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. 2009 Jan 7;10(3):285–299. doi: 10.1111/j.1600-0854.2008.00864.x

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© 2009 The Authors. Journal compilation © 2009 Blackwell Munksgaard

Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.

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Immunoblot with α-GFP antibodies against GBP130 chimaeras fractionated with saponin indicates that processing occurred in the parasite fraction (pellet) before export. Antibodies to aldolase were used to validate parasite membrane integrity following saponin treatment (note the presence of aldolase in the pellet fractions but absence from the supernatant fractions) and reflects the quantity of protein loaded in each lane. More of the GBP130_R>A and GBP130_L>A chimaera samples were loaded because of rapid loss of fluorescence over time in parasites overexpressing these mutant chimaeras. The GBP130_RILE>A chimaera traffics predominantly to the parasitophorous vacuole (see supernatant fraction). That unprocessed bands of GBP130_R>A, GBP130_L>A and GBP130_RILE>A are present in the supernatant fraction confirms breakdown of the parasitophorous vacuole membrane by saponin.