Peptidic sequence “HSEAETGPP” is recognized by the sera of pars planitis patients

Purpose: HLA class II, p-36 protein, heat shock protein and retinal antigens have been associated with pars planitis (PP), but their participation in the development of the disease are unknown. A search for new molecules related to PP is necessary. This work focused on the identification of peptides recognized by PP patient sera using the phage display method. Methods: Sera of PP patients were used to isolate peptides fused to M13-phage pIII protein. The response of PP and healthy sera to peptides was determined by ELISA. PCR amplification and sequencing of peptide-encoding fragments from clones with high recognition by PP sera were used to characterize displayed peptides. Results: One hundred clones were randomly selected from a phage display library after three panning rounds using serum proteins from a PP patient. The immunologic response level of 100 clones selected were determined with a major number of patients, it was found that one clone was recognized stronger in PP patients sera than in healthy sera (PP vs. healthy; P < 0.05). The peptide-encoding region of this clone was sequenced and translated. The peptide sequence corresponded to HSEAETGPP. An identical amino acid sequence to HSEAETGPP is found in the human proline-rich transmembrane protein 2 which has not been related with eye diseases. Conclusion: These results suggest that the peptide HSEAETGPP is associated with PP.

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In vitro selection of high affinity anti-retinal antigens (S-antigen, IRBP, rhodopsin) antibodies from a combinatorial phage display library derived from a patient with autoimmune uveitis

Immunology Letters ◽

10.1016/s0165-2478(97)86521-2 ◽

1997 ◽

Vol 56 ◽

pp. 377

Author(s):

S. O'Brien ◽

J. Liversidge ◽

J.V. Forrester ◽

W.J. Harris

Keyword(s):

Phage Display ◽

In Vitro Selection ◽

Phage Display Library ◽

Autoimmune Uveitis ◽

High Affinity ◽

Retinal Antigens ◽

Selection Of

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Isolation of Peptide Ligands that Inhibit Glutamate Racemase Activity from a Random Phage Display Library

CrossRef Listing of Deleted DOIs ◽

10.1177/108705710000500606 ◽

2000 ◽

Vol 5 (6) ◽

pp. 435-440 ◽

Cited By ~ 12

Author(s):

Woo-Chang Kim ◽

Hae-Ik Rhee ◽

Boo-Kil Park ◽

Kyoung-Ho Suk ◽

Sang-Hoon Cha

Keyword(s):

Cell Wall ◽

Phage Display ◽

Antibacterial Agents ◽

Bacterial Resistance ◽

Phage Display Library ◽

Peptide Sequence ◽

Membrane Function ◽

Glutamate Racemase ◽

Positive Phage

Several new antibacterial agents are currently being developed in response to the emergence of bacterial resistance to existing antibiotic substances. The new agents include compounds that interfere with bacterial membrane function. The peptidoglycan component of the bacterial cell wall is synthesized by glutamate racemase, and this enzyme is responsible for the biosynthesis of d-glutamate, which is an essential component of cell wall peptidoglycan. In this study, we screened a phage display library expressing random dodecapeptides on the surface of bacteriophage against an Escherichia coli glutamate racemase, and isolated specific peptide sequences that bind to the enzyme. Twenty-seven positive phage clones were analyzed, and seven different peptide sequences were obtained. Among them, the peptide sequence His-Pro-Trp-His-Lys-Lys-His-Pro-Asp-Arg-Lys-Thr was found most frequently, suggesting that this peptide might have the highest affinity to glutamate racemase. The positive phage clones and HPWHKKHPDRKT synthetic peptide were able to inhibit glutamate racemase activity in vitro, implying that our peptide inhibitors may be utilized for the molecular design of new potential antibacterial agents targeting cell wall synthesis.

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In vitro selection of high affinity anti-retinal antigens (S-antigen, IRBP, rhodopsin) antibodies from a combinatorial phage display library derived from a patient with autoimmune uveitis

Immunology Letters ◽

10.1016/s0165-2478(97)88361-7 ◽

1997 ◽

Vol 56 (1-3) ◽

pp. 377

Author(s):

S O'Brien

Keyword(s):

Phage Display ◽

In Vitro Selection ◽

Phage Display Library ◽

Autoimmune Uveitis ◽

High Affinity ◽

Retinal Antigens ◽

Selection Of

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M13 Bacteriophage-Assisted Biomineralization of Copper Sulfide

MRS Proceedings ◽

10.1557/opl.2012.1503 ◽

2012 ◽

Vol 1445 ◽

Author(s):

Mohammed Shahriar Zaman ◽

Elaine D. Haberer

Keyword(s):

Electron Microscopy ◽

Aqueous Solution ◽

Phage Display ◽

Copper Sulfide ◽

Room Temperature ◽

Phage Display Library ◽

Peptide Sequence ◽

Major Coat Protein ◽

M13 Bacteriophage ◽

Linear Chains

ABSTRACTCombinatorial phage display with a pVIII library of M13 bacteriophage was used to identify a peptide sequence capable of recognition and mineralization of copper sulfide. The six sequences isolated from the final biopanning round were rich in basic, hydrophobic, and polar amino acids compared to the phage display library. The peptide sequence, DTRAPEIV, was used to biomineralize copper sulfide on the pVIII major coat protein thus producing linear chains of nanoparticles. Electron microscopy revealed that the phage was capable of controlling the size of the nucleated nanoparticles in an aqueous solution at room temperature and that the mineralized material was copper sulfide. Phage-templated biomineralization is a low temperature, aqueous-based approach to synthesis of copper sulfide nanoparticles with hierarchical order.

