Novel peptides binding to the Fc-portion of immunoglobulins obtained from a combinatorial phage display peptide library

Krook, Margareta; Mosbach, Klaus; Ramström, Olof

doi:10.1016/s0022-1759(98)00177-x

Cited by 16 publications

(17 citation statements)

References 20 publications

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“…Fassina et al used peptide derivatives as affinity ligands, which have broader specificity to IgG than Protein A, and applied them to antibody affinity chromatography (4). Ehrlish and Bailon, and Krook et al also reported IgGbinding peptides discovered using the filamentous phage display technique (5,6). Recently, Verdoliva et al screened a synthetic peptide library and identified an IgG-binding cyclic dimeric peptide that recognized the lower hinge region of IgG (7,8).…”

mentioning

confidence: 99%

Discovery and Characterization of a Peptide Motif That Specifically Recognizes a Non-native Conformation of Human IgG Induced by Acidic pH Conditions

Sakamoto

Ito

Hatanaka

et al. 2009

Journal of Biological Chemistry

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In therapeutic antibody preparation, acidic pH conditions are generally used for elution from Protein A affinity column of IgG or for its viral inactivation. Exposing IgG to low pH conditions induces conformational changes, leading to its functional damage or loss, although the mechanisms have not been fully elucidated. In this study using random peptide T7 phage display libraries, we isolated a unique and novel peptide motif that specifically recognized the non-native conformer (acid conformer) of human IgG that was generated by the low pH treatment, but not the native conformer. We examined the generation conditions and biochemical properties of acid conformer using the peptide motif as an affinity ligand. The acid conformer was easily generated at acidic pH (25°C). The peptides isolated here could contribute to the elucidation of the mechanisms of antibody dysfunction or aggregation during acid exposure as well as storage of human IgG.

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confidence: 99%

Discovery and Characterization of a Peptide Motif That Specifically Recognizes a Non-native Conformation of Human IgG Induced by Acidic pH Conditions

Sakamoto

Ito

Hatanaka

et al. 2009

Journal of Biological Chemistry

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“…TUPs scan in SAROTUP found only partial homology within the three amino acid sequence (SSL) of dodecapeptide M13 with the peptide FARLVSSIRY, which compete for the protein A binding site [45]. No hits were found in the MimoDB database for the phagotopes described in Table 1.…”

Section: Resultsmentioning

confidence: 99%

Phage-displayed peptides that mimic epitopes of hepatitis E virus capsid

Larralde

Petrík

2017

Med Microbiol Immunol

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Hepatitis E is an emerging zoonotic infection of increasing public health threat for the UK, especially for immunosuppressed individuals. A human recombinant vaccine has been licensed only in China and is not clear whether it protects against hepatitis E virus (HEV) genotype 3, the most prevalent in Europe. The aim of this study was to use phage display technology as a tool to identify peptides that mimic epitopes of HEV capsid (mimotopes). We identified putative linear and conformational mimotopes using sera from Scottish blood donors that have the immunological imprint of past HEV infection. Four mimotopes did not have homology with the primary sequence of HEV ORF2 capsid but competed effectively with a commercial HEV antigen for binding to anti-HEV reference serum. When the reactivity profile of each mimotope was compared with Wantai HEV-IgG ELISA, the most sensitive HEV immunoassay, mimotopes showed 95.2-100% sensitivity while the specificity ranged from 81.5 to 95.8%. PepSurf algorithm was used to map affinity-selected peptides onto the ORF2 crystal structure of HEV genotype 3, which predicted that these four mimototopes are clustered in the P domain of ORF2 capsid, near conformational epitopes of anti-HEV neutralising monoclonal antibodies. These HEV mimotopes may have potential applications in the design of structural vaccines and the development of new diagnostic tests.

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“…Peptides that bind with high affinity to the Fc region of human IgG have been selectively identified in screenings of PDPLs [41][42][43]. Ehrlich and Bailon [41] screened two PDPLs with the Fc of a humanized monoclonal antibody and, among multiple sequences, found the motif SS[I/L] ( Table 4).…”

Section: Ss[i/l] Motifmentioning

confidence: 99%

“…Ehrlich and Bailon [41] screened two PDPLs with the Fc of a humanized monoclonal antibody and, among multiple sequences, found the motif SS[I/L] ( Table 4). Krook et al [42] isolated clones bearing the sequence SSI, by screening a decapeptide library with a commercial preparation of human IgG Fc and eluting with protein A. One clone containing the SSI motif was found to compete with protein A for binding to the screening Fc, suggesting that it interacts with the protein-A-binding site on human IgG Fc.…”

Section: Ss[i/l] Motifmentioning

confidence: 99%

“…In summary, peptides bearing the SS[I/L] sequence have been isolated in screenings with a wide variety of antibody targets; they have been associated with binding to the Ig-Fc [41,42] and to xenoreactive (polyreactive) human antibodies [52]. It can be argued that the emergence of the SSL motif is due to bias in the randomized library DNA sequence, which contains three codons for both Ser and Leu.…”

Section: Ss[i/l] Motifmentioning

confidence: 99%

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The nature of target-unrelated peptides recovered in the screening of phage-displayed random peptide libraries with antibodies

Menéndez

Scott

2005

Analytical Biochemistry

114

105

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Novel peptides binding to the Fc-portion of immunoglobulins obtained from a combinatorial phage display peptide library

Cited by 16 publications

References 20 publications

Discovery and Characterization of a Peptide Motif That Specifically Recognizes a Non-native Conformation of Human IgG Induced by Acidic pH Conditions

Discovery and Characterization of a Peptide Motif That Specifically Recognizes a Non-native Conformation of Human IgG Induced by Acidic pH Conditions

Phage-displayed peptides that mimic epitopes of hepatitis E virus capsid

The nature of target-unrelated peptides recovered in the screening of phage-displayed random peptide libraries with antibodies

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