Investigation of the specificity of a monoclonal antibody C3.1 that binds to the phosphomannan of Candida albicans cell wall has aided the reverse engineering of a potential conjugate vaccine to combat this fungal infection. MAb C3.1 was preferentially inhibited by di- and trisaccharide, while larger oligosaccharides were progressively worse inhibitors. Chemical mapping of the binding sites of these antibodies in combination with NMR studies confirm the size and conformation of the protective epitope and establish the antigen surface contacting the antibody. Surprisingly the recognition unit is an internal �1,2-mannose disaccharide. Since linear epitopes of a homo-oligosaccharide may frame shift in the binding site we have synthesized trisaccharides designed to unravel the precise portion of the native antigen that is recognized by C3.1. The results of these studies based on chemical mapping and STD NMR experiments will be described together with the evaluation of vaccine constructs that evolved from these findings.

Reverse engineering a <i>Candida albicans</i> conjugate vaccine

241st National Meeting (2011)

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Reverse engineering a Candida albicans conjugate vaccine