Cysteine proteases of parasitic organisms

被引:679
作者
Sajid, M [1 ]
McKerrow, JH [1 ]
机构
[1] Univ Calif San Francisco, Trop Dis Res Unit, San Francisco, CA 94122 USA
关键词
cysteine protease; Papain-family; legumain-like; GPI : protein transamidase; classification; protease trafficking; evolution; nutrition; biological function; S-2; pocket; occluding loop; chemotherapy; pH; immunoevasion; tissue and cell invasion; protein processing; excystment and serodiagnostics;
D O I
10.1016/S0166-6851(01)00438-8
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
Cysteine proteases play numerous indispensable roles in the biology of parasitic organisms. Aside from previously known general catabolic functions and protein processing. cysteine proteases may be key to parasite immunoevasion, excystment/encystment, exsheathing and cell and tissue invasion. Parasite cysteine proteases are unusually immunogenic and have been exploited as serodiagnostic markers and vaccine targets. Although host homologues exist. parasite cysteine proteases have distinct structural and biochemical properties including, pH optima and stability. the alteration in peptide loops or domain extensions, diverse substrate specificity and cellular location. The disparate nature of parasite cysteine protease compared to the host orthologous proteins has opened opportunities for chemotherapy. This review will highlight recent research on the 'papain-like' class of cysteine proteases, the most abundant family, and the newly, discovered class of asparaginyl-endopeptidases. Cysteine protease classification will be re-examined in light of the diversity uncovered within parasitic organisms. (C) 2002 Published by Elsevier Science B.V.
引用
收藏
页码:1 / 21
页数:21
相关论文
共 106 条
[1]   NAEGLERIA-FOWLERI - CHARACTERIZATION OF A SECRETED HISTOLYTIC CYSTEINE PROTEASE [J].
ALDAPE, K ;
HUIZINGA, H ;
BOUVIER, J ;
MCKERROW, J .
EXPERIMENTAL PARASITOLOGY, 1994, 78 (02) :230-241
[2]   IRON MEDIATES TRICHOMONAS-VAGINALIS RESISTANCE TO COMPLEMENT LYSIS [J].
ALDERETE, JF ;
PROVENZANO, D ;
LEHKER, MW .
MICROBIAL PATHOGENESIS, 1995, 19 (02) :93-103
[3]  
Alexander J, 1998, J IMMUNOL, V161, P6794
[4]   Looking for the exit: How do malaria parasites escape from red blood cells? [J].
Bannister, LH .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (02) :383-384
[5]  
BARRETT AJ, 1994, METHOD ENZYMOL, V244, P1
[6]   ISOLATION OF LMCPC, A GENE ENCODING A LEISHMANIA-MEXICANA CATHEPSIN-B-LIKE CYSTEINE PROTEINASE [J].
BART, G ;
COOMBS, GH ;
MOTTRAM, JC .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1995, 73 (1-2) :271-274
[7]   PLASMODIUM-BERGHEI AND PLASMODIUM-CHABAUDI - A NEUTRAL ENDOPEPTIDASE IN PARASITE EXTRACTS AND PLASMA OF INFECTED ANIMALS [J].
BERNARD, F ;
MAYER, R ;
PICARD, I ;
DEGUERCY, A ;
MONSIGNY, M ;
SCHREVEL, J .
EXPERIMENTAL PARASITOLOGY, 1987, 64 (01) :95-103
[8]   PURIFICATION OF A PLASMODIUM-BERGHEI NEUTRAL ENDOPEPTIDASE AND ITS LOCALIZATION IN MEROZOITE [J].
BERNARD, F ;
SCHREVEL, J .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1987, 26 (1-2) :167-173
[9]   ALIGNMENT PHYLOGENY OF THE PAPAIN SUPERFAMILY OF CYSTEINE PROTEASES [J].
BERTI, PJ ;
STORER, AC .
JOURNAL OF MOLECULAR BIOLOGY, 1995, 246 (02) :273-283
[10]  
Blackman Michael J., 2000, Current Drug Targets, V1, P59, DOI 10.2174/1389450003349461