A novel anti-plant viral protein from coelomic fluid of the earthworm Eisenia foetida: purification, characterization and its identification as a serine protease.
A novel protein showing strong antiviral activities against cucumber mosaic virus (CMV) and tomato mosaic virus (TMV) was purified from the coelomic fluid of the earthworm Eisenia foetida. The protein was characterized as a cold-adapted serine protease. Its molecular weight was estimated to be 27,000 by SDS-PAGE. The enzyme was most active at pH 9.5 and 40-50 degrees C. The protease activity at 4 degrees C was 60% of that obtained at the optimal temperature. The activity was suppressed by various serine protease inhibitors. Partial N-terminal amino acid sequence of the enzyme showed homology with serine proteases of earthworms, E. foetida and Lumbricus rubellus previously studied. Our results suggest that the enzyme can be applicable as a potential antiviral factor against CMV, TMV, and other plant viruses.
Ueda
Mitsuhiro
M
Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Osaka, 599-8531, Japan. mueda@biochem.osakafu-u.ac.jp
Noda
Kanako
K
Nakazawa
Masami
M
Miyatake
Kazutaka
K
Ohki
Satoshi
S
Sakaguchi
Minoru
M
Inouye
Kuniyo
K
D000818:Animals; D000998:Antiviral Agents / Q000302:isolation & purification; D001826:Body Fluids / Q000201:enzymology; D017799:Cucumovirus; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009835:Oligochaeta / Q000201:enzymology* / Q000276:immunology; D010942:Plant Viruses / Q000276:immunology*; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D013696:Temperature
D000998:Antiviral Agents; D012697:Serine Endopeptidases