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Identification of oversulphated galactosaminoglycans in intestinal-mucosal mast cells of rats infected with the nematode worm Nippostrongylus brasiliensis.

ABSTRACT: The oversulphated galactosaminoglycans synthesized by rat mucosal mast cells were isolated from the small intestine of animals infected with the nematode Nippostrongylus brasiliensis, which causes proliferation of these cells. The 35S-labelled polysaccharides were degraded by digestion with chondroitinase ABC, and the structures of the disaccharide products were determined by cleavage with mercuric acetate followed by electrophoretic characterization of the resultant sulphated monosaccharides. It was concluded that about half of the disulphated disaccharide units in the polysaccharide consisted of chondroitin sulphate E-type structures [GlcA-GalNAc(4,6-di-OSO3)], in which both sulphate groups were located on the N-acetylgalactosamine unit. The remainder consisted of isomeric structures with one sulphate group on the N-acetylgalactosamine residue and one on the hexuronic acid unit and presumably represented the dermatan sulphate-type sequence [IdoA(2-OSO3)-GalNAc(4-OSO3)].

SUBMITTER: Kusche M

PROVIDER: S-EPMC1149385 | biostudies-other | 1988 Aug

REPOSITORIES: biostudies-other

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Project description:BACKGROUND: Nematode secreted haemoglobins have unusually high affinity for oxygen and possess nitric oxide deoxygenase, and catalase activity thought to be important in protection against host immune responses to infection. In this study, we generated a monoclonal antibody (48Eg) against haemoglobin of the nematode Anisakis pegreffii, and aimed to characterize cross-reactivity of 4E8g against haemoglobins of different nematodes and its potential to mediate protective immunity against a murine hookworm infection. METHODOLOGY/PRINCIPAL FINDINGS: Immunoprecipitation was used to isolate the 4E8g-binding antigen in Anisakis and Ascaris extracts, which were identified as haemoglobins by peptide mass fingerprinting and MS/MS. Immunological cross-reactivity was also demonstrated with haemoglobin of the rodent hookworm N. brasiliensis. Immunogenicity of nematode haemoglobin in mice and humans was tested by immunoblotting. Anisakis haemoglobin was recognized by IgG and IgE antibodies of Anisakis-infected mice, while Ascaris haemoglobin was recognized by IgG but not IgE antibodies in mouse and human sera. Sequencing of Anisakis haemoglobin revealed high similarity to haemoglobin of a related marine nematode, Psuedoterranova decipiens, which lacks the four -HKEE repeats of Ascaris haemoglobin important in octamer assembly. The localization of haemoglobin in the different parasites was examined by immunohistochemistry and associated with the excretory-secretary ducts in Anisakis, Ascaris and N. brasiliensis. Anisakis haemoglobin was strongly expressed in the L3 stage, unlike Ascaris haemoglobin, which is reportedly mainly expressed in adult worms. Passive immunization of mice with 4E8g prior to infection with N. brasiliensis enhanced protective Th2 immunity and led to a significant decrease in worm burdens. CONCLUSION: The monoclonal antibody 4E8g targets haemoglobin in broadly equivalent anatomical locations in parasitic nematodes and enhances host immunity to a hookworm infection.

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Identification of oversulphated galactosaminoglycans in intestinal-mucosal mast cells of rats infected with the nematode worm Nippostrongylus brasiliensis.

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