Digestive function of lysozyme in synanthropic acaridid mites enables utilization of bacteria as a food source.
The activity of lysozyme, the enzyme that hydrolyzes peptidoglycan in G(+) bacterial cell walls, was detected in whole mite extracts (WME) and in spent growth medium extracts (SGME) of 14 species of synanthropic mites (Acari: Acaridida). The adaptation of lysozyme for digestive activity and bacteriophagy was based on: (i) high lysozyme activity in SGME, and (ii) the correlation of maximum lysozyme activity at acidic pH values, corresponding to pH in the ventriculus and caeca. We show that the digestion of fluorescein-labeled Micrococcus lysodeikticus cells began in ventriculus and continued during the passage of a food bolus through the gut. The fluorescein was absorbed by midgut cells and penetrated to parenchymal tissues. Eight species showed a higher rate of population growth on a M. lysodeikticus diet than on a control diet. The lysozyme activity in SGME was positively correlated to the standardized rate (r (s)) of population growth, although no correlation was found between r (s) and lysozyme activity in WME. The lysozyme activity in WME was negatively correlated to that in SGME. The highest activity of digestive lysozyme was found in Lepidoglyphus destructor, Chortoglyphus arcuatus and Dermatophagoides farinae. All of these findings indicate that lysozyme in acaridid mites possesses both defensive and digestive functions. The enzymatic properties of mite lysozyme are similar to those of the lysozymes present in the ruminant stomach and in the insect midgut.
Erban
Tomas
T
Department of Zoology, Faculty of Science, Charles University, Vinicna 7, Praha, Czech Republic.
Hubert
Jan
J
D000821:Animal Feed; D000818:Animals; D004063:Digestion / Q000502:physiology*; D004064:Digestive System / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008837:Micrococcus; D008925:Mites / Q000201:enzymology* / Q000254:growth & development*; D009113:Muramidase / Q000378:metabolism*
D009113:Muramidase