Identification and partial characterisation of metalloproteases secreted by a Mesanophrys-like ciliate parasite of the Norway lobster Nephrops norvegicus.
A ciliate parasite, tentatively identified as Mesanophrys sp. of Norway lobsters Nephrops norvegicus, is demonstrated to secrete several proteases into the culture medium (modified Nephrops saline). Analyses using substrate-impregnated sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed 12 activity bands differing greatly in mobility in the gels. The complete inhibition of proteolytic activity by 1,10-phenanthroline indicated that the proteases are of the metallo class. The proteases were active at the physiological temperature (8 degrees C) and haemolymph pH (7.8) of the host. The proteases were selective in the degradation of several host proteins, including the myosin heavy chain, which is a major structural component of lobster muscle. Consequently, these proteases may have important roles in several aspects of the host-parasite interaction including invasion, nutrient uptake by the ciliate, and pathogenesis.
Small
H J
HJ
Division of Environmental and Evolutionary Biology, Institute of Biomedical & Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK. hamish@vims.edu
Neil
D M
DM
Taylor
A C
AC
Coombs
G H
GH
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D045726:Metalloproteases / Q000302:isolation & purification* / Q000378:metabolism*; D018995:Myosin Heavy Chains / Q000378:metabolism; D008121:Nephropidae / Q000469:parasitology*; D016802:Oligohymenophorea / Q000201:enzymology*; D012606:Scotland; D013053:Spectrophotometry; D013696:Temperature
D045726:Metalloproteases; D018995:Myosin Heavy Chains