Sporothrix brasiliensis Gp70 is a cell wall protein required for adhesion, proper interaction with innate immune cells, and virulence

Sporothrix brasiliensis is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently associated with epidemic outbreaks in Brazil. Despite the medical relevance of this species, little is known about its virul...

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Published inCell surface (Amsterdam) Vol. 13; p. 100139
Main Authors Padró-Villegas, Leonardo, Gómez-Gaviria, Manuela, Martínez-Duncker, Iván, López-Ramírez, Luz A., Martínez-Álvarez, José A., Niño-Vega, Gustavo A., Mora-Montes, Héctor M.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.06.2025
Elsevier
Subjects
Adhesin
Cell wall
Galleria mellonella
Glycosylation
Immune recognition
Phagocytosis
Research Paper
Virulence
Virulence
Immune recognition
Adhesin
Glycosylation
Galleria mellonella
Cell wall
Phagocytosis
Online AccessGet full text
ISSN2468-2330
2468-2330
DOI10.1016/j.tcsw.2024.100139

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Abstract Sporothrix brasiliensis is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently associated with epidemic outbreaks in Brazil. Despite the medical relevance of this species, little is known about its virulence factors, and most of the information on this subject is extrapolated from Sporothrix schenckii. Here, we generated S. brasiliensis mutants, where GP70 was silenced. In S. schenckii, this gene encodes a glycoprotein with adhesive properties required for virulence. The S. brasiliensis GP70 silencing led to an abnormal cellular phenotype, with smaller, round yeast-like cells that aggregate. Cell aggregation was disrupted with glucanase, suggesting this phenotype is linked to changes in the cell wall. The cell wall characterization confirmed changes in the structural polysaccharide β-1,3-glucan, which increased in quantity and exposure at the cell surface. This was accompanied by a reduction in protein content and N-linked glycans. Mutant strains with high GP70-silencing levels showed minimal levels of 3-carboxy-cis,cis-muconate cyclase activity, this glycoprotein's predicted enzyme function, and decreased ability to bind laminin and fibronectin. These phenotypical changes coincided with abnormal interaction with human peripheral blood mononuclear cells, where production of IL-1β, IL-17, and IL-22 was reduced and the strong dependence on cytokine stimulation via mannose receptor was lost. Phagocytosis by monocyte-derived macrophages was increased and virulence attenuated in a Galleria mellonella larvae. In conclusion, Gp70 is an abundant cell wall glycoprotein in S. brasiliensis that contributes to virulence and proper interaction with innate immnune cells. •Sporothrix brasiliensis GP70 encodes a cell wall and secreted protein.•The GP70 silencing affected cell morphology, generating smaller, rounded, and aggregated yeast-like cells.•The GP70-silenced mutants showed reduced adhesion to laminin and fibronectin, as well as trace levels of enzyme activity.•The GP70 silencing led to defects in the cell wall composition and organization.•Cells with low Gp70 levels were differentially recognized by human mononuclear cells and monocyte-derived macrophages.•The GP70-silenced mutants showed attenuation in virulence when interacting with Galleria mellonella larvae.
AbstractList is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently associated with epidemic outbreaks in Brazil. Despite the medical relevance of this species, little is known about its virulence factors, and most of the information on this subject is extrapolated from . Here, we generated mutants, where was silenced. In , this gene encodes a glycoprotein with adhesive properties required for virulence. The silencing led to an abnormal cellular phenotype, with smaller, round yeast-like cells that aggregate. Cell aggregation was disrupted with glucanase, suggesting this phenotype is linked to changes in the cell wall. The cell wall characterization confirmed changes in the structural polysaccharide β-1,3-glucan, which increased in quantity and exposure at the cell surface. This was accompanied by a reduction in protein content and -linked glycans. Mutant strains with high -silencing levels showed minimal levels of 3-carboxy-cis,cis-muconate cyclase activity, this glycoprotein's predicted enzyme function, and decreased ability to bind laminin and fibronectin. These phenotypical changes coincided with abnormal interaction with human peripheral blood mononuclear cells, where production of IL-1β, IL-17, and IL-22 was reduced and the strong dependence on cytokine stimulation mannose receptor was lost. Phagocytosis by monocyte-derived macrophages was increased and virulence attenuated in a larvae. In conclusion, Gp70 is an abundant cell wall glycoprotein in that contributes to virulence and proper interaction with innate immnune cells.
