Growth and mating of Cryptococcus neoformans var. grubii on woody debris

Microb Ecol. 2009 May;57(4):757-65. doi: 10.1007/s00248-008-9452-1. Epub 2008 Oct 11.

Abstract

A total of 36 Cryptococcus neoformans strains originating from South Africa were screened for wood degrading enzymes. All strains tested positive for cellulase activity while none where capable of xylan degradation. Three C. neoformans var. grubii strains, originating from clinical and environmental samples, representing the same genotype (VNI/AFLP1-C. neoformans var. grubii) and MATalpha, were evaluated for growth on debris of two common tree species in South Africa: Acacia mearnsii and Eucalyptus camaldulensis. The mating capability of all the C. neoformans strains was evaluated on similar debris. Strains grown on A. mearnsii yielded substantially greater yeast populations. A total of 26%, 6%, 46%, and 80% of the 36 C. neoformans strains tested were either able to mate or develop filaments when crossed on A. mearnsii and E. camaldulensis debris, V8 juice, and yeast carbon base (YCB) agar, respectively. Filamentation and monokaryotic fruiting was observed in 3% of strains when C. neoformans was cultured on either A. mearnsii, E. camaldulensis debris, or YCB. The results indicate that this fungus is capable of completing its life cycle and can produce basidiospores on woody debris. In the future, these findings should be considered when studying the epidemiology, microbial ecology, and proposed infection process of this global pathogen.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acacia / microbiology
  • Cellulases / metabolism
  • Cryptococcus neoformans / enzymology
  • Cryptococcus neoformans / genetics
  • Cryptococcus neoformans / growth & development*
  • Culture Media
  • Endo-1,4-beta Xylanases / metabolism
  • Eucalyptus / microbiology
  • Genes, Mating Type, Fungal
  • Genotype
  • South Africa
  • Wood / chemistry
  • Wood / microbiology*
  • Xylans / metabolism

Substances

  • Culture Media
  • Xylans
  • Cellulases
  • Endo-1,4-beta Xylanases