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Mannosyl transfer in Cryptococcus neoformans

C W White1, E S Jacobson

  • 1Department of Biochemistry, Medical College of Virginia-Virginia Commonwealth University, Richmond 23298.

Canadian Journal of Microbiology
|January 1, 1993
PubMed
Summary
This summary is machine-generated.

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Researchers identified a mannosyltransferase enzyme in Cryptococcus neoformans that synthesizes alpha(1-->2) mannan linkages. This enzyme is crucial for creating high-mannose oligosaccharides in glycoproteins, not for capsule synthesis.

Area of Science:

  • Biochemistry
  • Microbiology
  • Glycobiology

Background:

  • Cryptococcus neoformans is an opportunistic fungal pathogen.
  • Oligosaccharide synthesis is vital for fungal cell structure and virulence.
  • Understanding mannosyltransferase activity is key to elucidating glycosylation pathways.

Purpose of the Study:

  • To characterize a mannosyltransferase from Cryptococcus neoformans.
  • To determine the role of this enzyme in oligosaccharide synthesis.
  • To investigate its potential involvement in capsular polysaccharide production.

Main Methods:

  • Enzyme assays using GDP-mannose and a synthetic mannosyl acceptor.
  • Analysis of product linkages using alpha-mannosidase and Nuclear Magnetic Resonance (NMR).

Related Experiment Videos

  • Testing acapsular mutants for enzyme deficiency.

    • Main Results:

    • The enzyme transfers mannose from GDP-mannose, forming alpha(1-->2) linkages.
    • Optimal activity observed at 37°C and pH 7.0, requiring Mn2+.
    • Enzyme activity was not deficient in acapsular mutants, suggesting a non-capsular role.
    • Dolichyl phosphate intermediates were not implicated in this mannose transfer.

    Conclusions:

    • The identified mannosyltransferase extends alpha(1-->2) mannan chains.
    • This enzyme is likely involved in synthesizing high-mannose oligosaccharides of glycoproteins.
    • It does not appear to be involved in the synthesis of the fungal capsule backbone.