cDNA cloning of a salivary chymotrypsin-like protease and the identification of six additional cDNAs encoding putative digestive proteases from the green mirid, Creontiades dilutus (Hemiptera: Miridae)

Colebatch, Gillian; Cooper, Paul D.; East, Peter D.

doi:10.1016/s0965-1748(02)00044-9

Cited by 27 publications

(19 citation statements)

References 39 publications

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“…The deduced amino acid sequence of Es-CLSP showed several structural features that are typical of SPs (Figures 1 and 2). Although the substrate-binding pocket residues of SPs are variable, in CLSP, they usually consist of Ser, Gly, and Ala/Gly (Colebatch et al, 2002). One of the substrate-binding pocket residues of Es-CLSP was replaced by a Gly residue (at position 216); this substitution is also found in the trypsin and CLSP in the gut of Mayetiola destructor (Zhu et al, 2005), a small amino acid found in vertebrate CLSP.…”

Section: Discussionmentioning

confidence: 99%

“…Similarity analysis revealed that Es-CLSP has several typical structural features of SPs (Kraut, 1977;Perona and Craik, 1995), such as the catalytic triad (H, D, and S), conserved serine catalytic site, and 6 cysteine residues. In the conserved trypsin-like SP domain, there are 6 cysteine residues common to all invertebrate CLSPs, and these are believed to form 3 disulfide bonds (Colebatch et al, 2002). In addition to the 3 pairs of conserved cysteine residues, there is another free cysteine residue in the signal peptide.…”

Section: Discussionmentioning

confidence: 99%

“…In Drosophila, a CLSP is involved in immune defense reactions against bacteria (de Morais et al, 2005;Moffitt et al, 2012). Recently, more and more CLSPs have been discovered in invertebrates Colebatch et al, 2002;Zhu et al, 2005;Broehan et al, 2007;Shi et al, 2008;Danwattananusorn et al, 2009;Yadav et al, 2011). CLSPs have been cloned in the shrimp and their polymorphism patterns and immune response to bacteria have been analyzed Van Wormhoudt et al, 1992;Shi et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

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Molecular characteristic and expression analysis of collagenolytic serine protease from the Chinese mitten crab Eriocheir sinensis with defense response to Vibrio anguillarum challenge

Yang

Zhang

et al. 2014

Genet. Mol. Res.

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ABSTRACT.A novel collagenolytic serine protease (CLSP) was cloned from the hemocytes of the Chinese mitten crab Eriocheir sinensis (Es-CLSP). The full-length cDNA of Es-CLSP contains 990 nucleotides. It encodes a 270-amino acid-long peptide with the mature peptide containing 221 amino acids. It contains the conserved catalytic triad (H, D, and S). Similarity analysis shows that Es-CLSP shares high identity with CLSPs from the fiddler crab Uca pugilator. Es-CLSP mRNA expression in E. sinensis is a) tissue-related with the highest expression in hemocytes and widely distributed, b) highly responsive to Vibrio anguillarum challenge in hemocytes, and c) a different response to the intruding pathogens. The results of this study demonstrate the successful isolation of Es-CLSP and indicate that Es-CLSP is an immune-related gene, and show the possible role of CLSP in the invertebrate innate immune system.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Molecular characteristic and expression analysis of collagenolytic serine protease from the Chinese mitten crab Eriocheir sinensis with defense response to Vibrio anguillarum challenge

Yang

Zhang

et al. 2014

Genet. Mol. Res.

