Substrate-specific gene expression in Batrachochytrium dendrobatidis, the chytrid pathogen of amphibians

PLoS One. 2012;7(11):e49924. doi: 10.1371/journal.pone.0049924. Epub 2012 Nov 20.

Abstract

Determining the mechanisms of host-pathogen interaction is critical for understanding and mitigating infectious disease. Mechanisms of fungal pathogenicity are of particular interest given the recent outbreaks of fungal diseases in wildlife populations. Our study focuses on Batrachochytrium dendrobatidis (Bd), the chytrid pathogen responsible for amphibian declines around the world. Previous studies have hypothesized a role for several specific families of secreted proteases as pathogenicity factors in Bd, but the expression of these genes has only been evaluated in laboratory growth conditions. Here we conduct a genome-wide study of Bd gene expression under two different nutrient conditions. We compare Bd gene expression profiles in standard laboratory growth media and in pulverized host tissue (i.e., frog skin). A large proportion of genes in the Bd genome show increased expression when grown in host tissue, indicating the importance of studying pathogens on host substrate. A number of gene classes show particularly high levels of expression in host tissue, including three families of secreted proteases (metallo-, serine- and aspartyl-proteases), adhesion genes, lipase-3 encoding genes, and a group of phylogenetically unusual crinkler-like effectors. We discuss the roles of these different genes as putative pathogenicity factors and discuss what they can teach us about Bd's metabolic targets, host invasion, and pathogenesis.

Publication types

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

MeSH terms

  • Amphibians* / genetics
  • Amphibians* / microbiology
  • Animals
  • Chytridiomycota* / genetics
  • Chytridiomycota* / pathogenicity
  • Gene Expression Profiling
  • Genome
  • Host-Pathogen Interactions / genetics*
  • Peptide Hydrolases* / genetics
  • Peptide Hydrolases* / metabolism
  • Skin / metabolism
  • Skin / microbiology
  • Substrate Specificity

Substances

  • Peptide Hydrolases