Candida albicans Heat Shock Proteins and Hsps-Associated Signaling Pathways as Potential Antifungal Targets

被引:65
作者
Gong, Ying [1 ]
Li, Tao [2 ]
Yu, Cuixiang [3 ]
Sun, Shujuan [4 ]
机构
[1] Shandong Univ, Sch Pharmaceut Sci, Jinan, Shandong, Peoples R China
[2] Shandong Univ, Intens Care Unit, Qianfoshan Hosp, Jinan, Shandong, Peoples R China
[3] Shandong Univ, Respirat Med, Qianfoshan Hosp, Jinan, Shandong, Peoples R China
[4] Shandong Univ, Dept Pharm, Qianfoshan Hosp, Jinan, Shandong, Peoples R China
关键词
heat shock proteins; Candida albicans; signaling pathways; antifungal targets; virulence; HUMAN RECOMBINANT ANTIBODY; CELL-CYCLE PROGRESSION; DRUG-RESISTANCE; AMPHOTERICIN-B; SACCHAROMYCES-CEREVISIAE; STRESS-RESPONSE; SEROLOGICAL RESPONSE; HYPHAL DEVELOPMENT; KINASE HOMOLOG; MAP KINASE;
D O I
10.3389/fcimb.2017.00520
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
In recent decades, the incidence of invasive fungal infections has increased notably. Candida albicans (C. albicans), a common opportunistic fungal pathogen that dwells on human mucosal surfaces, can cause fungal infections, especially in immunocompromised and high-risk surgical patients. In addition, the wide use of antifungal agents has likely contributed to resistance of C. albicans to traditional antifungal drugs, increasing the difficulty of treatment. Thus, it is urgent to identify novel antifungal drugs to cope with C. albicans infections. Heat shock proteins (Hsps) exist in most organisms and are expressed in response to thermal stress. In C. albicans, Hsps control basic physiological activities or virulence via interaction with a variety of diverse regulators of cellular signaling pathways. Moreover, it has been demonstrated that Hsps confer drug resistance to C. albicans. Many studies have shown that disrupting the normal functions of C. albicans Hsps inhibits fungal growth or reverses the tolerance of C. albicans to traditional antifungal drugs. Here, we review known functions of the diverse Hsp family, Hsp-associated intracellular signaling pathways and potential antifungal targets based on these pathways in C. albicans. We hope this review will aid in revealing potential new roles of C. albicans Hsps in addition to canonical heat stress adaptions and provide more insight into identifying potential novel antifungal targets.
引用
收藏
页数:13
相关论文
共 134 条
[1]  
[Anonymous], BOUND VALUE PROBL
[2]   Involvement of Heat Shock Proteins in Candida albicans Biofilm Formation [J].
Becherelli, Marco ;
Tao, Jianshi ;
Ryder, Neil S. .
JOURNAL OF MOLECULAR MICROBIOLOGY AND BIOTECHNOLOGY, 2013, 23 (06) :396-400
[3]   The mitotic Cyclins Clb2p and Clb4p affect morphogenesis in Candida albicans [J].
Bensen, ES ;
Clemente-Blanco, A ;
Finley, KR ;
Correa-Bordes, J ;
Berman, J .
MOLECULAR BIOLOGY OF THE CELL, 2005, 16 (07) :3387-3400
[4]   Morphogenesis and cell cycle progression in Candida albicans [J].
Berman, Judith .
CURRENT OPINION IN MICROBIOLOGY, 2006, 9 (06) :595-601
[5]  
Bockmühl DP, 2001, GENETICS, V157, P1523
[6]   Ras-regulated signaling processes in Saccharomyces cerevisiae [J].
Broach, James R. .
CURRENT OPINION IN GENETICS & DEVELOPMENT, 1991, 1 (03) :370-377
[7]   Stress adaptation in a pathogenic fungus [J].
Brown, Alistair J. P. ;
Budge, Susan ;
Kaloriti, Despoina ;
Tillmann, Anna ;
Jacobsen, Mette D. ;
Yin, Zhikang ;
Ene, Iuliana V. ;
Bohovych, Iryna ;
Sandai, Doblin ;
Kastora, Stavroula ;
Potrykus, Joanna ;
Ballou, Elizabeth R. ;
Childers, Delma S. ;
Shahana, Shahida ;
Leach, Michelle D. .
JOURNAL OF EXPERIMENTAL BIOLOGY, 2014, 217 (01) :144-155
[8]   Human Monoclonal Antibody-Based Therapy in the Treatment of Invasive Candidiasis [J].
Bugli, Francesca ;
Cacaci, Margherita ;
Martini, Cecilia ;
Torelli, Riccardo ;
Posteraro, Brunella ;
Sanguinetti, Maurizio ;
Sterbini, Francesco Paroni .
CLINICAL & DEVELOPMENTAL IMMUNOLOGY, 2013,
[9]   Fungal heat-shock proteins in human disease [J].
Burnie, JR ;
Carter, TL ;
Hodgetts, SJ ;
Matthews, RC .
FEMS MICROBIOLOGY REVIEWS, 2006, 30 (01) :53-88
[10]   Candida albicans lacking the gene encoding the regulatory subunit of protein kinase A displays a defect in hyphal formation and an altered localization of the catalytic subunit [J].
Cassola, A ;
Parrot, M ;
Silberstein, S ;
Magee, BB ;
Passeron, S ;
Giasson, L ;
Cantore, ML .
EUKARYOTIC CELL, 2004, 3 (01) :190-199