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dc.contributor.author
Baldo, A.
dc.contributor.author
Chevigné, A.
dc.contributor.author
Dumez, M. E.
dc.contributor.author
Mathy, A.
dc.contributor.author
Power, Pablo
dc.contributor.author
Tabart, J.
dc.contributor.author
Cambier, L.
dc.contributor.author
Galleni, Lorena Alejandra
dc.contributor.author
Mignon, María Belen
dc.date.available
2020-05-26T19:50:57Z
dc.date.issued
2012-10
dc.identifier.citation
Baldo, A.; Chevigné, A.; Dumez, M. E.; Mathy, A.; Power, Pablo; et al.; Inhibition of the keratinolytic subtilisin protease Sub3 from Microsporum canis by its propeptide (proSub3) and evaluation of the capacity of proSub3 to inhibit fungal adherence to feline epidermis; Elsevier Science; Veterinary Microbiology; 159; 3-4; 10-2012; 479-484
dc.identifier.issn
0378-1135
dc.identifier.uri
http://hdl.handle.net/11336/105932
dc.description.abstract
Microsporum canis is a pathogenic fungus that causes a superficial cutaneous infection called dermatophytosis, mainly in cats, dogs and humans. Proteolytic enzymes have been postulated to be key factors involved in the invasion of the stratum corneum and keratinized epidermal structures. Among these proteases, the secreted subtilisin protease Sub3 was found to be required for adherence of M. canis arthroconidia to feline epidermis. This protease is synthetized as a preproenzyme consisting of a signal peptide followed by the propeptide and the protease domain. In order to assess whether the enzymatic activity of Sub3 could be responsible for the role of the protease in the adherence process, we expressed and characterized the propeptide of Sub3 and demonstrated that this propeptide is a strong inhibitor of its mature enzyme. This propeptide acts as a noncompetitive inhibitor with dissociation constants, Ki and K?i of 170 and 130 nM respectively. When tested for its capacity to inhibit adherence of M. canis to feline epidermis using an ex vivo adherence model made of feline epidermis, the propeptide does not prevent adherence of M. canis arthroconidia because it loses its capacity to inhibit rSub3 following a direct contact with living arthroconidia, presumably through inactivation by fungal membrane-bound proteases.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
dermatophyte
dc.subject
feline epidermis
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adherence
dc.subject
secreted subtilisin
dc.subject
propeptide
dc.subject.classification
Parasitología
dc.subject.classification
Ciencias de la Salud
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CIENCIAS MÉDICAS Y DE LA SALUD
dc.title
Inhibition of the keratinolytic subtilisin protease Sub3 from Microsporum canis by its propeptide (proSub3) and evaluation of the capacity of proSub3 to inhibit fungal adherence to feline epidermis
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-05-11T18:16:57Z
dc.journal.volume
159
dc.journal.number
3-4
dc.journal.pagination
479-484
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Baldo, A.. Université de Liège; Bélgica
dc.description.fil
Fil: Chevigné, A.. Université de Liège; Bélgica
dc.description.fil
Fil: Dumez, M. E.. Université de Liège; Bélgica
dc.description.fil
Fil: Mathy, A.. Université de Liège; Bélgica
dc.description.fil
Fil: Power, Pablo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Université de Liège; Bélgica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Tabart, J.. Université de Liège; Bélgica
dc.description.fil
Fil: Cambier, L.. Université de Liège; Bélgica
dc.description.fil
Fil: Galleni, Lorena Alejandra. Université de Liège; Bélgica
dc.description.fil
Fil: Mignon, María Belen. Université de Liège; Bélgica
dc.journal.title
Veterinary Microbiology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.vetmic.2012.04.041
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0378113512002908
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