Genetic and biochemical characterization of PrtA, an RTX-like metalloprotease from Photorhabdus

D J Bowen, T A Rocheleau, C K Grutzmacher, L Meslet, M Valens, D Marble, A Dowling, R Ffrench-Constant, M A Blight

Research output: Contribution to journalArticlepeer-review

53 Citations (SciVal)

Abstract

Proteases play a key role in the interaction between pathogens and their hosts. The bacterial entomopathogen Photorhabdus lives in symbiosis with nematodes that invade insects. Following entry into the insect, the bacteria are released from the nematode gut into the open blood system of the insect. Here they secrete factors which kill the host and also convert the host tissues into food for the replicating bacteria and nematodes. One of the secreted proteins is PrtA, which is shown here to be a repeats-in-toxin (RTX) alkaline zinc metalloprotease. PrtA has high affinity for artificial substrates such as casein and gelatin and can be inhibited by zinc metalloprotease inhibitors. The metalloprotease also shows a calcium- and temperature-dependent autolysis. The prtA gene carries the characteristic RTX repeated motifs and predicts high similarity to proteases from Erwinia chrysanthemi, Pseudomonas aeruginosa and Serratia marcescens. The prtA gene resides in a locus encoding both the protease ABC transporter (prtBCD) and an intervening ORF encoding a protease inhibitor (inh). PrtA activity is detectable 24 h after artificial bacterial infection of an insect, suggesting that the protease may play a key role in degrading insect tissues rather than in overcoming the insect immune system. Purified PrtA also shows cytotoxicity to mammalian cell cultures, supporting its proposed role in bioconversion of the insect cadaver into food for bacterial and nematode development.
Original languageEnglish
Pages (from-to)1581-1591
Number of pages11
JournalMicrobiology
Volume149
DOIs
Publication statusPublished - 2003

Bibliographical note

ID number: ISI:000183621600021

Keywords

  • aeruginosa alkaline protease
  • terminal secretion signal
  • bacteroides-fragilis
  • extracellular protease
  • pseudomonas-aeruginosa
  • xenorhabdus-luminescens
  • escherichia-coli
  • gram-negative bacteria
  • coli alpha-hemolysin
  • erwinia-chrysanthemi

Fingerprint

Dive into the research topics of 'Genetic and biochemical characterization of PrtA, an RTX-like metalloprotease from Photorhabdus'. Together they form a unique fingerprint.

Cite this