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Heat shock affects host-pathogen interaction in Galleria mellonella infected with Bacillus thuringiensis.

Abstract
We report that Galleria mellonella larvae exposed to heat shock was more resistant to infection with entomopathogenic bacteria Bacillus thuringiensis. The insects were exposed to a temperature of 40°C for 30 min directly before injection of vegetative bacterial cells. It appeared that the kinetics of the immune response was affected in heat-shocked animals. The infection-induced antimicrobial activity of larval hemolymph was stronger in shocked animals in comparison to the non-shocked ones. Hemolymph proteins of molecular weight below 10 kDa, corresponding to the size of antimicrobial peptides, were responsible for this activity. Furthermore, the transcription level of genes encoding antimicrobial peptides: cecropin, gallerimycin, and galiomycin was increased in the fat bodies of insects exposed to heat shock before infection. On the contrary, the heat-shock treatment did not enhance expression of the metalloproteinase inhibitor-IMPI in the infected animals. The difference in the amount of antimicrobial peptides and, consequently, in the defense activity of insect hemolymph, persisted after the action of bacterial metalloproteinases, which are well-known virulence factors. Furthermore, peptides with antimicrobial activity in the hemolymph of infected larvae pre-exposed to heat shock appeared to be more resistant to proteolytic degradation both in vitro and in vivo. Our results point to the mechanism of cross-protection of thermal stress toward innate immune response.
AuthorsIwona Wojda, Paulina Taszłow
JournalJournal of insect physiology (J Insect Physiol) Vol. 59 Issue 9 Pg. 894-905 (Sep 2013) ISSN: 1879-1611 [Electronic] England
PMID23834825 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
CopyrightCopyright © 2013 Elsevier Ltd. All rights reserved.
Chemical References
  • Antimicrobial Cationic Peptides
  • Bacterial Proteins
  • Peptide Hydrolases
  • Thermolysin
Topics
  • Animals
  • Antimicrobial Cationic Peptides (metabolism)
  • Bacillus thuringiensis (physiology)
  • Bacterial Proteins (metabolism)
  • Hemolymph (metabolism)
  • Host-Pathogen Interactions
  • Hot Temperature
  • Larva (immunology, microbiology)
  • Moths (immunology, microbiology)
  • Peptide Hydrolases (metabolism)
  • Proteolysis
  • Stress, Physiological
  • Thermolysin (metabolism)

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