Extracellular lipid droplets promote hemozoin crystallization in the gut of the blood fluke Schistosoma mansoni

被引:44
作者
Correa Soares, Juliana B. R.
Maya-Monteiro, Clarissa M.
Bittencourt-Cunha, Paula R. B.
Atella, Georgia C.
Lara, Flavio A.
d'Avila, Joana C. P.
Menezes, Diego
Vannier-Santos, Marcos A.
Oliveira, Pedro L.
Egan, Timothy J.
Oliveira, Marcus F.
机构
[1] Univ Fed Rio de Janeiro, Inst Bioquim Med, Programa Biol Mol & Biotecnol, Rio De Janeiro, Brazil
[2] Inst Oswaldo Cruz, FIOCRUZ, Dept Fisiol & Farmacodinam, BR-20001 Rio De Janeiro, Brazil
[3] Inst Oswaldo Cruz, FIOCRUZ, Dept Micobacterioses, BR-20001 Rio De Janeiro, Brazil
[4] Fiocruz MS, Inst Goncalo Moniz, Salvador, BA, Brazil
[5] Univ Cape Town, Dept Chem, ZA-7700 Rondebosch, South Africa
关键词
hemozoin; heme; lipid droplets; Schistosoma mansoni;
D O I
10.1016/j.febslet.2007.03.054
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Hemozoin (Hz) is a heme crystal produced upon hemoglobin digestion as the main mechanism of heme disposal in several hematophagous organisms. Here, we show that, in the helminth Schistosoma mansoni, Hz formation occurs in extracellular lipid droplets (LDs). Transmission electron microscopy of adult worms revealed the presence of numerous electron-lucent round structures similar to LDs in gut lumen, where multicrystalline Hz assemblies were found associated to their surfaces. Female regurgitates promoted Hz formation in vitro in reactions partially inhibited by boiling. Fractionation of regurgitates showed that Hz crystallization activity was essentially concentrated on lower density fractions, which have small amounts of pre-formed Hz crystals, suggesting that hydrophilic-hydrophobic interfaces, and not Hz itself, play a key catalytic role in Hz formation in S. mansoni. Thus, these data demonstrate that LDs present in the gut lumen of S. mansoni support Hz formation possibly by allowing association of heme to the lipid-water interface of these structures. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:1742 / 1750
页数:9
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