Document Type
Article
Department/Program
Virginia Institute of Marine Science
Publication Date
10-2005
Journal
Diseases of Aquatic Organisms
Volume
67
Issue
3
First Page
225
Last Page
231
Abstract
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.
DOI
10.3354/dao067225
Recommended Citation
Small, Hamish J.; Neil, DM; and al, et, Identification and partial characterisation of metalloproteases secreted by a Mesanophrys-like ciliate parasite of the Norway lobster Nephrops norvegicus (2005). Diseases of Aquatic Organisms, 67(3), 225-231.
10.3354/dao067225
