Selection of a human anti-progesterone antibody fragment from a transgenic mouse library by ARM ribosome display

He, Mingyue; Menges, Margit; Groves, Maria; Corps, Elaine M.; Liu, Hong; Brüggemann, Marianne; Taussig, Michael J.

doi:10.1016/s0022-1759(99)00144-1

Cited by 68 publications

(27 citation statements)

References 26 publications

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“…Although ribosome display has many advantages over phage display, to the best of our knowledge only four reports have been published about antibody selection from a library using ribosome display (Hanes et al, 1998(Hanes et al, , 2000He et al, 1999;Schaffitzel et al, 2001). Moreover, only one of these described selection using a eukaryotic translation system (He et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, only one of these described selection using a eukaryotic translation system (He et al, 1999). Therefore, our work is valuable as an example of selection of an antibody from an antibody library by ribosome display using a eukaryotic translation system.…”

Section: Discussionmentioning

confidence: 99%

“…The PCR products obtained are then used for the next cycle of enrichment. This method was originally developed as an efficient tool for obtaining scFvs that have binding affinity to target antigen (Hanes and Pluckthun, 1997;He and Taussig, 1997), and some antibodies with high affinity have been selected and evolved from mouse and human libraries using this method (Hanes et al, 1998(Hanes et al, , 2000He et al, 1999). The advantages of ribosome display are that, in comparison to phage display, larger libraries can be constructed without the transformation step, and the libraries can be further diversified by PCR during ribosome display (Dall'Acqua and Carter, 1998).…”

Section: Introductionmentioning

confidence: 99%

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Selection of scFvs specific for HBV DNA polymerase using ribosome display

Lee

Kwon

Kim

et al. 2004

Journal of Immunological Methods

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Selection of scFvs specific for HBV DNA polymerase using ribosome display

Lee

Kwon

Kim

et al. 2004

Journal of Immunological Methods

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“…The feasibility of carrying out ribosome display in a eukaryotic cell-free translation extracts was subsequently demonstrated with an scFv-kappa fusion ( 39 ) , and then by selecting an antibody in the same format from immunized transgenic mice ( 40 ) .…”

Section: Development Of Ribosome Displaymentioning

confidence: 99%

Ribosome Display: A Perspective

Plückthun

2011

Methods in Molecular Biology

116

106

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Ribosome display is an in vitro evolution technology for proteins. It is based on in vitro translation, but prevents the newly synthesized protein and the mRNA encoding it from leaving the ribosome. It thereby couples phenotype and genotype. Since no cells need to be transformed, very large libraries can be used directly in selections, and the in vitro amplification provides a very convenient integration of random mutagenesis that can be incorporated into the procedure. This review highlights concepts, mechanisms, and different variations of ribosome display and compares it to related methods. Applications of ribosome display are summarized, e.g., the directed evolution of proteins for higher binding affinity, for higher stability or other improved biophysical parameters and enzymatic properties. Ribosome display has developed into a robust technology used in academia and industry alike, and it has made the cell-free Darwinian evolution of proteins over multiple generations a reality.

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“…7) has previously been described as an alternative display method for both the selection (8)(9)(10)) and evolution of ligand-binding proteins. It works by transcribing a library of DNA to mRNA, translating it in vitro with stoichiometric amounts of ribosomes such that at the end of the reaction, the protein (as peptidyl-tRNA), and the mRNA are still connected to the ribosome.…”

mentioning

confidence: 99%

Tailoringin vitroevolution for protein affinity or stability

Jermutus

Honegger

Schwesinger

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

162

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We describe a rapid and general technology working entirely in vitro to evolve either the affinity or the stability of ligand-binding proteins, depending on the chosen selection pressure. Tailored in vitro selection strategies based on ribosome display were combined with in vitro diversification by DNA shuffling to evolve either the off-rate or thermodynamic stability of single-chain Fv antibody fragments (scFvs). To demonstrate the potential of this method, we chose to optimize two proteins already possessing favorable properties. A scFv with an initial affinity of 1.1 nM (koff at 4°C of 10 ؊4 s ؊1 ) was improved 30-fold by the use of off-rate selections over a period of several days. As a second example, a generic selection strategy for improved stability exploited the property of ribosome display that the conditions can be altered under which the folding of the displayed protein occurs. We used decreasing redox potentials in the selection step to select for molecules stable in the absence of disulfide bonds. They could be functionally expressed in the reducing cytoplasm, and, when allowed to form disulfides again, their stability had increased to 54 kJ͞mol from an initial value of 24 kJ͞mol. Sequencing revealed that the evolved mutant proteins had used different strategies of residue changes to adapt to the selection pressure. Therefore, by a combination of randomization and appropriate selection strategies, an in vitro evolution of protein properties in a predictable direction is possible.

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Selection of a human anti-progesterone antibody fragment from a transgenic mouse library by ARM ribosome display

Cited by 68 publications

References 26 publications

Selection of scFvs specific for HBV DNA polymerase using ribosome display

Selection of scFvs specific for HBV DNA polymerase using ribosome display

Ribosome Display: A Perspective

Tailoringin vitroevolution for protein affinity or stability

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