A cytochrome b561 with ferric reductase activity from the parasitic blood fluke, Schistosoma japonicum.

BACKGROUND: Iron has an integral role in numerous cellular reactions and is required by virtually all organisms. In physiological conditions, iron is abundant in a largely insoluble ferric state. Ferric reductases are an essential component of iron uptake by cells, reducing iron to the soluble ferro...

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Bibliographic Details
Published in:PLoS Neglected Tropical Diseases
Main Authors: Amber Glanfield, Donald P McManus, Danielle J Smyth, Erica M Lovas, Alex Loukas, Geoffrey N Gobert, Malcolm K Jones
Format: Article in Journal/Newspaper
Language:English
Published: Public Library of Science (PLoS) 2010
Subjects:
Arctic medicine. Tropical medicine
RC955-962
Public aspects of medicine
RA1-1270
Arctic
Online Access:https://doi.org/10.1371/journal.pntd.0000884
https://doaj.org/article/d7b2ea59f98d4c45af8f16a9ab7e5e4d
Description
Summary:BACKGROUND: Iron has an integral role in numerous cellular reactions and is required by virtually all organisms. In physiological conditions, iron is abundant in a largely insoluble ferric state. Ferric reductases are an essential component of iron uptake by cells, reducing iron to the soluble ferrous form. Cytochromes b561 (cyts-b561) are a family of ascorbate reducing transmembrane proteins found in most eukaryotic cells. The identification of the ferric reductase duodenal cytochrome b (dcytb) and recent observations that other cyts-b561 may be involved in iron metabolism have opened novel perspectives for elucidating their physiological function. METHODOLOGY/PRINCIPAL FINDINGS: Here we have identified a new member of the cytochrome b561 (Sjcytb561) family in the pathogenic blood fluke Schistosoma japonicum that localises to the outer surface of this parasitic trematode. Heterologous expression of recombinant Sjcyt-b561 in a Saccharomyces cerevisiae mutant strain that lacks plasma membrane ferrireductase activity demonstrated that the molecule could rescue ferric reductase activity in the yeast. SIGNIFICANCE/CONCLUSIONS: This finding of a new member of the cytochrome b561 family further supports the notion that a ferric reductase function is likely for other members of this protein family. Additionally, the localisation of Sjcytb561 in the surface epithelium of these blood-dwelling schistosomes contributes further to our knowledge concerning nutrient acquisition in these parasites and may provide novel targets for therapeutic intervention.

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