Sporothrix brasiliensis is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently associated with epidemic outbreaks in Brazil. Despite the medical relevance of this species, little is known about its virulence factors, and most of the information on this subject is extrapolated from Sporothrix schenckii. Here, we generated S. brasiliensis mutants, where GP70 was silenced. In S. schenckii, this gene encodes a glycoprotein with adhesive properties required for virulence. The S. brasiliensis GP70 silencing led to an abnormal cellular phenotype, with smaller, round yeast-like cells that aggregate. Cell aggregation was disrupted with glucanase, suggesting this phenotype is linked to changes in the cell wall. The cell wall characterization confirmed changes in the structural polysaccharide β-1,3-glucan, which increased in quantity and exposure at the cell surface. This was accompanied by a reduction in protein content and N-linked glycans. Mutant strains with high GP70-silencing levels showed minimal levels of 3-carboxy-cis,cis-muconate cyclase activity, this glycoprotein's predicted enzyme function, and decreased ability to bind laminin and fibronectin. These phenotypical changes coincided with abnormal interaction with human peripheral blood mononuclear cells, where production of IL-1β, IL-17, and IL-22 was reduced and the strong dependence on cytokine stimulation via mannose receptor was lost. Phagocytosis by monocyte-derived macrophages was increased and virulence attenuated in a Galleria mellonella larvae. In conclusion, Gp70 is an abundant cell wall glycoprotein in S. brasiliensis that contributes to virulence and proper interaction with innate immnune cells. •Sporothrix brasiliensis GP70 encodes a cell wall and secreted protein.•The GP70 silencing affected cell morphology, generating smaller, rounded, and aggregated yeast-like cells.•The GP70-silenced mutants showed reduced adhesion to laminin and fibronectin, as well as trace levels of enzyme activity.•The GP70 silencing led to defects in the cell wall composition and organization.•Cells with low Gp70 levels were differentially recognized by human mononuclear cells and monocyte-derived macrophages.•The GP70-silenced mutants showed attenuation in virulence when interacting with Galleria mellonella larvae.
Sporothrix brasiliensis is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently associated with epidemic outbreaks in Brazil. Despite the medical relevance of this species, little is known about its virulence factors, and most of the information on this subject is extrapolated from Sporothrix schenckii. Here, we generated S. brasiliensis mutants, where GP70 was silenced. In S. schenckii, this gene encodes a glycoprotein with adhesive properties required for virulence. The S. brasiliensis GP70 silencing led to an abnormal cellular phenotype, with smaller, round yeast-like cells that aggregate. Cell aggregation was disrupted with glucanase, suggesting this phenotype is linked to changes in the cell wall. The cell wall characterization confirmed changes in the structural polysaccharide β-1,3-glucan, which increased in quantity and exposure at the cell surface. This was accompanied by a reduction in protein content and N-linked glycans. Mutant strains with high GP70-silencing levels showed minimal levels of 3-carboxy-cis,cis-muconate cyclase activity, this glycoprotein's predicted enzyme function, and decreased ability to bind laminin and fibronectin. These phenotypical changes coincided with abnormal interaction with human peripheral blood mononuclear cells, where production of IL-1β, IL-17, and IL-22 was reduced and the strong dependence on cytokine stimulation via mannose receptor was lost. Phagocytosis by monocyte-derived macrophages was increased and virulence attenuated in a Galleria mellonella larvae. In conclusion, Gp70 is an abundant cell wall glycoprotein in S. brasiliensis that contributes to virulence and proper interaction with innate immnune cells.Sporothrix brasiliensis is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently associated with epidemic outbreaks in Brazil. Despite the medical relevance of this species, little is known about its virulence factors, and most of the information on this subject is extrapolated from Sporothrix schenckii. Here, we generated S. brasiliensis mutants, where GP70 was silenced. In S. schenckii, this gene encodes a glycoprotein with adhesive properties required for virulence. The S. brasiliensis GP70 silencing led to an abnormal cellular phenotype, with smaller, round yeast-like cells that aggregate. Cell aggregation was disrupted with glucanase, suggesting this phenotype is linked to changes in the cell wall. The cell wall characterization confirmed changes in the structural polysaccharide β-1,3-glucan, which increased in quantity and exposure at the cell surface. This was accompanied by a reduction in protein content and N-linked glycans. Mutant strains with high GP70-silencing levels showed minimal levels of 3-carboxy-cis,cis-muconate cyclase activity, this glycoprotein's predicted enzyme function, and decreased ability to bind laminin and fibronectin. These phenotypical changes coincided with abnormal interaction with human peripheral blood mononuclear cells, where production of IL-1β, IL-17, and IL-22 was reduced and the strong dependence on cytokine stimulation via mannose receptor was lost. Phagocytosis by monocyte-derived macrophages was increased and virulence attenuated in a Galleria mellonella larvae. In conclusion, Gp70 is an abundant cell wall glycoprotein in S. brasiliensis that contributes to virulence and proper interaction with innate immnune cells.
