigen (red).

Source: microbiolspec February 2015 vol. 3 no. 1 doi:10.1128/microbiolspec.AID-0028-2014
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Tables

Phage and Yeast Display
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Citation: Sheehan J, Marasco W. 2015. Phage and yeast display. microbiolspec 3(1): doi:10.1128/microbiolspec.AID-0028-2014
/content/microbiolspec/10.1128/microbiolspec.AID-0028-2014.T1
TABLE 1
Summary of antiviral antibodies discovered using phage display
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TABLE 1

Summary of antiviral antibodies discovered using phage display

Source: microbiolspec February 2015 vol. 3 no. 1 doi:10.1128/microbiolspec.AID-0028-2014
/content/microbiolspec/10.1128/microbiolspec.AID-0028-2014.T2
TABLE 2
Summary of antibacterial antibodies discovered using phage display
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TABLE 2

Summary of antibacterial antibodies discovered using phage display

Source: microbiolspec February 2015 vol. 3 no. 1 doi:10.1128/microbiolspec.AID-0028-2014
/content/microbiolspec/10.1128/microbiolspec.AID-0028-2014.T3
TABLE 3
Summary of antiviral antibodies discovered using yeast display
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TABLE 3

Summary of antiviral antibodies discovered using yeast display

Source: microbiolspec February 2015 vol. 3 no. 1 doi:10.1128/microbiolspec.AID-0028-2014
/content/microbiolspec/10.1128/microbiolspec.AID-0028-2014.T4
TABLE 4
Summary of antibacterial antibodies discovered using yeast display
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TABLE 4

Summary of antibacterial antibodies discovered using yeast display

Source: microbiolspec February 2015 vol. 3 no. 1 doi:10.1128/microbiolspec.AID-0028-2014

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