The effect of temperature and antimetabolites on antibody binding to the outer surface of second stage Toxocara canis larvae

Smith, H. V.; Quinn, R.; Kusel, J. R.; Girdwood, R. W. A.

doi:10.1016/0166-6851(81)90017-7

Cited by 82 publications

(36 citation statements)

References 9 publications

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“…One mode of immune evasion is the ability of T canis larvae to shed the entire surface coat in response to binding by antibodies (35) or eosinophils (36), thus permitting parasites to physically escape immune attack (37). The identification of a mucin on the surface may, in addition, explain a generally nonadhesive property of the parasite.…”

Section: Discussionmentioning

confidence: 99%

An abundantly expressed mucin-like protein from Toxocara canis infective larvae: the precursor of the larval surface coat glycoproteins.

Gems¹,

Maizels²

1996

Proc. Natl. Acad. Sci. U.S.A.

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Section: Discussionmentioning

confidence: 99%

An abundantly expressed mucin-like protein from Toxocara canis infective larvae: the precursor of the larval surface coat glycoproteins.

Gems¹,

Maizels²

1996

Proc. Natl. Acad. Sci. U.S.A.

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“…The antibody response to proteases secreted by A. simplex might be responsible for the eventual death of tissue-invasive larvae through prevention of nutrient acquisition by the parasite and/or restriction of its mobility so that other immune effectors, such as cellular attack, can act. It has been observed, however, that antibodies bound to the surface of living larvae are rapidly shed (M. W. Kennedy, unpublished data) in a fashion similar to that seen with larvae of the humaninfective larvae of the dog ascaridid Toxocara canis, for instance (143,250).…”

Section: Innate Immune Responsesmentioning

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 membrane was stained with Stains-all (Bio-Rad) and the bands corresponding to TES-120 identified. Approximately 210 g of TES products were then carboxymethylated with 50 Ci of iodo [2][3][4][5][6][7][8][9][10][11][12][13][14] C]acetic acid; 53 g of the labeled TES products were applied to a Q-Sepharose column (15 m; Amersham Pharmacia Biotech) and subjected to strong anion exchange (SAX) chromatography. Fractions were eluted using a gradient of 0 -1 M NaCl in 20 mM Tris-HCl (pH 8.0) and 20% acetonitrile.…”

Section: Methodsmentioning

confidence: 99%

“…Although the life cycle is completed only in the definitive canine host, larval stages are capable of infecting a vast range of organisms, including humans in whom it causes visceral and ocular larva migrans (6). The immune system is singularly ineffective against the larvae, due in part to the parasite's ability to shed its surface coat when under attack from antibodies and/or leukocytes (7)(8)(9)(10). In addition, larvae release prodigious quantities of heavily glycosylated Toxocara excretory/secretory (TES) 1 antigens, which can be collected by in vitro cultivation (11)(12)(13)(14).…”

mentioning

confidence: 99%

A Family of Secreted Mucins from the Parasitic Nematode Toxocara canis Bears Diverse Mucin Domains but Shares Similar Flanking Six-cysteine Repeat Motifs

Loukas

Hintz

Linder

et al. 2000

Journal of Biological Chemistry

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Infective larvae of the parasitic nematode Toxocara canis secrete a family of mucin-like glycoproteins, which are implicated in parasite immune evasion. Analysis of T. canis expressed sequence tags identified a family of four mRNAs encoding distinct apomucins (Tcmuc-1-4), one of which had been previously identified in the TES-120 family of glycoproteins secreted by this parasite. The protein products of all four cDNAs contain signal peptides, a repetitive serine/threonine-rich tract, and varying numbers of 36-amino acid six-cysteine (SXC) domains. SXC domains are found in many nematode proteins and show similarity to cnidarian (sea anemone) toxins. Antibodies to the SXC domains of Tc-MUC-1 and Tc-MUC-3 recognize differently migrating members of TES-120. TES-120 proteins separated by chromatographic methods showed distinct amino acid composition, mass, and sequence information by both Edman degradation and matrix-assisted laser desorption ionization/time of flight mass spectrometry on peptide fragments. Tc-MUC-1, -2, and -3 were shown to be secreted mucins with real masses of 39.7, 47.8, and 45.0 kDa in contrast to their predicted peptide masses of 15.7, 16.2, and 26.0 kDa, respectively. The presence of SXC domains in all mucin products supports the suggestion that the SXC motif is required for mucin assembly or export. Homology modeling indicates that the sixcysteine domains of the T. canis mucins adopt a similar fold to the sea anemone potassium channel-blocking toxin BgK, forming three disulfide bonds within each subunit.

show abstract

The effect of temperature and antimetabolites on antibody binding to the outer surface of second stage Toxocara canis larvae

Cited by 82 publications

References 9 publications

An abundantly expressed mucin-like protein from Toxocara canis infective larvae: the precursor of the larval surface coat glycoproteins.

An abundantly expressed mucin-like protein from Toxocara canis infective larvae: the precursor of the larval surface coat glycoproteins.

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

A Family of Secreted Mucins from the Parasitic Nematode Toxocara canis Bears Diverse Mucin Domains but Shares Similar Flanking Six-cysteine Repeat Motifs

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