A lipase isolated from the silkworm Bombyx mori shows antiviral activity against nucleopolyhedrovirus.
A protein showing strong antiviral activity against Bombyx mori nucleopolyhedrovirus (BmNPV) was purified from the digestive juice of B. mori larvae. A homology search of the deduced amino acid sequence of the protein cDNA revealed 56% homology with Drosophila melanogaster lipase and 21% homology with human lipase. As lipase activity of the protein was confirmed in vitro, this protein was designated Bmlipase-1. Northern blot analysis showed that the Bmlipase-1 gene is expressed in the midgut but not in other tissues, nor is it activated by BmNPV infection. In addition, the Bmlipase-1 gene was shown not to be expressed in the molting and wandering stages, indicating that the gene is hormonally regulated. Our results suggest that an insect digestive enzyme has potential as a physiological barrier against BmNPV at the initial site of viral infection.
Ponnuvel
Kangayam M
KM
Innate Immunity Laboratory, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8634, Japan.
Nakazawa
Hiroshi
H
Furukawa
Seiichi
S
Asaoka
Ai
A
Ishibashi
Jun
J
Tanaka
Hiromitsu
H
Yamakawa
Minoru
M
D000595:Amino Acid Sequence; D000818:Animals; D000998:Antiviral Agents / Q000494:pharmacology*; D001483:Base Sequence; D012831:Bombyx / Q000201:enzymology*; D019476:Insect Proteins / Q000494:pharmacology*; D008049:Lipase / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology*; D008969:Molecular Sequence Data; D017924:Nucleopolyhedroviruses / Q000187:drug effects*
D000998:Antiviral Agents; D019476:Insect Proteins; D008049:Lipase