Functional characterization of a masquerade-like serine proteinase homologue from the black tiger shrimp Penaeus monodon

Jitvaropas, Rungrat; Amparyup, Piti; Gross, Paul S.; Tassanakajon, Anchalee

doi:10.1016/j.cbpb.2009.03.007

Cited by 42 publications

(27 citation statements)

References 47 publications

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“…In addition, PcALF1 may have opsonic activity to enhance phagocytosis of bacterial cells by hemocytes. This higher bacterial clearance efficiency was also reported in some previous studies [50,51], and the authors suggested the results were due to the opsonic activities of the investigated proteins as well. Thus, the mechanism on how PcALF1 functions should be studied further in subsequent in vivo experiments.…”

Section: Discussionsupporting

confidence: 79%

An anti-lipopolysaccharide factor from red swamp crayfish, Procambarus clarkii, exhibited antimicrobial activities in vitro and in vivo

Sun

Zhang

et al. 2011

Fish & Shellfish Immunology

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Section: Discussionsupporting

confidence: 79%

An anti-lipopolysaccharide factor from red swamp crayfish, Procambarus clarkii, exhibited antimicrobial activities in vitro and in vivo

Sun

Zhang

et al. 2011

Fish & Shellfish Immunology

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“…LGGQGGG repeats might have antimicrobial peptide activity [26]. Recombinant N-terminal region of the PmMasSPH comprising the glycine rich repeats and the clip domain show antibacterial activity [14]. FcMas in hemocytes was down-regulated by Vibrio and WSSV challenge.…”

Section: Discussionmentioning

confidence: 99%

“…A masquerade-like protein discovered in Pacifastacus leniusculus hemocytes is involved in granulocyte adhesion, pattern recognition, and opsonization [12,13]. The recombinant C-terminal SP-like domain of Penaeus mondon masquerade has the ability to bind Vibrio harveyi and LPS, showing hemocyte adhesion activity [14]. The N-terminal region, including clip domain, shows antimicrobial activity in vitro.…”

mentioning

confidence: 99%

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

Ren

Zhao

Wang

2011

Fish & Shellfish Immunology

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“…observed that the SP from tobacco hornworm, Manduca sexta, showed the antibacterial activity against both gram-negative and grampositive bacteria. Further researchers Wang et al 2001;Lin et al 2006;Jitvaropas et al 2009) also observed that the SP homologues from various crustacean species have the antibacterial activity against both gram-negative and gram-positive bacteria. Tsuji et al (1998) found that a 26 kDa SP from flesh fly Sarcophaga peregrina was toxic to the following bacteria and yeasts: S. aureus, Corynebacterium bovis, B. subtilis, E. coli, Salmonella typhi, Candida albicans and Candida pseudotropicalis.…”

Section: Discussionmentioning

confidence: 94%

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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Functional characterization of a masquerade-like serine proteinase homologue from the black tiger shrimp Penaeus monodon

Cited by 42 publications

References 47 publications

An anti-lipopolysaccharide factor from red swamp crayfish, Procambarus clarkii, exhibited antimicrobial activities in vitro and in vivo

An anti-lipopolysaccharide factor from red swamp crayfish, Procambarus clarkii, exhibited antimicrobial activities in vitro and in vivo

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

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

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