Sporothrix brasiliensis is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently associated with epidemic outbreaks in Brazil. Despite the medical relevance of this species, little is known about its virulence factors, and most of the information on this subject is extrapolated from Sporothrix schenckii . Here, we generated S. brasiliensis mutants, where GP70 was silenced. In S. schenckii , this gene encodes a glycoprotein with adhesive properties required for virulence. The S. brasiliensis GP70 silencing led to an abnormal cellular phenotype, with smaller, round yeast-like cells that aggregate. Cell aggregation was disrupted with glucanase, suggesting this phenotype is linked to changes in the cell wall. The cell wall characterization confirmed changes in the structural polysaccharide β-1,3-glucan, which increased in quantity and exposure at the cell surface. This was accompanied by a reduction in protein content and N -linked glycans. Mutant strains with high GP70 -silencing levels showed minimal levels of 3-carboxy-cis,cis-muconate cyclase activity, this glycoprotein's predicted enzyme function, and decreased ability to bind laminin and fibronectin. These phenotypical changes coincided with abnormal interaction with human peripheral blood mononuclear cells, where production of IL-1β, IL-17, and IL-22 was reduced and the strong dependence on cytokine stimulation via mannose receptor was lost. Phagocytosis by monocyte-derived macrophages was increased and virulence attenuated in a Galleria mellonella larvae. In conclusion, Gp70 is an abundant cell wall glycoprotein in S. brasiliensis that contributes to virulence and proper interaction with innate immnune cells. • Sporothrix brasiliensis GP70 encodes a cell wall and secreted protein. • The GP70 silencing affected cell morphology, generating smaller, rounded, and aggregated yeast-like cells. • The GP70 -silenced mutants showed reduced adhesion to laminin and fibronectin, as well as trace levels of enzyme activity. • The GP70 silencing led to defects in the cell wall composition and organization. • Cells with low Gp70 levels were differentially recognized by human mononuclear cells and monocyte-derived macrophages. • The GP70 -silenced mutants showed attenuation in virulence when interacting with Galleria mellonella larvae.
Sporothrix brasiliensis is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently associated with epidemic outbreaks in Brazil. Despite the medical relevance of this species, little is known about its virulence factors, and most of the information on this subject is extrapolated from Sporothrix schenckii. Here, we generated S. brasiliensis mutants, where GP70 was silenced. In S. schenckii, this gene encodes a glycoprotein with adhesive properties required for virulence. The S. brasiliensis GP70 silencing led to an abnormal cellular phenotype, with smaller, round yeast-like cells that aggregate. Cell aggregation was disrupted with glucanase, suggesting this phenotype is linked to changes in the cell wall. The cell wall characterization confirmed changes in the structural polysaccharide β-1,3-glucan, which increased in quantity and exposure at the cell surface. This was accompanied by a reduction in protein content and N-linked glycans. Mutant strains with high GP70-silencing levels showed minimal levels of 3-carboxy-cis,cis-muconate cyclase activity, this glycoprotein's predicted enzyme function, and decreased ability to bind laminin and fibronectin. These phenotypical changes coincided with abnormal interaction with human peripheral blood mononuclear cells, where production of IL-1β, IL-17, and IL-22 was reduced and the strong dependence on cytokine stimulation via mannose receptor was lost. Phagocytosis by monocyte-derived macrophages was increased and virulence attenuated in a Galleria mellonella larvae. In conclusion, Gp70 is an abundant cell wall glycoprotein in S. brasiliensis that contributes to virulence and proper interaction with innate immnune cells.
ArticleNumber 100139
Author Mora-Montes, Héctor M.
López-Ramírez, Luz A.
Niño-Vega, Gustavo A.
Martínez-Álvarez, José A.
Padró-Villegas, Leonardo
Martínez-Duncker, Iván
Gómez-Gaviria, Manuela
Author_xml – sequence: 1
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  surname: Gómez-Gaviria
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  fullname: López-Ramírez, Luz A.
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  organization: Departamento de Biología, División de Ciencias Naturales y Exactas, Campus Guanajuato, Universidad de Guanajuato, Noria Alta s/n, col. Noria Alta, C.P. 36050 Guanajuato, Gto, Mexico
– sequence: 5
  givenname: José A.
  surname: Martínez-Álvarez
  fullname: Martínez-Álvarez, José A.
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  organization: Departamento de Biología, División de Ciencias Naturales y Exactas, Campus Guanajuato, Universidad de Guanajuato, Noria Alta s/n, col. Noria Alta, C.P. 36050 Guanajuato, Gto, Mexico
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  email: gustavo.nino@ugto.mx
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  givenname: Héctor M.
  surname: Mora-Montes
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Keywords Virulence
Immune recognition
Adhesin
Glycosylation
Galleria mellonella
Cell wall
Phagocytosis
Language English
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2025 The Authors.
This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
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Snippet Sporothrix brasiliensis is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism...
is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently...
Sporothrix brasiliensis is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism...
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StartPage 100139
SubjectTerms Adhesin
Cell wall
Galleria mellonella
Glycosylation
Immune recognition
Phagocytosis
Research Paper
Virulence
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Title Sporothrix brasiliensis Gp70 is a cell wall protein required for adhesion, proper interaction with innate immune cells, and virulence
URI https://dx.doi.org/10.1016/j.tcsw.2024.100139
https://www.ncbi.nlm.nih.gov/pubmed/39866864
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