Differential virulence of Candida glabrata glycosylation mutants

J Biol Chem. 2013 Jul 26;288(30):22006-18. doi: 10.1074/jbc.M113.478743. Epub 2013 May 28.

Abstract

The fungus Candida glabrata is an important and increasingly common pathogen of humans, particularly in immunocompromised hosts. Despite this, little is known about the attributes that allow this organism to cause disease or its interaction with the host immune system. However, in common with other fungi, the cell wall of C. glabrata is the initial point of contact between the host and pathogen, and as such, it is likely to play an important role in mediating interactions and hence virulence. Here, we show both through genetic complementation and polysaccharide structural analyses that C. glabrata ANP1, MNN2, and MNN11 encode functional orthologues of the respective Saccharomyces cerevisiae mannosyltransferases. Furthermore, we show that deletion of the C. glabrata Anp1, Mnn2, and Mnn11 mannosyltransferases directly affects the structure of the fungal N-linked mannan, in line with their predicted functions, and this has implications for cell wall integrity and consequently virulence. C. glabrata anp1 and mnn2 mutants showed increased virulence, compared with wild-type (and mnn11) cells. This is in contrast to Candida albicans where inactivation of genes involved in mannan biosynthesis has usually been linked to an attenuation of virulence. In the long term, a better understanding of the attributes that allow C. glabrata to cause disease will provide insights that can be adopted for the development of novel therapeutic and diagnostic approaches.

Keywords: Candida albicans; Cell Wall; Fungi; Host-Pathogen Interactions; Virulence Factors.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Candida glabrata / enzymology
  • Candida glabrata / genetics*
  • Candida glabrata / pathogenicity
  • Candidiasis / microbiology
  • Carbohydrate Sequence
  • Cell Line
  • Cell Wall / genetics
  • Cell Wall / metabolism
  • Endothelial Cells / cytology
  • Endothelial Cells / microbiology
  • Fungal Proteins / genetics*
  • Fungal Proteins / metabolism
  • Genetic Complementation Test
  • Glycosylation
  • Humans
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Kaplan-Meier Estimate
  • Magnetic Resonance Spectroscopy
  • Male
  • Mannans / chemistry
  • Mannans / metabolism
  • Mannosyltransferases / genetics*
  • Mannosyltransferases / metabolism
  • Mice
  • Molecular Sequence Data
  • Mutation*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Virulence / genetics

Substances

  • Fungal Proteins
  • Isoenzymes
  • Mannans
  • Saccharomyces cerevisiae Proteins
  • Anp1 protein, Candida glabata
  • Mannosyltransferases
  • Mnn11 protein, Candida glabata
  • Mnn2 protein, Candida glabata