Purification and characterization of a new serine protease (EF-SP2) with anti-plant viral activity from Eisenia foetida: Analysis of anti-plant viral activity of EF-SP2

Previously, we have reported that purification and characterization of an anti-plant viral serine protease (EF-SP1) from Eisenia foetida. In this study, a new serine protease (EF-SP2) showing strong antiviral activities against cucumber mosaic virus (CMV) and tobacco mosaic virus (TMV) was purified...

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Bibliographic Details
Published in:Process biochemistry (1991) 2011-09, Vol.46 (9), p.1711-1716
Main Authors: Ueda, Mitsuhiro, Yamashita, Takayuki, Nakazawa, Masami, Miyatake, Kazutaka, Ohki, Satoshi, Sakaguchi, Minoru, Inouye, Kuniyo
Format: Article
Language:English
Subjects:
amino acid sequences
Amino acids
Anti-plant viral protein
antiviral properties
Cucumber mosaic virus
Cytomegalovirus
Earthworm
earthworms
Eisenia fetida
Eisenia foetida
Enzymes
Inhibitors
Molecular weight
Mosaics
plant viruses
polyacrylamide gel electrophoresis
Protease
proteinase inhibitors
Purification
Serine protease
serine proteinases
substrate specificity
temperature
Tobacco mosaic virus
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Summary:Previously, we have reported that purification and characterization of an anti-plant viral serine protease (EF-SP1) from Eisenia foetida. In this study, a new serine protease (EF-SP2) showing strong antiviral activities against cucumber mosaic virus (CMV) and tobacco mosaic virus (TMV) was purified from the coelomic fluid of the earthworm E. foetida. The activity of EF-SP2 was suppressed by various known serine protease inhibitors, suggesting that the EF-SP2 is a serine protease. Its molecular weight was estimated to be 26,000 by SDS–PAGE, and its optimal pH and temperature were pH 9.5 and 60°C, respectively. N-terminal amino acid sequence of EF-SP2 was the same as those of E. foetida serine proteases (EFE-d and EFE-e) with fibrinolytic activity, but different from that of EF-SP1. The enzymatic properties of anti-plant serine proteases (EF-SP1 and EF-SP2) and fibrinolytic enzymes (EFE-d and EFE-e) were similar to each other, e.g., substrate specificity, molecular weight, and effect of inhibitors. Our results suggest that EF-SP2 as well as EF-SP1 can be also applicable as a potential antiviral factor against CMV, TMV, and other plant viruses.
ISSN:1359-5113
1873-3298
DOI:10.1016/j.procbio.2011.05.009