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The beta-l,3-glucan-binding protein from the crayfish Pacifastacus leniusclus, when reacted with a beta-l,3-glucan, induces spreading and degranulation of crayfish granular cells

Abstract : A beta-1,3-glucan-binding protein (beta-GBP) was purified from crayfish plasma, and incubated with laminarin (L), a beta-1,3-glucan. The beta-GBP reacted with laminarin (beta-GBP-L) induced strong spreading and partial degranulation of isolated and separated crayfish granular haemocytes. However, neither the beta-GBP nor laminarin alone induced any changes in the crayfish granular cells. When monolayers of granular haemocytes were incubated with 20-mu-g of beta-GBP-L, more than 82% of the haemocytes were affected. The activity of beta-GBP-L on granular cells was dose-dependent and a plateau was reached at 10-mu-g of beta-GBP-L. The degranulation of crayfish haemocytes induced by beta-GBP-L seemed to occur by a regulated exocytosis, since it was strongly inhibited by specific blockers of this process such as SITS or calmidazolium. Monospecific anti-beta-GBP antibodies also totally blocked the effect of beta-GBP-L on crayfish granular cells. Indirect immunofluorescence staining demonstrated that the beta-GBP-L could bind to the surface of granular cells, whereas beta-GBP did not bind or bound very weakly to the haemocyte surface.
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Submitted on : Monday, June 1, 2020 - 7:32:07 PM
Last modification on : Tuesday, February 2, 2021 - 6:08:02 PM

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Margherita A. Barracco, Bernard Duvic, Kenneth Söderhäll. The beta-l,3-glucan-binding protein from the crayfish Pacifastacus leniusclus, when reacted with a beta-l,3-glucan, induces spreading and degranulation of crayfish granular cells. Cell and Tissue Research, Springer Verlag, 1991, 266 (3), pp.491-497. ⟨10.1007/bf00318590⟩. ⟨hal-02714323⟩

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