A Genetic Study of an Extracellular Elastin-hydrolysing Protease in the Ringworm Fungus Arthroderma benhamiae

Cheung, S.C.; Maniotis, James

doi:10.1099/00221287-74-2-299

Cited by 6 publications

(3 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Dermatophytes are equipped with a broad spectrum of enzymes, enabling them to penetrate the stratum corneum and to digest keratins, other proteins, lipids and DNA 24,30–39 . Gene expression and the release of enzymes by dermatophytes strongly depend on the nutritional conditions 36,40,41 .…”

Section: Invasion and Pathogenicitymentioning

confidence: 99%

Current knowledge of host response in human tinea

Brasch

2009

Mycoses

View full text Add to dashboard Cite

Skin infection caused by dermatophytes is called tinea. In this short review, the known mechanisms and factors involved in human tinea and important for the host response are briefly delineated. To establish tinea, fungal propagules must attach to the skin, germinate and overcome the epidermal barrier. Keratinases and other enzymes are released in this process and host keratinocytes are activated. This is followed by an inflammatory response mediated by a plentitude of cytokines and receptors, comprising innate as well as acquired immunity, including neutrophilic granulocytes, macrophages, antibodies and T cells. Cellular defence mechanisms appear to be decisive for clearing of infection. Nails and hair follicles are the particular sites often invaded by dermatophytes that show distinctive patterns of infection. Nails are largely excluded from defence mechanisms and steroid hormones of the pilosebaceous units may have a particular effect on follicular infection. Fungal invasion of the dermis can cause granulomatous reactions. Immune reactions to dermatophytes may lead to sterile eruptions distant from the infected skin areas.

show abstract

Section: Invasion and Pathogenicitymentioning

confidence: 99%

Current knowledge of host response in human tinea

Brasch

2009

Mycoses

View full text Add to dashboard Cite

show abstract

“…Their pattern of nitrogen utilisation is very similar to that of areA r mutants of A. nidulans. However, wild-type A. nidulans could not eciently degrade elastin (Cheung and Maniotis 1973) to serve as a good nitrogen source. In contrast, the proteolytic activity required to degrade this elastin is present in A. niger.…”

Section: Disruption Of the Area Niger Genementioning

confidence: 99%

Isolation of UV-induced mutations in the areA nitrogen regulatory gene of Aspergillus niger, and construction of a disruption mutant

et al. 2001

View full text Add to dashboard Cite

The areA gene of filamentous fungi encodes a positive-acting transcriptional factor required for the expression of genes involved in the utilisation of nitrogen sources other than ammonium and glutamine. In Aspergillus niger we have isolated three UV-induced areA mutants and constructed a well-defined disruption allele of the areA gene. The areA gene was genetically localised on Linkage Group III, 3.6 map units (m.u.) from bioA1 and 4.5 m.u. from lysA7. Analysis of the expression of the nitrate reductase encoding gene and of nitrate reductase activities show that the mutated areA strains behave as loss-of-function mutants and can be classified as areAr type. In addition, growth tests were performed using several nitrogen sources in combination with glucose. The results suggest that, unlike the case in A. nidulans, in A. niger the AreA protein also plays a role in the presence of ammonium. Furthermore, the spectrum of protease activities secreted by A. niger differs from that produced by A. nidulans, as only A. niger is able to degrade elastin.

show abstract

“…Nor are the human pathogens a preferred choice as sources of genes for recombinant expression of industrially relevant enzymes because the resulting enzymes may have strong inherent health risks. The keratinase activities of some of these fungi have been partly characterized without identification of the involved genes (Cheung and Maniotis 1973 ; Giudice et al 2012 ). Some proteases of these fungi have also been purified or recombinantly expressed to investigate their role in infection but not for investigation of their potential use as industrial keratinases (Asahi et al 1985 ; Brouta et al 2002 ; Chen et al 2010 ; Lee et al 1987 ; Sriranganadane et al 2011 ).…”

Section: Introductionmentioning

confidence: 99%

Genome and secretome analyses provide insights into keratin decomposition by novel proteases from the non-pathogenic fungus Onygena corvina

Huang

Busk

Herbst

et al. 2015

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Poultry processing plants and slaughterhouses produce huge quantities of feathers and hair/bristle waste annually. These keratinaceous wastes are highly resistant to degradation. Onygena corvina, a non-pathogenic fungus, grows specifically on feathers, hooves, horn, and hair in nature. Hence, the proteases secreted by O. corvina are interesting in view of their potential relevance for industrial decomposition of keratinaceous wastes. We sequenced and assembled the genome of O. corvina and used a method called peptide pattern recognition to identify 73 different proteases. Comparative genome analysis of proteases in keratin-degrading and non-keratin-degrading fungi indicated that 18 putative secreted proteases from four protease families (M36, M35, M43, and S8) may be responsible for keratin decomposition. Twelve of the 18 predicted protease genes could be amplified from O. corvina grown on keratinaceous materials and were transformed into Pichia pastoris. One of the recombinant proteases belonging to the S8 family showed high keratin-degrading activity. Furthermore, 29 different proteases were identified by mass spectrometry in the culture broth of O. corvina grown on feathers and bristle. The culture broth was fractionated by ion exchange chromatography to isolate active fractions with five novel proteases belonging to three protease families (S8, M28, and M3). Enzyme blends composed of three of these five proteases, one from each family, showed high degree of degradation of keratin in vitro. A blend of novel proteases, such as those we discovered, could possibly find a use for degrading keratinaceous wastes and provide proteins, peptides, and amino acids as valuable ingredients for animal feed.Electronic supplementary materialThe online version of this article (doi:10.1007/s00253-015-6805-9) contains supplementary material, which is available to authorized users.

show abstract

A Genetic Study of an Extracellular Elastin-hydrolysing Protease in the Ringworm Fungus Arthroderma benhamiae

Cited by 6 publications

References 4 publications

Current knowledge of host response in human tinea

Current knowledge of host response in human tinea

Isolation of UV-induced mutations in the areA nitrogen regulatory gene of Aspergillus niger, and construction of a disruption mutant

Genome and secretome analyses provide insights into keratin decomposition by novel proteases from the non-pathogenic fungus Onygena corvina

Contact Info

Product

Resources

About