6533b7d0fe1ef96bd125bab9

RESEARCH PRODUCT

The C-terminal antibody binding domain ofCandida albicansmp58 represents a protective epitope during candidiasis

Sofia PereaA ViudesJose L. Lopez-ribotJavier PemánJosé P. MartínezThomas F. PattersonAnna L. LazzellWilliam R. Kirkpatrick

subject

medicine.drug_classEnzyme-Linked Immunosorbent AssayMonoclonal antibodyMicrobiologyEpitopeImmunoglobulin GFungal ProteinsEpitopesMiceCandida albicansGeneticsmedicineAnimalsAmino Acid SequenceCandida albicansMolecular BiologyMice Inbred BALB CMembrane GlycoproteinsbiologyCandidiasisAntibodies Monoclonalbiology.organism_classificationDisseminated CandidiasisVirologyCorpus albicansProtein Structure TertiaryEpitope mappingbiology.proteinFemaleAntibodyEpitope Mapping

description

The 58-kDa surface mannoprotein of Candida albicans (mp58) elicits strong antibody responses during infection. Epitope mapping with sera from patients with candidiasis and control individuals indicated the presence of multiple IgG-reactive continuous epitopes on the protein, expanding both the amino- and carboxy-terminal domains and several internal regions. These immunoreactive regions were similar to the ones previously identified using sera from immunized animals. Two of the epitopic regions (including the C-terminal domain) showed increased reactivity with antibodies present in sera from patients with candidiasis as compared to control individuals. Patients who survived the infection displayed increased antibody reactivity towards the C-terminal epitope as compared to those succumbing to candidiasis. A monoclonal antibody directed towards this epitopic region conferred protection in serum therapy experiments in a murine model of hematogenously disseminated candidiasis. Together, these observations indicate the carboxy-terminal antibody binding domain of C. albicans mp58 represents a protective epitope during candidiasis.

https://doi.org/10.1016/s0378-1097(04)00042-4