Glucuronoxylomannan of Cryptococcus neoformans serotype C: structural analysis by gas—liquid chromatography— mass spectrometry and 13C-nuclear magnetic resonance spectroscopy

Cherniak, Robert; Morris, Laura C.; Meyer, Sally A.

doi:10.1016/s0008-6215(00)90505-6

Cited by 30 publications

(24 citation statements)

References 15 publications

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“…GXM from serotypes A and D are mainly substituted with Xylp at O-2, whereas GXM from serotypes B and C are substituted at O-2 and at O-4. Additional analytical data show that the precise molar ratios and typical substitution patterns, as proposed in the original models of GXM structure, are an oversimplification (12)(13)(14)(15)(16)50) except for serotype B (49). In addition, substituent dispositions previously thought to be characteristic of one serotype have been identified in heterologous isolates (16,50,51).…”

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confidence: 89%

Reactivity patterns and epitope specificities of anti-Cryptococcus neoformans monoclonal antibodies by enzyme-linked immunosorbent assay and dot enzyme assay

et al. 1997

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Cryptococcus neoformans glucuronoxylomannans (GXM) are capsular polysaccharides important for virulence in cryptococcosis. This study used dot enzyme assays (DEA) and enzyme-linked immunosorbent assays (ELISA) to determine the reactivity patterns of 21 murine monoclonal antibodies (MAbs) with structurally defined GXMs from five serotypes. The MAbs were categorized into eight groups on the basis of DEA and five groups on the basis of ELISA. MAbs 302, 339, and 439 were studied extensively for their binding to various native and chemically modified GXMs. Quantitative variation in the inhibitory effects of GXMs on the binding of MAbs 302, 339, and 439 were observed by competitive ELISA. O-Deacetylation of serotype A, B, and D GXM resulted in the complete loss of their inhibitory properties. Carboxyl group reduction of GXMs from serotypes A and D resulted in a significant decrease of inhibitory activity for MAb. Xylomannans and methyl glycosides exhibited no detectable inhibitory activity on MAb binding to GXM. The results indicate (i) the existence of five to eight MAb-defined distinct epitopes in C. neoformans GXM that can elicit antibody responses, (ii) MAb detection of antigenic variation within GXMs assigned to a particular serotype, (iii) good correspondence between the patterns of MAb reactivities and polyclonal rabbit factor sera, (iv) good agreement between MAb molecular structure and serotype reactivity, and (v) a dependence of the serotype reactivity profile for a given MAb on the technique used to measure binding.

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confidence: 89%

Reactivity patterns and epitope specificities of anti-Cryptococcus neoformans monoclonal antibodies by enzyme-linked immunosorbent assay and dot enzyme assay

et al. 1997

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“…Furthermore, the secondary and tertiary structure of these polysaccharides is not well known. Glucuronoxylomannan is a very complex polymer of high molecular weight (4 10 6 Da), and its structure has not been established, although it is thought that it contains at least six basic repeats that give origin to the entire polysaccharide (Cherniak et al, 1980(Cherniak et al, , 1992a. The spatial structure of the capsule is not uniform, and electron microscopy studies as well as analysis of dextrans penetration suggest that it is denser in the regions close to the cell wall and looser at the outer edge (Pierini & Doering, 2001;Gates et al, 2004).…”

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confidence: 99%

Equatorial ring-like channels in theCryptococcus neoformanspolysaccharide capsule

Zaragoza

McClelland

Telzak

et al. 2006

FEMS Yeast Research

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Under certain conditions, India ink particles can penetrate the capsule of the opportunistic pathogen Cryptococcus neoformans. India ink penetration gave two distinct patterns, one as a ring in the middle of the capsule, and another as a double spot located at opposite poles of the cells. These spots were perpendicularly orientated to the bud. This pattern suggests the existence of a localized structure deep in the capsule that can accumulate large insoluble particles. Although the mechanisms responsible for the assemblage and maintenance of ring-like channels are not understood, their existence deep within the capsule implies a new level of complexity for this enigmatic structure.

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“…In addition, it was shown that strains within a particular serotype produce structurally different capsular GXM molecules (7,36). Therefore, we hypothesized that besides the presence or absence of a capsule, capsule structure may also influence the ability of SP-D to bind to C. neoformans.…”

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Aggregation ofCryptococcus neoformansby Surfactant Protein D Is Inhibited by Its Capsular Component Glucuronoxylomannan

et al. 2004

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Glucuronoxylomannan of Cryptococcus neoformans serotype C: structural analysis by gas—liquid chromatography— mass spectrometry and 13C-nuclear magnetic resonance spectroscopy

Cited by 30 publications

References 15 publications

Reactivity patterns and epitope specificities of anti-Cryptococcus neoformans monoclonal antibodies by enzyme-linked immunosorbent assay and dot enzyme assay

Reactivity patterns and epitope specificities of anti-Cryptococcus neoformans monoclonal antibodies by enzyme-linked immunosorbent assay and dot enzyme assay

Equatorial ring-like channels in theCryptococcus neoformanspolysaccharide capsule

Aggregation ofCryptococcus neoformansby Surfactant Protein D Is Inhibited by Its Capsular Component Glucuronoxylomannan

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