The source, release and specificity of proteolytic enzyme activity produced by<i>Anisakis simplex</i>larvae (Nematoda: Ascaridida) in<i>vitro</i>

Matthews, Bernard E.

doi:10.1017/s0022149x00026924

Cited by 29 publications

(18 citation statements)

References 22 publications

(14 reference statements)

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“…Trypsinlike activity from the secretions of A. simplex larvae was also observed by Matthews (1984). Larval Anisakis hydrolyzed trypsin-specific substrates such as N-a-benzoyl-D,L-arginine p-nitroanilide and N-a-benzoyl-L-arginine ethyl ester but not the chymotrypsin substrate N-benzoyl-L-tryosine ethyl ester (Matthews, 1984).…”

Section: Discussionmentioning

confidence: 86%

“…Proteases secreted from larval A. simplex that degrade denatured collagen have been identified (Matthews, 1982(Matthews, , 1984Kennedy et al, 1988). To substantiate further the role proteases might play in tissue invasion by A. simplex, we identified and partially characterized the major neutral proteases released by third-stage larvae and determined that they degraded macromolecular components similar to those found in the wall of the stomach and intestine.…”

Section: Anisakiasis Is a Parasitic Disease Caused By The Accidental mentioning

confidence: 98%

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Identification of the Secreted Neutral Proteases from Anisakis simplex

Sakanari

McKerrow²

1990

The Journal of Parasitology

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Ingestion of larval nematodes (family: Anisakidae) can cause the human disease known as anisakiasis. After ingestion, Anisakis larvae can be invasive, penetrating host stomach or intestinal wall. Observation of larvae penetrating the tissue layers of human stomach in vitro by SEM showed tunnels and burrows were formed in the mucosa and submucosa. Based on these observations, we hypothesized that secreted proteases may be involved in the degradation of host tissue macromolecules to allow tunnel formation. Using a model of connective tissue extracellular matrix (ECM), we found that as few as 5 Anisakis simplex larvae could degrade approximately 25% of the ECM in a 16-mm culture well in 24 hr. Further characterization of the secreted proteases using synthetic peptide substrates and inhibitors revealed that there were 2 classes of proteases present: a metallo aminopeptidase and a trypsinlike serine protease. Extracts of Anisakis larvae contained a 25-kDa protease that was recognized by rabbit anti-rat trypsin antibody on western blots. This suggests that there is structural as well as functional similarity between the Anisakis trypsin and vertebrate trypsins.

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Section: Discussionmentioning

confidence: 86%

Section: Anisakiasis Is a Parasitic Disease Caused By The Accidental mentioning

confidence: 98%

Identification of the Secreted Neutral Proteases from Anisakis simplex

Sakanari

McKerrow²

1990

The Journal of Parasitology

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“…They are produced by cells situated in the oesophagus or by secretive glands and are referred to as excretive-secretive products (ES). The composition of the products has been particularly well-studied in Platyhelminthes and Nematoda (Ruitenberg & Loendersloot 1971;Hinck & Ivey 1976;Matthews 1984;Knox & Kennedy 1998;Moczoń & Wranicz 1999;Jefferies et al 2001;Irwin et al 2004). The enzymes contained in ES products (phosphatases, aminopeptydases, oxidoreductases, esterases, glucosidases) are referred to as penetrating enzymes.…”

Section: G -Glossiphonia Complanatamentioning

confidence: 99%

Activity of selected hydrolytic enzymes from leeches (Clitellata: Hirudinida) with different feeding strategies

2009

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Hydrolase activities of extracts from different parts of the bodies of parasitic (Theromyzon tessulatum, Piscicola geometra) and predatory (Erpobdella octoculata, Glossiphonia complanata) leeches were examined. The highest activity was detected in the extracts from sections containing the intestine. Hydrolase activities in the crop and intestine of parasitic leeches were higher than in predatory leeches. The high activity of most of hydrolases in those segments may indicate the intensity of digestion and absorption processes in leeches. A lack of trypsin activity and low chymotrypsin activity are likely to result from the presence of inhibitors of these enzymes. The high activity of the majority of the analyzed hydrolases in extracts derived from the head segment of predatory leeches enables, through digestion of tissues, their easy access to physiological fluids of a host. In turn, in extracts from the head segment of predatory leeches, only four hydrolases were shown to be active. Lipase activity was not found in any of the samples, while α-galactosidase activity was found only in extracts from the head segment of T. tessulatum and P. geometra. Trypsin activity was detected in the extract from the intestine contents of H. sanguisuga and in the extract from the head segment of P. geometra. The results demonstrate the presence of majority of hydrolases occurring in other animals in the alimentary tract of leeches. The study also shows that the crop of leeches is not only a food reservoir, but also the site where digestion and absorption processes take place.

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“…These proteases are probably produced by the dorsal esophageal gland and the excretory cell of the A. simplex larva to be secreted through the excretory pore and the oral opening, respectively (46,179,231). Proteolytic entities of 54.3 kDa (179), 23.4 and 46 kDa (149), and 25 to 26 kDa (234, 235) have been isolated from excretory-secretory (ES) products released by A. simplex L3 in vitro.…”

Section: Invasive Mechanismsmentioning

confidence: 99%

Anisakis simplex: from Obscure Infectious Worm to Inducer of Immune Hypersensitivity

2008

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SUMMARY Infection of humans with the nematode worm parasite Anisakis simplex was first described in the 1960s in association with the consumption of raw or undercooked fish. During the 1990s it was realized that even the ingestion of dead worms in food fish can cause severe hypersensitivity reactions, that these may be more prevalent than infection itself, and that this outcome could be associated with food preparations previously considered safe. Not only may allergic symptoms arise from infection by the parasites (“gastroallergic anisakiasis”), but true anaphylactic reactions can also occur following exposure to allergens from dead worms by food-borne, airborne, or skin contact routes. This review discusses A. simplex pathogenesis in humans, covering immune hypersensitivity reactions both in the context of a living infection and in terms of exposure to its allergens by other routes. Over the last 20 years, several studies have concentrated on A. simplex antigen characterization and innate as well as adaptive immune response to this parasite. Molecular characterization of Anisakis allergens and isolation of their encoding cDNAs is now an active field of research that should provide improved diagnostic tools in addition to tools with which to enhance our understanding of pathogenesis and controversial aspects of A. simplex allergy. We also discuss the potential relevance of parasite products such as allergens, proteinases, and proteinase inhibitors and the activation of basophils, eosinophils, and mast cells in the induction of A. simplex-related immune hypersensitivity states induced by exposure to the parasite, dead or alive.

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The source, release and specificity of proteolytic enzyme activity produced byAnisakis simplexlarvae (Nematoda: Ascaridida) invitro

Cited by 29 publications

References 22 publications

Identification of the Secreted Neutral Proteases from Anisakis simplex

Identification of the Secreted Neutral Proteases from Anisakis simplex

Activity of selected hydrolytic enzymes from leeches (Clitellata: Hirudinida) with different feeding strategies

Anisakis simplex: from Obscure Infectious Worm to Inducer of Immune Hypersensitivity

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