Subterranean termite prophylactic secretions and external antifungal defenses

J Insect Physiol. 2011 Sep;57(9):1259-66. doi: 10.1016/j.jinsphys.2011.05.016. Epub 2011 Jun 15.

Abstract

Termites exploit environments that make them susceptible to infection and rapid disease transmission. Gram-negative bacteria binding proteins (GNBPs) signal the presence of microbes and in some insects directly damage fungal pathogens with β-1,3-glucanase activity. The subterranean termites Reticulitermes flavipes and Reticulitermes virginicus encounter soil entomopathogenic fungi such as Metarhizium anisopliae, which can evade host immune responses after penetrating the cuticle. An external defense that prevents invasion of fungal pathogens could be crucial in termites, allowing them to thrive under high pathogenic pressures. We investigated the role of secreted β-1,3-glucanases in Reticulitermes defenses against M. anisopliae. Our results show that these termites secrete antifungal β-1,3-glucanases on the cuticle, and the specific inhibition of GNBP associated β-1,3-glucanase activity with d-δ-gluconolactone (GDL) reduces this activity and can cause significant increases in mortality after exposure to M. anisopliae. Secreted β-1,3-glucanases appear to be essential in preventing infection by breaking down fungi externally.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antifungal Agents / analysis
  • Antifungal Agents / antagonists & inhibitors
  • Antimicrobial Cationic Peptides
  • Glucan 1,3-beta-Glucosidase / antagonists & inhibitors
  • Glucan 1,3-beta-Glucosidase / metabolism
  • Host-Pathogen Interactions*
  • Insect Proteins / metabolism*
  • Isoptera / chemistry
  • Isoptera / physiology*
  • Metarhizium / physiology*
  • Molecular Sequence Data
  • Peptides / metabolism*
  • Sequence Alignment

Substances

  • Antifungal Agents
  • Antimicrobial Cationic Peptides
  • Insect Proteins
  • Peptides
  • termicin
  • Glucan 1,3-beta-Glucosidase