Purification and partial characterization of a β‐1,3‐glucan‐binding‐protein membrane receptor from blood cells of the crayfish <i>Pacifastacus leniusculus</i>

Duvic, Bernard; Söderhäll, Kenneth

doi:10.1111/j.1432-1033.1992.tb17041.x

Cited by 93 publications

(79 citation statements)

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“…It may, like a 76-kDa cell-adhesion protein that we have described earlier [12, 331, be stored in the secretory granules of the blood cells and released from there during degranulation. The blood cells are essential in host defence [2, 9, 341, and degradation is believed to occur during a microbial infection and can be triggered by a p-I ,3-glucan-binding protein in the plasma [35] after it has reacted with fungal cell wall &1,3-glucans [36]. As the crayfish Kazal inhibitor blocks subtilisin, it may be that its biological function is to inhibit microbial proteinases.…”

Section: Discussionmentioning

confidence: 99%

Purification and cDNA cloning of a four‐domain Kazal proteinase inhibitor from crayfish blood cells

Johansson

Keyser

Söderhäll

1994

European Journal of Biochemistry

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A cDNA with an open reading frame of 684 base pairs was isolated from a library from blood cells of the crayfish Pacifastacus leniusculus. It codes for a signal sequence and a mature protein of 209 amino acids with a predicted molecular mass of 22.7 kDa. The amino acid sequence consists of four repeated stretches (45-73% identical to each other), indicating that the protein has four domains. The domains have significant sequence similarity to serine proteinase inhibitors of the Kazal family. The three first domains have a leucine residue in the putative reactive site, suggesting that the protein is a chymotrypsin inhibitor.A monomeric 23-kDa proteinase inhibitor, which by amino terminal sequencing of the mature protein was confirmed to be the cloned Kazal inhibitor, was purified from crayfish blood cells. It inhibited chymotrypsin or subtilisin, but not trypsin, elastase or thrombin. The inhibitor seemed to form a 1 : 1 complex with chymotrypsin or subtilisin.This protein seems to be the first described Kazal inhibitor from blood cells of any animal and the first one with four domains.Invertebrates do not have antibodies or other features of the vertebrate adaptive immune system but have innate hostdefence reactions [l]. As many of them have an open circulatory system, they need efficient immediate and constitutive defence mechanisms. Proteinase inhibitors in the blood are believed to be important in this context, either aimed against proteinases of microorganisms or parasites, or being regulators of host-defence reactions [2-41.In our laboratory, several proteinase inhibitors from the blood of freshwater crayfish have been isolated. From crayfish plasma, an inhibitor homologous to mammalian a2-macroglobulin has been purified [ 5 ] and partially sequenced [6]. Also, a 155-kDa trypsin inhibitor that controls activation of the so-called prophenoloxidase activating system has been purified [7, 81 (for a review on the prophenoloxidase system, a proposed recognition and defence system in arthropods, see [2, 91). From the blood cells, a subtilisin inhibitor that inhibits fungal proteases was isolated [lo] and, recently, a proteinase inhibitor of the serpin family has been cloned (Liang, Z. and Soderhall, K., unpublished results).In this report, we present the cDNA cloning and sequencing as well as the purification and characterization of a fourdomain proteinase inhibitor of the Kazal family from crayfish blood cells.

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Section: Discussionmentioning

confidence: 99%

Purification and cDNA cloning of a four‐domain Kazal proteinase inhibitor from crayfish blood cells

Johansson

Keyser

Söderhäll

1994

European Journal of Biochemistry

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“…Purified p36 was applied to a mannose-or a GLcNAc-Sepharose column, but it did not bind (data not shown). There are no previous reports of lectins specific for glucose residues although several lectins that recognize ␤-1,3-glucan have been described (24,25). Therefore, we designated the ascidian lectin GBL.…”

Section: Binding Specificity Of P36 For Carbohydratesmentioning

confidence: 99%

An Ancient Lectin-Dependent Complement System in an Ascidian: Novel Lectin Isolated from the Plasma of the Solitary Ascidian, Halocynthia roretzi

Sekine

Kenjo²,

Azumi

et al. 2001

The Journal of Immunology

121

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Mannose-binding lectin (MBL) is a C-type lectin involved in the first line of host defense against pathogens and it requires MBL-associated serine protease (MASP) for activation of the complement lectin pathway. To elucidate the origin and evolution of MBL, MBL-like lectin was isolated from the plasma of a urochordate, the solitary ascidian Halocynthia roretzi, using affinity chromatography on a yeast mannan-Sepharose. SDS-PAGE of the eluted proteins revealed a major band of ∼36 kDa (p36). p36 cDNA was cloned from an ascidian hepatopancreas cDNA library. Sequence analysis revealed that the carboxy-terminal half of the ascidian lectin contains a carbohydrate recognition domain (CRD) that is homologous to C-type lectin, but it lacks a collagen-like domain that is present in mammalian MBLs. Purified p36 binds specifically to glucose but not to mannose or N-acetylglucosamine, and it was designated glucose-binding lectin (GBL). The two ascidian MASPs associated with GBL activate ascidian C3, which had been reported to act as an opsonin. The removal of GBL-MASPs complex from ascidian plasma using Ab against GBL inhibits C3-dependent phagocytosis. These observations strongly suggest that GBL acts as a recognition molecule and that the primitive complement system, consisting of the lectin-proteases complex and C3, played a major role in innate immunity before the evolution of an adaptive immune system in vertebrates.

