GD3‐replica peptides selected from a phage peptide library induce a GD3 ganglioside antibody response

Popa, Iuliana; Ishikawa, Dai; Tanaka, Motoyasu; Ogino, Kōichi; Portoukalian, Jacques; Taki, Takao

doi:10.1016/j.febslet.2006.01.063

Cited by 17 publications

(27 citation statements)

References 29 publications

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“…From comparison of the ganglioside- and peptide-derived site maps (Figure 6), the peptide appears to be a partial structural mimic of GD3 [20]. This partial structural mimicry could account for the observed immunological mimicry of GD3 by this peptide [25].…”

Section: Resultsmentioning

confidence: 94%

“…Peptides have been considered for this purpose against a wide range of targets [20]. Peptide mimics of the GD2 [21], [22], [23] and GD3 [24], [25] gangliosides have been identified, typically by phage display against anti-ganglioside antibodies. Some of these have been found to induce anti-ganglioside immune responses [23], [25], [26].…”

Section: Introductionmentioning

confidence: 99%

“…Peptide mimics of the GD2 [21], [22], [23] and GD3 [24], [25] gangliosides have been identified, typically by phage display against anti-ganglioside antibodies. Some of these have been found to induce anti-ganglioside immune responses [23], [25], [26]. Peptide mimics of anti-Neu5Gc-GM3 antibodies are not currently known, however, anti-idiotypic antibodies against these antibodies have been identified [27], [28].…”

Section: Introductionmentioning

confidence: 99%

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Antibody Recognition of Cancer-Related Gangliosides and Their Mimics Investigated Using in silico Site Mapping

2012

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Modified gangliosides may be overexpressed in certain types of cancer, thus, they are considered a valuable target in cancer immunotherapy. Structural knowledge of their interaction with antibodies is currently limited, due to the large size and high flexibility of these ligands. In this study, we apply our previously developed site mapping technique to investigate the recognition of cancer-related gangliosides by anti-ganglioside antibodies. The results reveal a potential ganglioside-binding motif in the four antibodies studied, suggesting the possibility of structural convergence in the anti-ganglioside immune response. The structural basis of the recognition of ganglioside-mimetic peptides is also investigated using site mapping and compared to ganglioside recognition. The peptides are shown to act as structural mimics of gangliosides by interacting with many of the same binding site residues as the cognate carbohydrate epitopes. These studies provide important clues as to the structural basis of immunological mimicry of carbohydrates.

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Section: Resultsmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Antibody Recognition of Cancer-Related Gangliosides and Their Mimics Investigated Using in silico Site Mapping

2012

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“…Several peptides mimicking carbohydrate have been found using phage-displayed libraries. [21][22][23][24][25][26] O et al also identified the dodecapeptide (DLWDWVVGKPAG) mimicking sLe a by screening a phage-displayed library using monoclonal antibody NS19-9. …”

mentioning

confidence: 99%

“…The previously reported peptides mimicking carbohydrates contained an aromatic amino acid, such as Phe, Tyr and Trp residues. [21][22][23][24][25][26][27] It was reported that the hydroxyl group of Tyr residue could mimic the OH group of sugar, and carbons of the aromatic side chain of Phe or Trp residue could mimic sugar carbons. The existence of an aromatic or branched aliphatic amino acid in carbohydrate-mimicking peptides could reflect that the binding between carbohydrates and anti-carbohydrate antibodies (or lectins) is mainly occupied by hydrophobic interaction.…”

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confidence: 99%

Identification of a Novel Carbohydrate-Mimicking Octapeptide from Chemical Peptide Library and Characterization as Selectin Inhibitor

Kawano

Iyaguchi

Sasaki

et al. 2011

Biological & Pharmaceutical Bulletin

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Selectins are a family of integral membrane glycoproteins that mediate adhesion between leukocytes and endothelial cells during the transient rolling phase of leukocyte migration.1-3) The selectin family consists of three glycoprotein members: E-, P-and L-selectins. E-and P-selectins are expressed on activated endothelium, whereas L-selectin is constitutively expressed on neutrophils, monocytes, and most lymphocytes. P-selectin mediates attachment and is translocated to the surface of the endothelium within minutes of activation. E-selectin mediates slow rolling and is expressed after several hours on the activated cell surface. 4,5) Each selectin has a calcium-dependent carbohydrate binding domain (C-type lectin domain) in its amino-terminal, followed by an epidermal growth factor-like domain, variable numbers of complement regulatory-like units, a transmembrane domain and an intracellular region. The adhesion activity of the selectins is mediated primarily by the binding of sialyl Lewis X (sLe X ) (NeuAca2→3Galb1→4(Fuca1→3)GlcNAc-R, Fig. 1) on the leukocyte to the carbohydrate-binding domain on activated endothelial cells. [6][7][8][9][10][11] In a productive immune response, this leads to isolation of infection; however, overzealous transfer of leukocytes causes widespread tissue damage, leading to several disease states, such as reperfusion injury, cardiovascular diseases, and allergic diseases.5) Inhibition of selectin-mediated rolling is a possible means of controlling inflammation-induced diseases. Therefore, the development of selectin inhibitors, which are able to control the leukocyte-endothelia cell adhesion process, is an excellent therapeutic target to treat inflammatory diseases.It is well known that all selectins recognize the carbohydrate structure of sLe X and sialyl Lewis a (sLe a ), an isomer of sLe X ; therefore, most reported selectin inhibitors are carbohydrate-based molecules mimicking sLe X or sLe a and antibodies.5,12-20) However, they have drawbacks as therapeutics, i.e., carbohydrate chains are difficult to synthesize in high yield and purity, and carbohydrate-based molecules are generally prone to rapid metabolism and elimination. On the other hand, antibodies have potential immunogenicity, high cost, and other possible side effects.The phage-displayed library is a representative method based on affinity binding between the displayed library and the target molecule or tissue. Recently, cloning of carbohydrate mimetic peptides within a short term has become available by the phage-displayed peptide library method. Several peptides mimicking carbohydrate have been found using phage-displayed libraries. [21][22][23][24][25][26] O et al. also identified the dodecapeptide (DLWDWVVGKPAG) mimicking sLe a by screening a phage-displayed library using monoclonal antibody NS19-9. 27)Generally, the synthesis of a long peptide in high yield and purity is difficult, and long or large peptides have relatively high antigenicity. Thus, short peptides are necessary to overcome the therapeutic drawbacks....

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Anti-glycolipid Antibodies in Guillain-Barré Syndrome and Related Neuropathies: Therapeutic Strategies for Disease Treatment

Usuki

Ariga

2011

Anticarbohydrate Antibodies

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GD3‐replica peptides selected from a phage peptide library induce a GD3 ganglioside antibody response

Cited by 17 publications

References 29 publications

Antibody Recognition of Cancer-Related Gangliosides and Their Mimics Investigated Using in silico Site Mapping

Antibody Recognition of Cancer-Related Gangliosides and Their Mimics Investigated Using in silico Site Mapping

Identification of a Novel Carbohydrate-Mimicking Octapeptide from Chemical Peptide Library and Characterization as Selectin Inhibitor

Anti-glycolipid Antibodies in Guillain-Barré Syndrome and Related Neuropathies: Therapeutic Strategies for Disease Treatment

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