Expression of a serine proteinase homolog prophenoloxidase-activating factor from the blue crab, Callinectes sapidus

Buda, Elizabeth S.; Shafer, Thomas H.

doi:10.1016/j.cbpc.2004.11.017

Cited by 43 publications

(33 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A previous study reported that the clip domain in PPAF had antibacterial activity in vitro ). In the clip domain of SpPPAF, six cysteine residues were identified, which is similar to the clip domain of PPAF from other arthropods, such as P. monodon (Ma et al, 2014) and C. sapidus (Buda and Shafer, 2005). By comparing the canonical clip domains with other SPs, it is predicted that these cysteines will form three pairs of disulfide bonds and thus, are expected to form quite a compact structure.…”

Section: Discussionmentioning

confidence: 83%

“…PPAFs also belong to the SPs/SPHs family and can convert pro-PO to the active form of PO, causing melanization of pathogens. Several PPAFs have been reported in crustaceans, including the blue crab Callinectes sapidus (Buda and Shafer, 2005), the freshwater crayfish Pacifastacus leniusculus , the black tiger shrimp Penaeus monodon (Charoensapsri et al, 2009(Charoensapsri et al, , 2011Ma et al, 2014), and the white shrimp Litopenaeus vannamei (Jang et al, 2011). According to some previous studies, PPAFs have different functions in different species.…”

Section: Introductionmentioning

confidence: 99%

“…According to some previous studies, PPAFs have different functions in different species. For example, PPAF in blue crabs can control and regulate molting (Buda and Shafer, 2005); PPAF II in Holotrichia diomphalia serves as a cofactor of PPAF-I and is involved in the activation of the pro-PO system (Kwon et al, 2000); in silkworm Bombyx mori, the purified PPAF enzyme itself can cleave prophenoloxidase at Arg 51 and fully activate the proenzyme (Satoh et al, 1999). Several PPAF protein sequences have been purified and cloned from some arthropod species, but few from crustacean species.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Characterization and expression analysis of the prophenoloxidase activating factor from the mud crab Scylla paramamosain

et al. 2015

View full text Add to dashboard Cite

ABSTRACT. Prophenoloxidase activating factors (PPAFs) are a group of clip domain serine proteinases that can convert prophenoloxidase (pro-PO) to the active form of phenoloxidase (PO), causing melanization of pathogens. Here, two full-length PPAF cDNAs from Scylla paramamosain (SpPPAF1 and SpPPAF2) were cloned and characterized. The full-length SpPPAF1 cDNA was 1677 bp in length, including a 5'-untranslated region (UTR) of 52 bp, an open reading frame (ORF) of 1131 bp coding for a polypeptide of 376 amino acids, and a 3'-UTR of 494 bp. The full-length SpPPAF2 cDNA was 1808 bp in length, including a 5'-UTR of 88 bp, an ORF of 1125 bp coding for a polypeptide of 374 amino acids, and a 3'-UTR of 595 bp. The estimated molecular weight of SpPPAF1 and SpPPAF2 was 38.43 and 38.56 kDa with an isoelectric point of 7.54 and 7.14, respectively. Both SpPPAF1 and SpPPAF2 proteins consisted of a signal peptide, a characteristic structure of clip domain, and a carboxyl-terminal trypsin- (2015) like serine protease domain. Expression analysis by qRT-PCR showed that SpPPAF1 mRNA was mainly expressed in the gill, testis, and hemocytes, and SpPPAF2 mRNA was mainly expressed in hemocytes. In addition, SpPPAF1 and SpPPAF2 mRNA was expressed in a timedependent manner after Vibrio parahaemolyticus challenge. The results showed that expression of both SpPPAF1 and SpPPAF2 was related to the bacterial challenge but the expression patterns differed. These findings suggest that SpPPAF is a serine proteinase and may be involved in the pro-PO activation pathway of the crab innate immune system.

show abstract

Section: Discussionmentioning

confidence: 83%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Characterization and expression analysis of the prophenoloxidase activating factor from the mud crab Scylla paramamosain

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Although the SIPC is present in both old and new cuticle of B. amphitrite (figure 4e), we believe it is unlikely that it is a structural protein since it does not contain the R&R (Rebers & Riddiford 1988) consensus sites that are involved in binding cuticular proteins to chitin (Rebers & Willis 2001;Willis et al 2005). A particular role of the arthropod cuticle is now realized to be in the immune response since it contains serine proteinases (Buda & Shafer 2005). In this respect, it is interesting to note that the B. amphitrite SIPC shows sequence similarities to the a 2 -macroglobulin (A2M) protein family (Dreanno et al in revision), which is involved in innate immunity (Armstrong & Quigley 1999) and that in the lobster, an A2M-like protein may play a role in olfaction (Hollins et al 2003).…”

