Selection of Peptides Targeting Helix 31 of Bacterial 16S Ribosomal RNA by Screening M13 Phage-Display Libraries

Background: Phage display is a biotechnological technique that presents peptides with coated proteins on the surface of phage. In the last two decades, growing applications of phage display in various fields of biotechnology have been investigated. Phage display libraries allow to present billions of peptides on phage surface for selection of a specific peptide with the desired affinity. Objective: In this regard, high-affinity phage antibodies against tumor antigens are produced and applied for diagnosis and treatment of cancer. Method: Moreover, phage display libraries are employed to select the high affinity T Cell Receptors (TCRs) for the peptide-MHC complex which is an attractive approach in cancer immunotherapy. Due to immunogenic properties of phage particles, phage-based vaccines do not require adjuvant, in addition the phage particles can effectively take up by Antigen Presenting Cells (APCs). Results: Taken together, phage-based cancer vaccines are ideal candidates that provide a key for eradication of tumor cells. Conclusion: In this review, we focus on various applications of a phage display platform in different types of cancer immunotherapy approaches.

Download Full-text

The anti-Shine-Dalgarno region in Escherichia coli 16S ribosomal RNA is not essential for the correct selection of translational starts

Biochemistry ◽

10.1021/bi00465a037 ◽

1990 ◽

Vol 29 (13) ◽

pp. 3402-3407 ◽

Cited By ~ 39

Author(s):

Pierre Melancon ◽

Daniel Leclerc ◽

Nathalie Destroismaisons ◽

Lea Brakier-Gingras

Keyword(s):

Escherichia Coli ◽

Ribosomal Rna ◽

16S Ribosomal Rna ◽

Correct Selection ◽

Selection Of

Download Full-text

Phage Display Selection of P1 Mutants of BPTI Directed against Five Different Serine Proteinases

Biological Chemistry ◽

10.1515/bc.1999.014 ◽

1999 ◽

Vol 380 (1) ◽

Cited By ~ 7

Author(s):

L. Kiczak ◽

K. Koscielska ◽

J. Otlewski ◽

M. Czerwinski ◽

M. Dadlez

Keyword(s):

Phage Display ◽

Trypsin Inhibitor ◽

Association Constant ◽

Serine Proteinases ◽

Wild Type ◽

Association Energy ◽

Basic Pancreatic Trypsin Inhibitor ◽

Pancreatic Trypsin Inhibitor ◽

M13 Phage ◽

Selection Of

AbstractThe P1 position of protein inhibitors and oligopeptide substrates determines, to a large extent, association energy with many serine proteinases. To test the agreement of phage display selection with the existing thermodynamic data, a small library of all 20 P1 mutants of basic pancreatic trypsin inhibitor (BPTI) was created, fused to protein III, and displayed on the surface of M13 phage. The wild type of displayed inhibitor monovalently and strongly inhibited trypsin with an association constant of

Download Full-text

Phage display as a tool to study human autoantibodies and autoantigens in systemic autoimmune disease. Selection of recombinant (auto)-antibodies specific for human autoantigens in rheumatic disease (RA, SLE, SSc) from human autoimmune-patient and immunized chicken derived phage display libraries

Arthritis Research & Therapy ◽

10.1186/ar285 ◽

2001 ◽

Vol 3 (S2) ◽

Author(s):

J Raats ◽

W Degen ◽

S Litjens ◽

I Bulduk ◽

G Mans ◽

...

Keyword(s):

Autoimmune Disease ◽

Rheumatic Disease ◽

Phage Display ◽

Systemic Autoimmune Disease ◽

Phage Display Libraries ◽

Selection Of

Download Full-text

Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1700407114 ◽

2017 ◽

Vol 114 (25) ◽

pp. 6444-6449 ◽

Cited By ~ 32

Author(s):

Anna Munke ◽

Jonas Persson ◽

Tanja Weiffert ◽

Erwin De Genst ◽

Georg Meisl ◽

...

Keyword(s):

Phage Display ◽

Amyloid Fibrils ◽

Amyloid Β ◽

Amyloid Β Peptide ◽

Nucleation Process ◽

Single Chain ◽

Secondary Nucleation ◽

Single Chain Antibody ◽

Phage Display Libraries ◽

Selection Of

The aggregation of the amyloid β peptide (Aβ) into amyloid fibrils is a defining characteristic of Alzheimer’s disease. Because of the complexity of this aggregation process, effective therapeutic inhibitors will need to target the specific microscopic steps that lead to the production of neurotoxic species. We introduce a strategy for generating fibril-specific antibodies that selectively suppress fibril-dependent secondary nucleation of the 42-residue form of Aβ (Aβ42). We target this step because it has been shown to produce the majority of neurotoxic species during aggregation of Aβ42. Starting from large phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach that we describe includes (i) selection of scFvs with high affinity for Aβ42 fibrils after removal of scFvs that bind Aβ42 in its monomeric form; (ii) ranking, by surface plasmon resonance affinity measurements, of the resulting candidate scFvs that bind to the Aβ42 fibrils; and (iii) kinetic screening and analysis to find the scFvs that inhibit selectively the fibril-catalyzed secondary nucleation process in Aβ42 aggregation. By applying this approach, we have identified four scFvs that inhibit specifically the fibril-dependent secondary nucleation process. Our method also makes it possible to discard antibodies that inhibit elongation, an important factor because the suppression of elongation does not target directly the production of toxic oligomers and may even lead to its increase. On the basis of our results, we suggest that the method described here could form the basis for rationally designed immunotherapy strategies to combat Alzheimer’s and related neurodegenerative diseases.

Download Full-text