Identification of three different types of serine proteases (one SP and two SPHs) in Chinese white shrimp

Ren, Qian; Zhao, Xiao‐Fan; Wang, Jin-Xing

doi:10.1016/j.fsi.2010.11.009

Cited by 21 publications

(8 citation statements)

References 34 publications

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“…In our study, PtSP was strongly expressed in haemocytes, which is similar to that observed in P. vannamei [14]. However, it is not consistent with the cSP in P. argus [15] and CUBSP in F. chinensis [16], where SP transcripts were highest expressed in olfactory organ and gill, respectively. PtSPH1 mRNA was mostly expressed in stomach, which is different from mas-like in P. leniusculus [22] and SPH2 in F. chinensis [16].…”

Section: Discussioncontrasting

confidence: 77%

“…However, it is not consistent with the cSP in P. argus [15] and CUBSP in F. chinensis [16], where SP transcripts were highest expressed in olfactory organ and gill, respectively. PtSPH1 mRNA was mostly expressed in stomach, which is different from mas-like in P. leniusculus [22] and SPH2 in F. chinensis [16]. Although the single domain SPs or SPHs are generally to be involved in digestion processes [30], all these results imply that they are tissue and species specific in crustaceans.…”

Section: Discussionmentioning

confidence: 62%

“…SP in Penaeus vannamei [14], Csp in Panulirus argus [15], CUBSP in Fenneropenaeus chinensis [16], maslike in Pacifastacus leniusculus [2] and SPH2 in F. chinensis [16]. They are proved to be properly involved in immunity system [2,16]. It is absolutely necessary to provide more information on single domain or non-clip domain SPs or SPHs.…”

Section: Introductionmentioning

confidence: 99%

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Identification and characterization of two novel types of non-clip domain serine proteases (PtSP and PtSPH1) from cDNA haemocytes library of swimming crab Portunus trituberculatus

Cui

Liu

et al. 2012

Fish & Shellfish Immunology

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Section: Discussioncontrasting

confidence: 77%

Section: Discussionmentioning

confidence: 62%

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Identification and characterization of two novel types of non-clip domain serine proteases (PtSP and PtSPH1) from cDNA haemocytes library of swimming crab Portunus trituberculatus

Cui

Liu

et al. 2012

Fish & Shellfish Immunology

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“…In arthopods, melanisation, a key step in pathogen defence, is moderated by a serine protein cascade as demonstrated for D. melanogaster serine protease MP2, which activates its prophenoloxidase system . Genes of two serine protease chymotrypsins, Fenneropenaeus chinensis chymotrypsin and Fenneropenaeus chinensis serine protease homolog 2 were up‐regulated in hepatopancreas of F. chinensis challenged with WSSV and Vibrio anguillarum . These studies suggest that serine proteases could be involved in innate immune reaction of the shrimp.…”

Section: Resultsmentioning

confidence: 78%

Protein profiling in the gut of Penaeus monodon gavaged with oral WSSV‐vaccines and live white spot syndrome virus

et al. 2014

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White spot syndrome virus (WSSV) is a pathogen that causes considerable mortality of the farmed shrimp, Penaeus monodon. Candidate 'vaccines', WSSV envelope protein VP28 and formalin-inactivated WSSV, can provide short-lived protection against the virus. In this study, P. monodon was orally intubated with the aforementioned vaccine candidates, and protein expression in the gut of immunised shrimps was profiled. The alterations in protein profiles in shrimps infected orally with live-WSSV were also examined. Seventeen of the identified proteins in the vaccine and WSSV-intubated shrimps varied significantly compared to those in the control shrimps. These proteins, classified under exoskeletal, cytoskeletal, immune-related, intracellular organelle part, intracellular calcium-binding or energy metabolism, are thought to directly or indirectly affect shrimp's immunity. The changes in the expression levels of crustacyanin, serine proteases, myosin light chain, and ER protein 57 observed in orally vaccinated shrimp may probably be linked to immunoprotective responses. On the other hand, altered expression of proteins linked to exoskeleton, calcium regulation and energy metabolism in WSSV-intubated shrimps is likely to symbolise disturbances in calcium homeostasis and energy metabolism.

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“…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

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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.

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Identification of three different types of serine proteases (one SP and two SPHs) in Chinese white shrimp

Cited by 21 publications

References 34 publications

Identification and characterization of two novel types of non-clip domain serine proteases (PtSP and PtSPH1) from cDNA haemocytes library of swimming crab Portunus trituberculatus

Identification and characterization of two novel types of non-clip domain serine proteases (PtSP and PtSPH1) from cDNA haemocytes library of swimming crab Portunus trituberculatus

Protein profiling in the gut of Penaeus monodon gavaged with oral WSSV‐vaccines and live white spot syndrome virus

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

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