Functional characterisation of a nematode secreted GM2-activator protein.

Abstract:

:We have identified a GM2-activator protein (GM2AP) with highly unusual properties secreted by the nematode parasite Trichinella spiralis. Expression in Pichia pastoris resulted in a hyperglycosylated protein of 28 kDa, but the 18 kDa native protein was not glycosylated. The parasite GM2AP does not facilitate degradation of GM2 ganglioside by N-acetyl-beta-hexosaminidase A, although it does inhibit phospholipase D activity. Lack of the former activity might be explained by the absence of a domain implicated in binding to hexosaminidase. In addition, and contrary to data on the human GM2AP, the nematode homologue does not inhibit platelet activating factor-induced calcium mobilisation in neutrophils, but actually enhances mediator-induced chemotaxis.

journal_name

Mol Biochem Parasitol

authors

Bruce AF,Gares MP,Selkirk ME,Gounaris K

doi

10.1016/j.molbiopara.2006.02.014

subject

Has Abstract

pub_date

2006-06-01 00:00:00

pages

224-9

issue

2

eissn

0166-6851

issn

1872-9428

pii

S0166-6851(06)00072-7

journal_volume

147

pub_type

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