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“…The Turkish crayfish has been subjected to biochemical, physiological and ecological studies where as physiology, ecology, reproduction and distribution have been subjects for P. leniusculus (Duvic & Soderhall, 1990;Firkins, 1993;Guan, This study is a part of PhD study of M.M. Harlıog˘lu supported by Fırat University Elazıg˘, TURKEY.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Consequently, many investigators have concentrated on its immune system (e.g. Persson et al, 1987;Duvic & Soderhall;Aspan & Söderhall, 1991;Kopacek et al, 1993) and the implications for susceptible crayfish when this species has been translocated (Holdich & Reeve, 1991).Descriptions of P. leniusculus and A. leptodactylus have been given in a few keys (Curra, 1967;Pennack, 1978;Laurent & Forest, 1979;Brodski, 1983;Gledhill et al, 1993;Vigneux et al, 1993) and Andrews (1907) illustrated the appendage structure of the signal crayfish. Recently, P. leniusculus was chosen as a model in the description of functional morphology of crayfish by Holdich & Reeve (1988), and Holdich (1992) also reviewed the early postembryonic development of astacid, cambarid and parastacid crayfish.…”

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A Scanning Electron Microscopic Study on the Appendage Morphology of Astacus leptodactylus (Eschscholtz, 1823) and Pacifastacus leniusculus (Daña, 1852) (Crustácea:Decapoda: Astacoidea)

Harlıoğlu

2008

Int. J. Morphol.

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Estudio en Microscopio Electrónico de SUMMARY:This study compares the morphology of rostrum, pereipods 1,2,4 and mouthparts of juvenile Astacus leptodactylus with those of Pacifastacus leniusculus. Differences in morphology were observed, in particular with regard to the mouthparts e.g. including setal armature and number of teeth on the mandible. In general, the shape of the rostra in the two species is similar in that both taper to a point with a pair of sharp spines distally. Laterally the rostrum of A. leptodactylus is bordered by a regular row of setae, which is not so well defined in P. leniusculus. The observations also showed that in addition to an increase in size, changes in morphology in the feeding apparatus between the developmental stages of the two species were present. It was concluded that both species have similar rostra, but different setal patterns and there are differences between the two species in the armature of mouthparts as development progresses. Therefore, important differences in the morphology of mouthparts between P. leniusculus and A. leptodactylus and in the different stages of the species might cause a difference in the feeding behavior and food choice of the species.KEY WORDS: Appendages; Astacus; Crayfish; Mouthparts; Pacifastacus; Scanning electron microscope. INTRODUCTIONThe signal crayfish, Pacifastacus leniusculus (Dana, 1852), is native to north-western North America inhabiting lakes, streams and rivers (Lowery & Holdich, 1988) as well as saline waters (Henry & Wheatly, 1988;Holdich et al., 1997). It is also tolerant to environmental extremes such as temperature and various pollutants (Firkins, 1993). Pacifastacus leniusculus is similar in many ways to Astacus astacus (Linnaeus, 1758) and consequently has proved popular alternative since the decline of the latter species due to the introduction crayfish plague into many Europe catchments (Holdich, 1999). The signal crayfish is identified by its red colour, and large robust chela including a white to turquoise patch on the claw gives this crayfish its common name. This North American crayfish has been introduced into many European watersheds.The narrow-clawed crayfish, Astacus leptodactylus (Eschscoltz, 1823) is a native of Turkey and near East Europe.It occupies a similar niche to that of P. leniusculus. However, in addition to streams, rivers, lakes, and ponds, it also inhabits swamps. Thus, it is sometimes called the swamp crayfish (Cherkashina, 1975;Köksal 1988, Harlioglu & Harlioglu, 2004. Astacus leptodactylus is commercially exploited either as imports or from introduced populations distributed widely across Europe, exception of the Iberian Peninsula and Nordic countries (Harlioglu & Holdich, 2001;Holdich 2002;Skurdal & Taugbol, 2002). This species is identified by its long claws (mainly typical for males) and is commonly named the narrow-clawed or Turkish crayfish (Harlioglu, 1996).Pacificastacus leniusculus and A. leptodactylus have become popular experimental animals. The Turkish crayfish has been subjected to bi...

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Purification and partial characterization of a β‐1,3‐glucan‐binding‐protein membrane receptor from blood cells of the crayfish Pacifastacus leniusculus

Cited by 93 publications

References 43 publications

Purification and cDNA cloning of a four‐domain Kazal proteinase inhibitor from crayfish blood cells

Purification and cDNA cloning of a four‐domain Kazal proteinase inhibitor from crayfish blood cells

An Ancient Lectin-Dependent Complement System in an Ascidian: Novel Lectin Isolated from the Plasma of the Solitary Ascidian, Halocynthia roretzi

A Scanning Electron Microscopic Study on the Appendage Morphology of Astacus leptodactylus (Eschscholtz, 1823) and Pacifastacus leniusculus (Daña, 1852) (Crustácea:Decapoda: Astacoidea)

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