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...

Autores: Baldo, A.; Chevigné, A.; Dumez, M. E.; Mathy, A.; Power, Pablo; Tabart, J.; Cambier, L.; Galleni, Lorena Alejandra; Mignon, María Belen
Año de publicación: 2012
Idioma: inglés
Tipo de recurso: artículo
Estado: versión publicada
Descripción: 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.
Fil: Baldo, A.. Université de Liège; Bélgica
Fil: Chevigné, A.. Université de Liège; Bélgica
Fil: Dumez, M. E.. Université de Liège; Bélgica
Fil: Mathy, A.. Université de Liège; Bélgica
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
Fil: Tabart, J.. Université de Liège; Bélgica
Fil: Cambier, L.. Université de Liège; Bélgica
Fil: Galleni, Lorena Alejandra. Université de Liège; Bélgica
Fil: Mignon, María Belen. Université de Liège; Bélgica
Materia: dermatophyte
feline epidermis
adherence
secreted subtilisin
propeptide
Nivel de accesibilidad: acceso abierto
Condiciones de uso: https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
Institución: Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador: oai:ri.conicet.gov.ar:11336/105932

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repository_id_str	3498
network_name_str	CONICET Digital (CONICET)
spelling	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 epidermisBaldo, A.Chevigné, A.Dumez, M. E.Mathy, A.Power, PabloTabart, J.Cambier, L.Galleni, Lorena AlejandraMignon, María Belendermatophytefeline epidermisadherencesecreted subtilisinpropeptidehttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Microsporum 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.Fil: Baldo, A.. Université de Liège; BélgicaFil: Chevigné, A.. Université de Liège; BélgicaFil: Dumez, M. E.. Université de Liège; BélgicaFil: Mathy, A.. Université de Liège; BélgicaFil: Power, Pablo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Université de Liège; Bélgica. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Tabart, J.. Université de Liège; BélgicaFil: Cambier, L.. Université de Liège; BélgicaFil: Galleni, Lorena Alejandra. Université de Liège; BélgicaFil: Mignon, María Belen. Université de Liège; BélgicaElsevier Science2012-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/105932Baldo, 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; 479-4840378-1135CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.vetmic.2012.04.041info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0378113512002908info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T13:18:48Zoai:ri.conicet.gov.ar:11336/105932instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-12-23 13:18:48.79CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv	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
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
spellingShingle	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 Baldo, A. dermatophyte feline epidermis adherence secreted subtilisin propeptide
title_short	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
title_full	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
title_fullStr	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
title_full_unstemmed	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
title_sort	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.creator.none.fl_str_mv	Baldo, A. Chevigné, A. Dumez, M. E. Mathy, A. Power, Pablo Tabart, J. Cambier, L. Galleni, Lorena Alejandra Mignon, María Belen
author	Baldo, A.
author_facet	Baldo, A. Chevigné, A. Dumez, M. E. Mathy, A. Power, Pablo Tabart, J. Cambier, L. Galleni, Lorena Alejandra Mignon, María Belen
author_role	author
author2	Chevigné, A. Dumez, M. E. Mathy, A. Power, Pablo Tabart, J. Cambier, L. Galleni, Lorena Alejandra Mignon, María Belen
author2_role	author author author author author author author author
dc.subject.none.fl_str_mv	dermatophyte feline epidermis adherence secreted subtilisin propeptide
topic	dermatophyte feline epidermis adherence secreted subtilisin propeptide
purl_subject.fl_str_mv	https://purl.org/becyt/ford/3.3 https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv	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. Fil: Baldo, A.. Université de Liège; Bélgica Fil: Chevigné, A.. Université de Liège; Bélgica Fil: Dumez, M. E.. Université de Liège; Bélgica Fil: Mathy, A.. Université de Liège; Bélgica 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 Fil: Tabart, J.. Université de Liège; Bélgica Fil: Cambier, L.. Université de Liège; Bélgica Fil: Galleni, Lorena Alejandra. Université de Liège; Bélgica Fil: Mignon, María Belen. Université de Liège; Bélgica
description	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.
publishDate	2012
dc.date.none.fl_str_mv	2012-10
dc.type.none.fl_str_mv	info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo
format	article
status_str	publishedVersion
dc.identifier.none.fl_str_mv	http://hdl.handle.net/11336/105932 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 0378-1135 CONICET Digital CONICET
url	http://hdl.handle.net/11336/105932
identifier_str_mv	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 0378-1135 CONICET Digital CONICET
dc.language.none.fl_str_mv	eng
language	eng
dc.relation.none.fl_str_mv	info:eu-repo/semantics/altIdentifier/doi/10.1016/j.vetmic.2012.04.041 info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0378113512002908
dc.rights.none.fl_str_mv	info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv	openAccess
rights_invalid_str_mv	https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv	application/pdf application/pdf
dc.publisher.none.fl_str_mv	Elsevier Science
publisher.none.fl_str_mv	Elsevier Science
dc.source.none.fl_str_mv	reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str	CONICET Digital (CONICET)
collection	CONICET Digital (CONICET)
instname_str	Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv	CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv	dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score	12.952241

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...

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