The subtilisins of fungal pathogens of insects, nematodes and plants: distribution and variation

Segers, R.; Butt, Tariq M.; Carder, John; Keen, Jeff N.; Kerry, B. R.; Peberdy, John F.

doi:10.1017/s0953756298007345

Cited by 39 publications

(11 citation statements)

References 42 publications

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“…For M. anisopliae, proteases are fundamental for pathogenicity, since proteins are abundant molecules present in arthropod cuticle (St Leger et al 1989, 1996aGillespie et al 1998). This fungus secretes a diverse array of proteases, particularly subtilisins, which are fundamental to transpose insect cuticle, colonize and digest tissues, to survive in diverse niches in the environment during saprophytic existence, and may also influence virulence and/or host specificity (St Leger et al 1996c;Segers et al 1999;Freimoser et al 2003;Wang et al 2005a, b). The identification of different proteases, including the subtilisins Pr1I and Pr1J, elastase-like serine protease, carboxypeptidase, chymotrypsin and trypsin, reinforces the importance of proteases and the ability of this isolate to cross arthropod cuticle.…”

Section: Discussionmentioning

confidence: 99%

Metarhizium anisopliae host–pathogen interaction: differential immunoproteomics reveals proteins involved in the infection process of arthropods

et al. 2010

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Section: Discussionmentioning

confidence: 99%

Metarhizium anisopliae host–pathogen interaction: differential immunoproteomics reveals proteins involved in the infection process of arthropods

et al. 2010

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“…The second is the subtilisin N domain-containing family, which is only expanded in Coccidioides and U. reesii. These extracellular serine-proteases are implicated in the pathogenic activity of several fungi (Segers et al 1999;da Silva et al 2006), including Aspergillus fumigatus (Monod et al 2002), and are important virulence factors in many prokaryotes (Henderson and Nataro 2001). Subtilisin N domains often associate with a peptidase S8 family domain, which includes several well-described keratinolytic subtilases (keratinases) (Descamps 2005;Cao et al 2008).…”

Section: Gene Family Expansions and Contractionsmentioning

confidence: 99%

Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives

et al. 2009

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While most Ascomycetes tend to associate principally with plants, the dimorphic fungi Coccidioides immitis and Coccidioides posadasii are primary pathogens of immunocompetent mammals, including humans. Infection results from environmental exposure to Coccidiodies, which is believed to grow as a soil saprophyte in arid deserts. To investigate hypotheses about the life history and evolution of Coccidioides, the genomes of several Onygenales, including C. immitis and C. posadasii; a close, nonpathogenic relative, Uncinocarpus reesii; and a more diverged pathogenic fungus, Histoplasma capsulatum, were sequenced and compared with those of 13 more distantly related Ascomycetes. This analysis identified increases and decreases in gene family size associated with a host/substrate shift from plants to animals in the Onygenales. In addition, comparison among Onygenales genomes revealed evolutionary changes in Coccidioides that may underlie its infectious phenotype, the identification of which may facilitate improved treatment and prevention of coccidioidomycosis. Overall, the results suggest that Coccidioides species are not soil saprophytes, but that they have evolved to remain associated with their dead animal hosts in soil, and that Coccidioides metabolism genes, membrane-related proteins, and putatively antigenic compounds have evolved in response to interaction with an animal host.

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“…Fungal subtilases are typically extracellular and have a role in nutrition (Segers et al, 1999). Fungal proteases can degrade host proteins to provide nitrogen for plant pathogenic fungi (Sreedhar et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

Leptosphaeria maculans, a fungal pathogen of Brassica napus, secretes a subtilisin-like serine protease

Wilson

Howlett

2005

Eur J Plant Pathol

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Leptosphaeria maculans, a fungal pathogen of Brassica napus, secretes large amounts of a 28 kDa protein (SP2) in liquid culture. This protein shows high sequence similarity to secreted serine proteases from other ascomycetes and is the major component of culture filtrate with protease activity, as analysed on casein zymogels. The sp2 gene is expressed during infection of B. napus cotyledons when L. maculans hyphae are growing between mesophyll cells, as well as at later stages when the fungus invades the vascular tissue.

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The subtilisins of fungal pathogens of insects, nematodes and plants: distribution and variation

Cited by 39 publications

References 42 publications

Metarhizium anisopliae host–pathogen interaction: differential immunoproteomics reveals proteins involved in the infection process of arthropods

Metarhizium anisopliae host–pathogen interaction: differential immunoproteomics reveals proteins involved in the infection process of arthropods

Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives

Leptosphaeria maculans, a fungal pathogen of Brassica napus, secretes a subtilisin-like serine protease

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