Characterisation of a serine proteinase from Penaeus vannamei haemocytes

Jiménez-Vega, Florinda; Vargas‐Albores, Francisco; Söderhäll, Kenneth

doi:10.1016/j.fsi.2004.02.001

Cited by 47 publications

(35 citation statements)

References 34 publications

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“…GenBank homology search and CLUSTAL W multiple sequence alignment confirmed that the cloned cDNA sequence of S. serrata encodes a SP domain. This sequence contains the conserved residues of the putative active site, His150, Asp217 and Ser331, which form the characteristic SP catalytic triad found in crustaceans [16,17,27]. Furthermore, the sequence alignment of S. serrata SP revealed that the predicted amino acid sequence was homologous to other arthropod trypsin-like SP in the NCBI GenBank and showed similarity of 55%, 51% and 50% to SP from spiny lobster P. argus, horseshoe crab T. tridentatus and crayfish P. leniusculus, respectively (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…For example, SP is involved in antimicrobial response in horseshoe crab Tachypleus tridentatus [11], pattern recognition in crayfish P. leniusculus [12], somatic muscle attachment in fruit fly Drosophila embryos [8] and immune response in African malaria mosquito Anopheles gambiae [13]. The SPs and SPHs have been cloned and characterised in domestic silkworm Bombyx mori [24], crayfish P. leniusculus [12,14], coleopteran Holotrichia diomphalia [7,15], kuruma shrimp Marsupenaeus japonicus [16], white shrimp Litopenaeus vannamei [17], horseshoe crab T. tridentatus [18], spiny lobster Panulirus argus [19], and centipede Scolopendra subspinipes mulilans [20].…”

Section: Introductionmentioning

confidence: 99%

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Cloning and characterisation of a serine proteinase from the haemocytes of mud crab Scylla serrata

Vaseeharan

Chen

2006

Fish & Shellfish Immunology

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Cloning and characterisation of a serine proteinase from the haemocytes of mud crab Scylla serrata

Vaseeharan

Chen

2006

Fish & Shellfish Immunology

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“…The serine protease domain confers a specific proteolytic activity to Csp as demonstrated in biochemical experiments on P. argus (Johns et al 2004). Serine proteases are involved in a wide range of physiologically important processes in which they act after being secreted extracellularly: digestion (Sellos and Van Wormhoudt 1999), development of diverse organs (Yamada et al 2000), and immune responses (Jiang et al 2003;Jimenez-Vega et al 2005). In several cases, however, serine proteases also have been found to be involved in the intracellular processing of proteins (Chen et al 2000;Sallmyr et al 2002).…”

Section: Possible Nature Of Secretions Produced By Atgs and Possible mentioning

confidence: 99%

Rosette-type tegumental glands associated with aesthetasc sensilla in the olfactory organ of the Caribbean spiny lobster, Panulirus argus

et al. 2006

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The lateral antennular flagellum of decapod crustaceans bears unique olfactory sensilla, namely the aesthetascs, and other sensilla types. In this study, we identify a new major tissue in the lateral flagellum of the Caribbean spiny lobster, Panulirus argus, namely "aesthetasc tegumental glands" (ATGs), based on immunostaining with antibodies against CUB serine protease (Csp), in situ hybridization with csp-specific probes, labeling with the F-actin marker phalloidin, labeling with the nuclear marker Hoechst 33258, and staining with methylene blue. Each ATG has 12-20 secretory cells arranged in a rosette. Each secretory cell has a Csp-immunoreactive basal portion and an apical portion containing granular material (metachromatic staining indicative of acid mucopolysaccharides). At the center of each secretory rosette is a phalloidin-positive common locus that gives rise to a main drainage duct projecting toward the cuticle. Scanning electron and light microscopy show that thin ducts traverse the cuticle and connect to "peg pores" proximal to the bases of the aesthetascs, with 3.4 peg pores per aesthetasc. Since the number of common loci is correlated with the number of peg pores, we conclude that each pore represents the outlet of one ATG, and that the secretions are released from them. We conclude further that ATGs and aesthetascs are functionally linked. We hypothesize that ATG secretions have antifouling and/or friction-reducing properties, and that they are spread over the surface of the aesthetascs by antennular grooming. A review of the literature suggests that ATGs are common in decapod crustacean antennules, and that rosette glands and grooming might be functionally coupled in other body areas.

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“…A common feature of these enzymes is that they contain at least one disulfide-bridged structure known as a clip domain, and therefore they are also called clip domain serine proteinases (clip-SPs) (Jiang and Kanost, 2000). SPHs are similar in amino acid sequence to SPs but apparently lack amidase activity since one or more of the catalytic residues are missing or mutated (Jiménez-Vega et al, 2005). SPs and SPHs have become a hotspot of recent research and were found to have diverse functions, such as melanocyte encapsulation, induction of anti-microbial peptide synthesis, embryo protection, and cytokine activation (Kawabata et al, 1996;Jiang and Kanost, 2000;Kanost et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2015

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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.

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Characterisation of a serine proteinase from Penaeus vannamei haemocytes

Cited by 47 publications

References 34 publications

Cloning and characterisation of a serine proteinase from the haemocytes of mud crab Scylla serrata

Cloning and characterisation of a serine proteinase from the haemocytes of mud crab Scylla serrata

Rosette-type tegumental glands associated with aesthetasc sensilla in the olfactory organ of the Caribbean spiny lobster, Panulirus argus

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

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