Section: Discussionmentioning

confidence: 99%

Locating the barnacle settlement pheromone: spatial and ontogenetic expression of the settlement-inducing protein complex ofBalanus amphitrite

2006

View full text Add to dashboard Cite

Barnacles are prominent members of hard substratum benthic communities and their study has been important to advances in experimental ecology and contemporary ecological theory. Having recently characterized the cue to gregarious settlement of Balanus amphitrite, the settlement-inducing protein complex (SIPC), we use two polyclonal antibodies to examine the tissue distribution and ontogenetic expression of this glycoprotein. These antibodies were raised against two separate peptides located near the N-and C-termini of the SIPC and were used to detect the glycoprotein by western blotting and immunohistochemistry. By in situ hybridization we also show that the SIPC mRNA co-occurs with the expressed glycoprotein in the cuticles of both nauplius and cypris larval stages and the adult. In the larvae, the SIPC is expressed most strongly in the mouthparts and the hindgut of the stage 2 nauplius and in the thoracopods, antennules and bivalved carapace of the cyprid. In adult B. amphitrite, the expressed SIPC is present in protein extracts of the shell and in all organs that are lined by cuticular tissues. We suggest that the SIPC is produced by the epidermal cells that secrete the cuticle and discuss these observations with regard to earlier studies and the role of the SIPC as a contact pheromone.

show abstract

“…So far, many reports have been published on clip domain SPs from aquatic species (Buda et al 2005;Jimenez-Vega et al 2005;Rattanachai et al 2005;Lin et al 2006;Amparyup et al 2007;Charoensapsri et al 2009;Ren et al 2009;Cui et al 2010;Tassanakajon et al 2010;Qin et al 2010;Vaseeharan et al 2011) and only a few on non-clip domain SPs from aquatic species including Penaeus vannamei (Jimenez-Vega et al 2005), Panulirus argus (Levine et al 2001), Fenneropenaeus chinensis (Ren et al 2011) and Pacifastacus leniusculus (Hernandez-Cortes et al 1999). It is interesting to note that all the SPs reported in aquatic organisms are from invertebrates only.…”

Section: Introductionmentioning

confidence: 99%

Striped murrel S1 family serine protease: immune characterization, antibacterial property and enzyme activities

et al. 2014

View full text Add to dashboard Cite

Abstract:We report a molecular characterization of S1 family serine protease (SP-1) from snakehead murrel (or called striped murrel) Channa striatus (Cs). CsSP-1 polypeptide contained a catalytic core domain (otherwise known as serine protease trypsin domain) between H 20 and I 237 along with a catalytic triad at H 61 , D 104 and S 197 . Phylogenetic analysis confirmed that CsSP-1 belongs to serine protease S1 family. The tertiary structure showed that CsSP-1 contains 14 β-sheets as 2 separate β-barrels (the first β-barrel consists of 8 β-sheets in the N-terminal region and the second β-barrel consists of 6 β-sheets in the C-terminal region) and 3 α-helical regions. Significantly (P < 0.05) the highest CsSP-1 mRNA expression was observed in intestine, liver and kidney, moderate expression was seen in spleen, head kidney, skin and blood, and the lowest one in brain, gill, muscle and heart. Further, the expression was induced in intestine with fungus Aphanomyces invadans and bacteria Aeromonas hydrophila. The recombinant CsSP-1 protein showed antibacterial activity against both gram-negative and gram-positive bacteria. The optimum CsSP-1 enzyme activity against the substrate casein was determined at 8 mM casein concentration. Moreover, the activity was highly influenced by 5 mM phenyl-methylsulfonyl fluoride followed by ethylenediaminetetraacetic acid, 4-(2-aminoethyl)benzenesulfonylfluoride hydrochloride and calpain inhibitor I. The CsSP-1 enzyme exhibited the highest activity at pH 7.5 and temperature 35• C. The overall results showed the potential involvement of CsSP-1 in the immune system of murrels. However, further research is necessary to study the mechanism of implicit trypsin association in the defence process.

show abstract

Expression of a serine proteinase homolog prophenoloxidase-activating factor from the blue crab, Callinectes sapidus

Cited by 43 publications

References 35 publications

Characterization and expression analysis of the prophenoloxidase activating factor from the mud crab Scylla paramamosain

Characterization and expression analysis of the prophenoloxidase activating factor from the mud crab Scylla paramamosain

Locating the barnacle settlement pheromone: spatial and ontogenetic expression of the settlement-inducing protein complex ofBalanus amphitrite

Striped murrel S1 family serine protease: immune characterization, antibacterial property and enzyme activities

Contact Info

Product

Resources

About