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“…The difference between trypsin and chymotrypsin is that Ser189 (numbering as in bovine chymotrypsin) [25] in trypsin is replaced with Asp at the bottom of the substrate-binding pocket. Although the substrate-binding pocket residues of SPs are variable, in chymotrypsins they usually consist of Ser189, Gly216 and Ala/Gly226 [26].…”

Section: Discussionmentioning

confidence: 99%

Molecular cloning, characterization and expression analysis of a chymotrypsin-like serine protease from kuruma shrimp Marsupenaeus japonicus

et al. 2009

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The mRNA encoding chymotrypsin-like serine protease (Mj-chy) from a kuruma shrimp Marsupenaeus japonicus hepatopancreas was identified as a peptidoglycan-inducible gene by 5 0 -end serial analysis of gene expression. The transcript of Mj-chy consists of a 816-nucleotide open reading frame encoding 271 amino acids, including a signal peptide of 17 amino acids and a trypsinlike serine protease domain of 219 amino acids. Like most serine proteases, Mj-chy has a catalytic triad consisting of histidine, aspartic acid and serine, and six cysteine residues forming three disulfide bridges. In a phylogenetic analysis, the trypsin-like serine protease domain clustered with invertebrate chymotrypsins and was closely related to chymotrypsin-like serine protease from Chinese shrimp Fenneropenaeus chinensis and chymotrypsin BI from Pacific white shrimp Litopenaeus vannamei. Mj-chy was detected in the hepatopancreas, stomach and intestine, and exhibited increased expression in defense-related tissues (i.e., hemocytes, lymphoid organ and hepatopancreas) after peptidoglycan stimulation.

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“…Salivary protease activity was detected in the mirids Lygus rugulipennis (Miridae) (Laurema et al, 1985) and Creontiades dilutus (Miridae) (Colebatch et al, 2001). In Zelus renardii and both Lygus hesperus and Lygus lineolaris (Miridae), salivary gland protease activity is predominantly trypsin-like (Cohen, 1993;Agusti and Cohen, 2000), but in Creontiades dilutus, chymotrypsin-like pro-tease activity appears to predominate in the salivary glands (Colebatch et al, 2002). Heteroptera midgut proteases are predominantly acidic proteases from both the cysteine and aspartic mechanistic classes (Houseman, 1978;Houseman andDowne, 1981, 1983;Overney et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning, Gene Structure, Expression, and Enzyme Activity of a Serine Protease from Water Scorpion, Laccotrephes japonensis (Hemiptera: Nepidae)

Park¹,

Choi²,

Nam³

et al. 2012

International Journal of Industrial Entomology

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Serine proteases are major insect enzymes involved in the digestion of dietary proteins and in the process of blood meal digestion. In this study, cDNA was constructed using the whole body of Laccotrephes japonensis. The flanking sequences of the 5-and 3-end of this gene were characterized by RACE-PCR. Sequence analysis showed that this gene contained a 963-bp ORF encoding 320 amino acids. The deduced amino acid sequence showed 62% identity with the Creontiades dilutus serine protease, 58% with the Lygus lineolaris trypsin precursor, and 54% with the Triatoma infestans salivary trypsin. To assess the expression of the L. japonensis serine protease (JGsp), the JGsp gene was cloned into a baculovirus transfer vector, pBac-1, and expressed in Sf9 cells (Spodoptera frugiperda). SDS-PAGE and western blot analysis have shown that the JGsp recombinant protein was a monomer with a molecular weight of about 32 kDa. Recombinant JGsp has shown activity in the protease enzyme assay using gelatin as a substrate.

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cDNA cloning of a salivary chymotrypsin-like protease and the identification of six additional cDNAs encoding putative digestive proteases from the green mirid, Creontiades dilutus (Hemiptera: Miridae)

Cited by 27 publications

References 39 publications

Molecular characteristic and expression analysis of collagenolytic serine protease from the Chinese mitten crab Eriocheir sinensis with defense response to Vibrio anguillarum challenge

Molecular characteristic and expression analysis of collagenolytic serine protease from the Chinese mitten crab Eriocheir sinensis with defense response to Vibrio anguillarum challenge

Molecular cloning, characterization and expression analysis of a chymotrypsin-like serine protease from kuruma shrimp Marsupenaeus japonicus

Molecular Cloning, Gene Structure, Expression, and Enzyme Activity of a Serine Protease from Water Scorpion, Laccotrephes japonensis (Hemiptera: Nepidae)

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