کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9140131 | 1163398 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Erythrocyte surface glycosylphosphatidyl inositol anchored receptor for the malaria parasite
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کلمات کلیدی
PBSmAbGPAPlasmodium yoeliiDuffy Antigen Receptor for ChemokinesMonoclonal antibody - آنتی بادی مونوکلونالEDTA - اتیلن دی آمین تترا استیک اسید Ethylenediaminetetraacetic acid - اتیلینیدامین تتراستیک اسیدInvasion - تهاجمDARC - دارسیPhosphate buffered saline - فسفات بافر شورGPI anchor - لنگر GPIMalaria - مالاریاErythrocyte - گلبول قرمز یا اریتروسیتGlycophorin A - گلیکوفورین A
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
Parasitophorous vacuole formation is a critical step for the successful invasion of host erythrocytes by the malaria parasite. Rhoptry proteins are believed to have essential roles in vacuole formation, although their biological roles are poorly understood. To understand the molecular interactions between parasite rhoptry proteins and the erythrocyte during invasion, we have characterized the binding specificity of the high molecular mass rhoptry protein (RhopH) complex to erythrocytes using the rodent malaria parasite, Plasmodium yoelii. RhopH complex binding to erythrocytes was species-specific, observed with mouse but not rabbit or human erythrocytes. Binding is abolished following treatment of erythrocytes with trypsin or chymotrypsin. Because host cell cholesterol-rich membrane domains are recruited into the nascent parasitophorous vacuole, we evaluated a possible role of RhopH complex binding to the cholesterol-rich membrane domain-associated glycosylphosphatidyl inositol (GPI)-anchored protein. Using chimeric mice harboring GPI-deficient erythrocytes, RhopH complex binding to GPI-deficient mouse erythrocytes was undetectable, indicating involvement of GPI-anchored protein in PyRhopH complex binding. Furthermore, a significant reduction of P. yoelii parasite infection of GPI-deficient erythrocytes was observed in vivo, probably due to inefficient invasion. We conclude that the major erythrocyte receptor for PyRhopH complex is a protein attached to the erythrocyte surface via GPI-anchor and that GPI-deficient erythrocytes are resistant to P. yoelii invasion.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Molecular and Biochemical Parasitology - Volume 140, Issue 1, March 2005, Pages 13-21
Journal: Molecular and Biochemical Parasitology - Volume 140, Issue 1, March 2005, Pages 13-21
نویسندگان
Thanaporn Rungruang, Osamu Kaneko, Yoshiko Murakami, Takafumi Tsuboi, Hiroshi Hamamoto, Nobuyoshi Akimitsu, Kazuhisa Sekimizu, Taroh Kinoshita, Motomi Torii,