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Glycobiology, 2001, Vol. 11, No. 8 693-701
© 2001 Oxford University Press

Peptides that mimic Candida albicans–derived ß-1,2-linked mannosides

Thierry Jouault1,2, Chantal Fradin2, Florence Dzierszinski3, Margareth Borg-Von-Zepelin4, Stanislas Tomavo3, Robert Corman5, Pierre-André Trinel2, Jean-Pierre Kerckaert6 and Daniel Poulain2

2Laboratoire de Mycologie Fondamentale et Appliquée, INSERM EPI 9915, Université de Lille II, Faculté de Médecine H. Warembourg, Pôle Recherche, Place Verdun, 59037 Lille Cedex, France, 3Laboratoire de Chimie Biologique, CNRS UMR 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d’Ascq Cedex, France, 4Zentrum für Hygiene und Humangenetik, Göttingen University, 37075 Göttingen, Germany, 5Eurogentec Bel S.A, Parc industriel des Hauts Sarts, B-4040 Herstal, Belgium, and 6INSERM U524, Cité hospitalière, Place de Verdun, 59045 Lille Cedex, France.

ß-1,2-linked mannosides from Candida albicans phosphopeptidomannan (PPM) bind to macrophages through a receptor independent from the macrophage {alpha}-linked mannose receptor and stimulate these cells to secrete immune mediators. Anti-ß-1,2-linked mannoside but not anti-{alpha}-linked mannoside antibodies produced after immunization with neoglycoproteins protect animals from disseminated candidiasis. In this study, peptides that mimic ß-1,2-linked mannosides were isolated using phage display methodology. A phage library expressing random peptides was panned with an anti-ß-1,2-linked mannoside monoclonal antibody (mAb). After three rounds of biopanning, the isolated phages were able to inhibit recognition of C. albicans by the mAb. Sixty percent of the phages had an identical DNA insert corresponding to the peptide sequence FHENWPS that was recognized specifically by the mAb. Injection of KLH-coupled peptide into mice generated high titers of polyclonal antibodies against C. albicans yeast cell walls. The anti-FHENWPS antibodies bound to C. albicans PPM and were inhibited by soluble ß-1,2-mannotetraose. Together, these data provide evidence for mimotopic activity of the peptide selected by biopanning with the anti-ß-1,2-oligomannoside mAb.

1 To whom correspondence should be addressed


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