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Antibody response to the 45 kDa Candida albicans antigen in an animal model and potential role of the antigen in adherence

Helena Bujdáková¹, Ema Pauloviová², Silvia Borecká-Melkusová¹, Juraj Gaperík³, Soa Kucharíková¹, Anna Kolecka¹, Claudia Lell⁴, Dorthe B. Jensen⁴, Reinhard Würzner⁴, Duan Chorvát, Jr⁵ and Iva Pichová⁶

¹ Department of Microbiology and Virology, Faculty of Natural Sciences, Comenius University, Bratislava, Slovakia

² Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovakia

³ Institute of Molecular Biology, Slovak Academy of Sciences, Bratislava, Slovakia

⁴ Department of Hygiene, Microbiology and Social Medicine, Innsbruck Medical University, Austria

⁵ Department of Biophotonics, International Laser Centre, Bratislava, Slovakia

⁶ Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic

Correspondence
Helena Bujdáková
bujdakova{at}fns.uniba.sk

Received March 4, 2008
Accepted August 14, 2008

The Candida antigen CR3-RP (complement receptor 3-related protein) is supposed to be a ‘mimicry’ protein because of its ability to bind antibody directed against the subunit of the mammalian CR3 (CD11b/CD18). This study aimed to (i) investigate the specific humoral isotypic response to immunization with CR3-RP in vivo in a rabbit animal model, and (ii) determine the role of CR3-RP in the adherence of Candida albicans in vitro using the model systems of buccal epithelial cells (BECs) and biofilm formation. The synthetic C. albicans peptide DINGGGATLPQ corresponding to 11 amino-acids of the CR3-RP sequence DINGGGATLPQALXQITGVIT, determined by N-terminal sequencing, was used for immunization of rabbits to obtain polyclonal anti-CR3-PR serum and for subsequent characterization of the humoral isotypic response of rabbits. A significant increase of IgG, IgA and IgM anti-CR3-RP specific antibodies was observed after the third (P<0.01) and the fourth (P<0.001) immunization doses. The elevation of IgA levels suggested peptide immunomodulation of the IgA1 subclass, presumably in coincidence with Candida epithelial adherence. Blocking CR3-RP with polyclonal anti-CR3-RP serum reduced the ability of Candida to adhere to BECs, in comparison with the control, by up to 35 % (P<0.001), and reduced biofilm formation by 28 % (P<0.001), including changes in biofilm thickness and integrity detected by confocal laser scanning microscopy. These properties of CR3-RP suggest that it has potential for future vaccine development.

Abbreviations: BEC, buccal epithelial cell; CLSM, confocal laser scanning microscopy; RT, room temperature; XTT, 2,3-bis(2-methoxy-4-nitro-5-sulfophenyl)-2H-tetrazolium-5-carboxanilide.

The GenBank/EMBL/DDBJ accession number for the N-terminal sequence fragment of CR3-RP is P85437.