Secreted proteases from pathogenic fungi

被引:264
作者
Monod, M
Capoccia, S
Léchenne, B
Zaugg, C
Holdom, M
Jousson, O
机构
[1] CHU Vaudois, Lab Mycol, Serv Dermatol, DHURDV, CH-1011 Lausanne, Switzerland
[2] Guys Hosp, St Johns Inst, Dept Dermatol, London SE1 9RT, England
关键词
proteases; virulence; Candida; Aspergillus; dermatophytes; adherence;
D O I
10.1078/1438-4221-00223
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Many species of human pathogenic fungi secrete proteases in vitro or during the infection process. Secreted endoproteases belong to the aspartic proteases of the pepsin family, serine proteases of the subtilisin family, and metalloproteases of two different families. To these proteases has to be added the non-pepsin-type aspartic protease from Aspergillus niger and a unique chymotrypsin-like protease from Coccidioides immitis. Pathogenic fungi also secrete aminopeptidases, carboxypeptidases and dipeptidyl-peptidases. The function of fungal secreted proteases and their importance in infections vary. It is evident that secreted proteases are important for the virulence of dermatophytes since these fungi grow exclusively in the stratum corneum, nails or hair, which constitutes their sole nitrogen and carbon sources. The aspartic proteases secreted by Caudida albicans are involved in the adherence process and penetration of tissues, and in interactions with the immune system of the infected host. For Aspergillus fumigatus, the role of proteolytic activity has not yet been proved. Although the secreted proteases have been intensively investigated as potential virulence factors, knowledge on protease substrate specificities is rather poor and few studies have focused on the research of inhibitors. Knowledge of substrate specificities will increase our understanding about the action of each protease secreted by pathogenic fungi and will help to determine their contribution to virulence.
引用
收藏
页码:405 / 419
页数:15
相关论文
共 153 条
[11]   MOLECULAR-CLONING AND DELETION OF THE GENE ENCODING ASPERGILLOPEPSIN-A FROM ASPERGILLUS-AWAMORI [J].
BERKA, RM ;
WARD, M ;
WILSON, LJ ;
HAYENGA, KJ ;
KODAMA, KH ;
CARLOMAGNO, LP ;
THOMPSON, SA .
GENE, 1990, 86 (02) :153-162
[12]  
BIGUET J, 1967, REV IMMUNOL, V31, P317
[13]  
Blinkovsky AM, 1999, APPL ENVIRON MICROB, V65, P3298
[14]   EXPRESSION OF EXTRACELLULAR ACID PROTEINASE BY PROTEOLYTIC CANDIDA SPP DURING EXPERIMENTAL-INFECTION OF ORAL-MUCOSA [J].
BORG, M ;
RUCHEL, R .
INFECTION AND IMMUNITY, 1988, 56 (03) :626-631
[15]   The expression of the secreted aspartyl proteinases Sap4 to Sap6 from Candida albicans in murine macrophages [J].
Borg-von Zepelin, M ;
Beggah, S ;
Boggian, K ;
Sanglard, D ;
Monod, M .
MOLECULAR MICROBIOLOGY, 1998, 28 (03) :543-554
[16]   Adherence of different Candida dubliniensis isolates in the presence of fluconazole [J].
Borg-von Zepelin, M ;
Niederhaus, T ;
Gross, U ;
Seibold, M ;
Monod, M ;
Tintelnot, K .
AIDS, 2002, 16 (09) :1237-1244
[17]   HIV-protease inhibitors reduce cell adherence of Candida albicans strains by inhibition of yeast secreted aspartic proteases [J].
Borg-von Zepelin, M ;
Meyer, I ;
Thomssen, R ;
Würzner, R ;
Sanglard, D ;
Telenti, A ;
Monod, M .
JOURNAL OF INVESTIGATIVE DERMATOLOGY, 1999, 113 (05) :747-751
[18]  
BorgvonZepelin M, 1997, MYCOSES, V40, P64, DOI 10.1111/j.1439-0507.1997.tb00544.x
[19]   Secreted metalloprotease gene family of Microsporum canis [J].
Brouta, F ;
Descamps, F ;
Monod, M ;
Vermout, S ;
Losson, B ;
Mignon, B .
INFECTION AND IMMUNITY, 2002, 70 (10) :5676-5683
[20]  
Brouta F, 2001, MED MYCOL, V39, P269, DOI 10.1080/mmy.39.3.269.275