Immunogenicity and protective effect of recombinant enolase of Candida albicans in a murine model of systemic candidiasis

Enolase, a 46-kDa glycolytic enzyme, is an immunodominant antigen of the opportunistic pathogen Candida albicans. A recombinant 6×His-tagged enolase was studied, in conjunction with interleukin-12 (IL-12), as an adjuvant for cytokine induction favouring protection in a murine model of haematogenous...

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Bibliographic Details
Published in:Medical mycology (Oxford) Vol. 42; no. 4; pp. 319 - 324
Main Authors: Montagnoli, Claudia, Sandini, Silvia, Bacci, Angela, Romani, Luigina, Valle, Roberto La
Format: Journal Article
Language:English
Published: UK Informa UK Ltd 01-08-2004
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Summary:Enolase, a 46-kDa glycolytic enzyme, is an immunodominant antigen of the opportunistic pathogen Candida albicans. A recombinant 6×His-tagged enolase was studied, in conjunction with interleukin-12 (IL-12), as an adjuvant for cytokine induction favouring protection in a murine model of haematogenous candidiasis. Mice immunized with enolase plus IL-12 showed increased antibody titres against enolase, as well as increased median survival time and decreased fungal burden in kidneys, in comparison to non-immunized or IL-12-treated mice. This increased survival was attributable to enolase-induced cell-mediated immunity as it also occurred in B-cell-deficient mice. Enolase immunization stimulated a predominant T-helper-1 (Th1) cytokine pattern in splenic cells and induced production of interferon-γ (IFN-γ) and interleukin-2 (IL-2) by purified CD4+ T cells. However, despite the elevation of immunogenicity, recombinant enolase induced only a modest protection against disseminated candidiasis, suggesting a form of protection likely attributable to the induction of a Th1 cell-mediated immune response.
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ISSN:1369-3786
1460-2709
DOI:10.1080/13693780310001644653