Literature DB >> 7507898

Structures of cell wall mannans of pathogenic Candida tropicalis IFO 0199 and IFO 1647 yeast strains.

H Kobayashi1, K Matsuda, T Ikeda, M Suzuki, S Takahashi, A Suzuki, N Shibata, S Suzuki.   

Abstract

We conducted a structural analysis of the cell wall mannans isolated from two Candida tropicalis strains, IFO 0199 and IFO 1647, exhibiting strong agglutinabilities against anti-Candida factor sera 5 and 6. The products released from these mannans by acid treatment were identified as the oligosaccharides, from biose to pentaose, consisting solely of beta-1,2-linked mannopyranose units corresponding to common epitopes of Candida albicans serotypes A and B (factor 5). Mild acetolysis of acid- and alkali-treated mannans produced large amounts of hexaose and heptaose, Man rho beta 1-2Man rho beta 1-2Man rho alpha 1-2Man rho alpha 1-2Man rho alpha 1-2Man and Man rho beta 1-2Man rho beta 1-2Man rho beta 1-2Man rho alpha 1-2 Man rho alpha 1-2Man, corresponding to the C. albicans serotype A-specific epitopes (factor 6). However, the homologous pentaose, Man rho beta 1-2Man rho alpha 1-2 Man, was not generated by this procedure. The oligosaccharides (biose to hexaose) obtained from the mannans by conventional acetolysis were composed exclusively of alpha-1,2-linked mannopyranose units. Therefore, the mannans of C. tropicalis IFO 0199 and IFO 1647 do not have the alpha-1,3-linked mannopyranose units previously observed in the mannans of C. albicans and Candida stellatoidea. The results of this study and previous findings indicate that the similarity of the antigenicities of three Candida species, C. albicans serotype A, C. stellatoidea type II, and C. tropicalis, reside in the beta-1,2 and alpha-1,2 linkages containing oligomannosyl side chain (factor 6) in the cell wall mannan.

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Year:  1994        PMID: 7507898      PMCID: PMC186148          DOI: 10.1128/iai.62.2.615-622.1994

Source DB:  PubMed          Journal:  Infect Immun        ISSN: 0019-9567            Impact factor:   3.441


  42 in total

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