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Detection of Cystic Fibrosis Serological Biomarkers Using a T7 Phage Display Library

Scientific Reports ◽

10.1038/s41598-017-18041-2 ◽

2017 ◽

Vol 7 (1) ◽

Cited By ~ 3

Author(s):

Harvinder Talwar ◽

Samer Najeeb Hanoudi ◽

Andreea Geamanu ◽

Dana Kissner ◽

Sorin Draghici ◽

...

Keyword(s):

Cystic Fibrosis ◽

Phage Display ◽

Phage Display Library ◽

T7 Phage Display ◽

Serological Biomarkers ◽

T7 Phage

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Production, characterization and in-vitro applications of single-domain antibody against thyroglobulin selected from novel T7 phage display library

Journal of Immunological Methods ◽

10.1016/j.jim.2021.112990 ◽

2021 ◽

Vol 492 ◽

pp. 112990

Author(s):

Jothivel Kumarasamy ◽

Samar Kumar Ghorui ◽

Chandrakala Gholve ◽

Bharti Jain ◽

Yogesh Dhekale ◽

...

Keyword(s):

Phage Display ◽

Phage Display Library ◽

Single Domain ◽

Single Domain Antibody ◽

Domain Antibody ◽

T7 Phage Display ◽

T7 Phage

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Stable heterodimers from remodeling the domain interface of a homodimer using a phage display library

Journal of Molecular Biology ◽

10.1006/jmbi.1997.1116 ◽

1997 ◽

Vol 270 (1) ◽

pp. 26-35 ◽

Cited By ~ 145

Author(s):

Shane Atwell ◽

John B.B Ridgway ◽

James A Wells ◽

Paul Carter

Keyword(s):

Phage Display ◽

Phage Display Library

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Isolation of a highly specific ligand for the alpha 5 beta 1 integrin from a phage display library

The Journal of Cell Biology ◽

10.1083/jcb.124.3.373 ◽

1994 ◽

Vol 124 (3) ◽

pp. 373-380 ◽

Cited By ~ 225

Author(s):

E Koivunen ◽

B Wang ◽

E Ruoslahti

Keyword(s):

Phage Display ◽

Cyclic Peptide ◽

Cell Attachment ◽

Phage Display Library ◽

Cell Binding ◽

Rgd Peptides ◽

Beta 1 Integrin ◽

Alpha V Beta 3 ◽

Integrin Ligand ◽

Specific Ligand

Our previous studies showed that the alpha 5 beta 1 integrin selects cysteine pair-containing RGD peptides from a phage display library based on a random hexapeptide. We have therefore searched for more selective peptides for this integrin using a larger phage display library, where heptapeptides are flanked by cysteine residues, thus making the inserts potentially cyclic. Most of the phage sequences that bound to alpha 5 beta 1 (69 of 125) contained the RGD motif. Some of the heptapeptides contained an NGR motif. As the NGR sequence occurs in the cell-binding region of the fibronectin molecule, this sequence could contribute to the specific recognition of fibronectin by alpha 5 beta 1. Selection for high affinity peptides for alpha 5 beta 1 surprisingly yielded a sequence RRETAWA that does not bear obvious resemblance to known integrin ligand sequences. The synthetic cyclic peptide GACRRETAWACGA (*CRRETAWAC*) was a potent inhibitor of alpha 5 beta 1-mediated cell attachment to fibronectin. This peptide is nearly specific for the alpha 5 beta 1 integrin, because much higher concentrations were needed to inhibit the alpha v beta 1 integrin, and there was no effect on alpha v beta 3- and alpha v beta 5-mediated cell attachment to vitronectin. The peptide also did not bind to the alpha IIb beta 3 integrin. *CRRETAWAC* appears to interact with the same or an overlapping binding site in alpha 5 beta 1 as RGD, because cell attachment to *CRRETAWAC* coated on plastic was divalent cation dependent and could be blocked by an RGD-containing peptide. These results reveal a novel binding specificity in the alpha 5 beta 1 integrin.

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Antibody design using LSTM based deep generative model from phage display library for affinity maturation

Scientific Reports ◽

10.1038/s41598-021-85274-7 ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

Koichiro Saka ◽

Taro Kakuzaki ◽

Shoichi Metsugi ◽

Daiki Kashiwagi ◽

Kenji Yoshida ◽

...

Keyword(s):

Phage Display ◽

Short Term Memory ◽

Current Method ◽

Phage Display Library ◽

Affinity Maturation ◽

Generative Model ◽

Sequence Generation ◽

Machine Learning Approach ◽

Antibody Design ◽

Ngs Data

AbstractMolecular evolution is an important step in the development of therapeutic antibodies. However, the current method of affinity maturation is overly costly and labor-intensive because of the repetitive mutation experiments needed to adequately explore sequence space. Here, we employed a long short term memory network (LSTM)—a widely used deep generative model—based sequence generation and prioritization procedure to efficiently discover antibody sequences with higher affinity. We applied our method to the affinity maturation of antibodies against kynurenine, which is a metabolite related to the niacin synthesis pathway. Kynurenine binding sequences were enriched through phage display panning using a kynurenine-binding oriented human synthetic Fab library. We defined binding antibodies using a sequence repertoire from the NGS data to train the LSTM model. We confirmed that likelihood of generated sequences from a trained LSTM correlated well with binding affinity. The affinity of generated sequences are over 1800-fold higher than that of the parental clone. Moreover, compared to frequency based screening using the same dataset, our machine learning approach generated sequences with greater affinity.

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