@article {649,
	title = {A virus essential for insect host-parasite interactions encodes cystatins},
	volume = {79},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalInstitut de Recherche sur la Biologie de l{\textquoteright}Insecte, UMR CNRS 6035, Faculte des Sciences et Techniques, Parc de Grandmont, Tours.eng SI  - GENBANK/AJ632321http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=16014938},
	pages = {9765 - 9776},
	abstract = {Cotesia congregata is a parasitoid wasp that injects its eggs in the host caterpillar Manduca sexta. In this host-parasite interaction, successful parasitism is ensured by a third partner: a bracovirus. The relationship between parasitic wasps and bracoviruses constitutes one of the few known mutualisms between viruses and eukaryotes. The C. congregata bracovirus (CcBV) is injected at the same time as the wasp eggs in the host hemolymph. Expression of viral genes alters the caterpillar{\textquoteright}s immune defense responses and developmental program, resulting in the creation of a favorable environment for the survival and emergence of adult parasitoid wasps. Here, we describe the characterization of a CcBV multigene family which is highly expressed during parasitism and which encodes three proteins with homology to members of the cystatin superfamily. Cystatins are tightly binding, reversible inhibitors of cysteine proteases. Other cysteine protease inhibitors have been described for lepidopteran viruses; however, this is the first description of the presence of cystatins in a viral genome. The expression and purification of a recombinant form of one of the CcBV cystatins, cystatin 1, revealed that this viral cystatin is functional having potent inhibitory activity towards the cysteine proteases papain, human cathepsins L and B and Sarcophaga cathepsin B in assays in vitro. CcBV cystatins are, therefore, likely to play a role in host caterpillar physiological deregulation by inhibiting host target proteases in the course of the host-parasite interaction.},
	keywords = {Amino Acid Sequence, Animals, Base Sequence, Cathepsins/antagonists \&amp, Cystatins/genetics/isolation \&amp, Diptera/enzymology, Genes, Viral, Host-Parasite Interactions, Humans, inhibitors, Manduca/*parasitology, Molecular Sequence Data, Multigene Family/physiology, OID - NLM: PMC1181612, Ovum/virology, Papain/antagonists \&amp, PMC - PMC1181612, Polydnaviridae/*metabolism, purification/*metabolism/pharmacology, Sequence Alignment, Wasps/*metabolism/*physiology/virology},
	author = {Espagne, E. and Douris, V. and Lalmanach, G. and Provost, B. and Cattolico, L. and Lesobre, J. and Kurata, S. and Iatrou, K. and Drezen, J. M. and Huguet, E.}
}
@article {468,
	title = {Purification of a cysteine protease inhibitor from larval hemolymph of the tobacco hornworm (Manduca sexta) and functional expression of the recombinant protein},
	volume = {37},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalLaboratory of Food Molecular Functionality, College of Agriculture, Ibaraki University, 3-21-1 Chuo, Ami-machi, Inashiki-gun, Ibaraki 300-0393, Japan.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=17681235},
	pages = {960 - 968},
	abstract = {A cysteine protease inhibitor (CPI) with an apparent molecular mass of 11.5kDa was purified from larval hemolymph of the tobacco hornworm (Manduca sexta) by gel filtration on Sephadex G-50 followed by hydrophobic and ion-exchange column chromatographies. The purified cysteine proteinase inhibitor, denoted as MsCPI, strongly inhibited the plant cysteine protease, papain, with a K(i) value of 5.5 x 10(-9)M. Nucleotide sequence analysis of a partial cDNA encoding MsCPI indicated that MsCPI consists of 105 amino acid residues in a sequence that is similar to sarcocystatin A from Sarcophaga peregrina. However, northern blotting and PCR analyses using the specific primers of MsCPI suggested that the mRNA encoding MsCPI had a size of more than 12 kilobases, which included at least six tandemly repeated MsCPI segments. MsCPI was expressed in Escherichia coli and the recombinant protein effectively inhibited cysteine proteases from plants as well as from animals such as cathepsins B (K(i), 6.8 nM), H (3.0 nM), and L (0.87 nM). There was no inhibition exhibited toward trypsin, chymotrypsin, subtilisin, pepsin or themolysin.},
	keywords = {Amino Acid Sequence, Animals, Cathepsins/drug effects/isolation \&amp, Cloning, Molecular, Conserved Sequence, Cysteine Proteinase Inhibitors/genetics/*isolation \&amp, development, DNA Primers, Escherichia coli/genetics, Hemolymph/*chemistry, Humans, inhibitors, Larva, Manduca/*growth \&amp, Molecular Sequence Data, Papain/antagonists \&amp, Polymerase Chain Reaction, purification/metabolism, purification/pharmacology, Recombinant Proteins/isolation \&amp, Sequence Alignment, Sequence Homology, Amino Acid},
	author = {Miyaji, T. and Kouzuma, Y. and Yaguchi, J. and Matsumoto, R. and Kanost, M. R. and Kramer, K. J. and Yonekura, M.}
}
