INDUCTION OF SECRETORY ACID PROTEINASE IN CANDIDA-ALBICANS

被引:44
作者
BANERJEE, A [1 ]
GANESAN, K [1 ]
DATTA, A [1 ]
机构
[1] JAWAHARLAL NEHRU UNIV,SCH LIFE SCI,MOLEC BIOL LAB,NEW DELHI 110067,INDIA
来源
JOURNAL OF GENERAL MICROBIOLOGY | 1991年 / 137卷
关键词
D O I
10.1099/00221287-137-10-2455
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Candida albicans and some other pathogenic Candida species, when grown in a medium containing a protein as a sole source of nitrogen, secrete an acid proteinase. Culture supernatants were assayed for proteinase activity, and were also analysed by Western blotting with antibodies raised and affinity-purified against proteinase of C. albicans. Proteinases secreted by C. tropicalis and C. parapsilosis were antigenically related to that of C. albicans, but had different molecular masses. The proteinases secreted by C. lipolytica, C. rugosa and C. lusitaniae were not antigenically related. The kinetics of proteinase secretion by C. albicans were monitored by activity and by Western blotting. With BSA as the nitrogen source, proteinase secretion increased exponentially until about 16 h. Culture supernatants of BSA-grown cultures accumulated proteinase to about a 1000-fold higher level than those of ammonium-sulphate-grown cultures. In vivo labelling experiments showed that proteinase was not detectably accumulated in the cells, but was secreted immediately after synthesis. Immunoprecipitation of in vitro translated poly(A)-containing RNA identified a putative pre-protein of about 54 kDa. As well as BSA, other proteins (haemoglobin, ovalbumin, histone), peptone and tryptone, when used as nitrogen sources, could induce proteinase, but to different levels. When Casamino acids or an amino acid mixture (equivalent to the composition of BSA) was used as nitrogen source, no induction was observed. Ammonium sulphate, or any other ammonium salt, repressed secretion of proteinase.
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页码:2455 / 2461
页数:7
相关论文
共 24 条
[1]  
ANDERSON DJ, 1983, METHOD ENZYMOL, V96, P111
[2]  
Ausubel FM., 1995, MOL REPROD DEV, V3rd edn, DOI DOI 10.1002/MRD.1080010210
[3]   FLUOROGRAPHIC DETECTION OF RADIOACTIVITY IN POLYACRYLAMIDE GELS WITH THE WATER-SOLUBLE FLUOR, SODIUM-SALICYLATE [J].
CHAMBERLAIN, JP .
ANALYTICAL BIOCHEMISTRY, 1979, 98 (01) :132-135
[4]  
CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
[5]   DETECTION OF PROTEASES BY CLOTTING OF CASEIN AFTER GEL-ELECTROPHORESIS [J].
FOLTMANN, B ;
SZECSI, PB ;
TARASOVA, NI .
ANALYTICAL BIOCHEMISTRY, 1985, 146 (02) :353-360
[6]   NUMBER AND DISTRIBUTION OF POLYADENYLATED RNA SEQUENCES IN YEAST [J].
HEREFORD, LM ;
ROSBASH, M .
CELL, 1977, 10 (03) :453-462
[7]   ALPHA-B-CRYSTALLIN IS EXPRESSED IN NON-LENTICULAR TISSUES AND ACCUMULATES IN ALEXANDERS DISEASE BRAIN [J].
IWAKI, T ;
KUMEIWAKI, A ;
LIEM, RKH ;
GOLDMAN, JE .
CELL, 1989, 57 (01) :71-78
[8]  
Kessler S W, 1981, Methods Enzymol, V73, P442
[9]   CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4 [J].
LAEMMLI, UK .
NATURE, 1970, 227 (5259) :680-+
[10]   INDUCIBLE PROTEINASE OF CANDIDA-ALBICANS IN DIAGNOSTIC SEROLOGY AND IN THE PATHOGENESIS OF SYSTEMIC CANDIDOSIS [J].
MACDONALD, F ;
ODDS, FC .
JOURNAL OF MEDICAL MICROBIOLOGY, 1980, 13 (03) :423-+