CpABC, a Cryptosporidium parvum ATP-binding cassette protein at the host-parasite boundary in intracellular stages

被引:55
作者
Perkins, ME
Riojas, YA
Wu, TW
Le Blancq, SM
机构
[1] Columbia Univ, Joseph L Mailman Sch Publ Hlth, Div Environm Hlth Sci, New York, NY 10032 USA
[2] Columbia Univ, Ctr Environm Res & Conservat, New York, NY 10027 USA
关键词
D O I
10.1073/pnas.96.10.5734
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The intracellular parasite Cryptosporidium parvum develops inside a vacuole at the apex of its epithelial host cell. The developing parasite is separated from the host cell cytoplasm by a zone of attachment that consists of an extensively folded membranous structure known as the feeder organelle, It has been proposed that the feeder organelle is the site of regulation of transport of nutrients and drugs into the parasite. In this report, we localize an approximate to 200-kDa integral membrane protein, CpABC, from Cryptosporidium parvum to the host-parasite boundary, possibly the feeder organelle, The predicted amino acid sequence of CpABC has significant structural similarity with the cystic fibrosis conductance regulator and the multidrug resistance protein subfamily of ATP-binding cassette proteins, This is an example of a parasite-encoded transport protein localized at the parasite-host interface of an intracellular protozoan.
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页码:5734 / 5739
页数:6
相关论文
共 52 条
[1]   Probing the structural and functional domains of the CFTR chloride channel [J].
Akabas, MH ;
Cheung, M ;
Guinamard, R .
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 1997, 29 (05) :453-463
[2]  
AMBUDKAR SV, 1998, METHOD ENZYMOL, V292, P1
[3]  
Ausubel FM, 1995, CURRENT PROTOCOLS MO
[4]   Membrane topology and glycosylation of the human multidrug resistance-associated protein [J].
Bakos, E ;
Hegedus, T ;
Hollo, Z ;
Welker, E ;
Tusnady, GE ;
Zaman, GJR ;
Flens, MJ ;
Varadi, A ;
Sarkadi, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (21) :12322-12326
[5]   Functional multidrug resistance protein (MRP1) lacking the N-terminal transmembrane domain [J].
Bakos, E ;
Evers, R ;
Szakács, G ;
Tusnády, GE ;
Welker, E ;
Szabó, K ;
de Haas, M ;
van Deemter, L ;
Borst, P ;
Váradi, A ;
Sarkadi, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (48) :32167-32175
[6]   Tandem genes of Chlamydia psittaci that encode proteins localized to the inclusion membrane [J].
Bannantine, JP ;
Rockey, DD ;
Hackstadt, T .
MOLECULAR MICROBIOLOGY, 1998, 28 (05) :1017-1026
[7]   THE TOXOPLASMA-GONDII RHOPTRY PROTEIN ROP-2 IS INSERTED INTO THE PARASITOPHOROUS VACUOLE MEMBRANE, SURROUNDING THE INTRACELLULAR PARASITE, AND IS EXPOSED TO THE HOST-CELL CYTOPLASM [J].
BECKERS, CJM ;
DUBREMETZ, JF ;
MERCEREAUPUIJALON, O ;
JOINER, KA .
JOURNAL OF CELL BIOLOGY, 1994, 127 (04) :947-961
[8]   Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins [J].
Belinsky, MG ;
Bain, LJ ;
Balsara, BB ;
Testa, JR ;
Kruh, GD .
JOURNAL OF THE NATIONAL CANCER INSTITUTE, 1998, 90 (22) :1735-1741
[9]   ROLES OF PEPTIDYL-PROLYL CIS-TRANS ISOMERASE AND CALCINEURIN IN THE MECHANISMS OF ANTIMALARIAL ACTION OF CYCLOSPORINE-A, FK506, AND RAPAMYCIN [J].
BELL, A ;
WERNLI, B ;
FRANKLIN, RM .
BIOCHEMICAL PHARMACOLOGY, 1994, 48 (03) :495-503
[10]  
BLAGBURN B.L., 1997, CRYPTOSPORIDIUM CRYP