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Unité 42, Institut National de la Santé et de la Recherche Médicale, Domaine du CERTIA, 369 Rue Jules Guesde, BP 39, 59651 Villeneuve d'Ascq Cedex, France
2Author for correspondence: D. Poulain. Tel: +33 20 472629. Fax: +33 20 059172.
ABSTRACT
A monoclonal antibody specific for ß-1,2-linked oligomannosides was used to study the association of these residues with Candida albicans mannan and phospholipomannan (PLM) in relation to growth conditions and in mannan mutant strains. Double immunofluorescence assays performed on cells grown under standard conditions indicated a highly heterogeneous cell surface expression of these epitopes in comparison with the homogeneous expression of 
-linked oligomannosidic epitopes. Growth in the presence of tunicamycin, which inhibits mannan N-glycosylation, resulted in an absence of ß-1,2-oligomannosidic epitopes on the cell surface, although PLM synthesis still occurred as shown by autoradiography. Similarly, growth in acidic conditions, which inhibits the incorporation of ß-1,2-oligomannosides in mannan, resulted in an absence of ß-1,2-oligomannosidic epitopes at the cell surface, although they still associated with PLM as shown by Western blotting. Western blots of C. albicans mutant strains with reduced amounts or an absence of phosphorus and acid-labile ß-1,2-oligomannosides in their mannan confirmed that the association of ß-1,2-linked oligomannosides with mannan and with PLM involves different mannosylation processes.
Present address: Facolta di Medecina e Chrurgia, Istituto di Microbiologia, Via Gramsci 14, 43100 Parma, Italy.
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