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. 1988 Jun;64(2):353–357.

The role of galactosyl-binding lectin in the cellular immune response of the cockroach Periplaneta americana (Dictyoptera).

A M Lackie 1, G R Vasta 1
PMCID: PMC1384968  PMID: 3391649

Abstract

Agglutinating activity of the major serum lectin of Periplaneta americana against mammalian erythrocytes has been found previously to be inhibited most effectively by galactose and glycoproteins rich in non-reducing terminal galactose, such as porcine stomach mucin (PSM) and desialylated fetuin and bovine submaxillary mucin. Antibody raised against the purified lectin was found, by immunofluorescence, to bind to the surface of washed fixed haemocytes (the cells responsible for cellular immunity in insects). The experiments described here were carried out in order to investigate whether or not the lectin plays any role in mediating the haemocytic response, by measuring the in vivo cellular response to galactose- or sialic acid-rich glycoproteins, either in solution or conjugated to Sepharose beads. Comparison of the ability of injected solutions to stimulate haemocytic aggregates (nodules) showed that PSM, whether native, desialylated or pronase-digested to produce small galactose-containing fragments, stimulated large numbers of nodules, in contrast to either sialic acid-rich glycoproteins such as bovine submaxillary mucin (BSM) and fetuin, or the protein bovine serum albumen (BSA). Multicellular capsules formed around Sepharose conjugated to galactose-rich molecules such as PSM, asialo-PSM, asialo-fetuin or asialo-BSM were highly significantly thicker than those formed around control untreated beads, whereas capsules around BSA, fetuin or BSM conjugates were significantly thinner. It is unlikely that the different results for sialylated and desialylated molecules are due merely to a non-specific charge effect, since the response due to charge alone is directly opposite to that found when specific carbohydrate groups are considered. The results tentatively support the idea that soluble and/or cell-associated lectins may be involved in immuno-recognition in insects.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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