Proteomic Analysis Revealed that DVL, a Lectin Purified from <i>Dioclea violacea</i> Seeds, Induced a Change in the Protein Profile of <i>Candida albicans</i>

<i>Candida albicans</i> is an important opportunistic fungal pathogen, and its resistance to conventional treatments poses a substantial challenge. Previous research by our group demonstrated that the anticandidal activity of <i>Dioclea violacea</i> seed lectin (DVL) involves multiple mechanisms of action. Our current objective is to analyze changes in the proteome of <i>C. albicans</i> cells after treatment with the DVL lectin. The proteomic analysis corroborated the previously observed mechanisms with greater specificity, encompassing processes such as cell wall integrity, expression of transport proteins, proteins related to metabolism and energy, DNA repair proteins, and proteins related to defense and stress, and downregulated cell cycle proteins affecting cell viability. Our findings provide novel insights into <i>C. albicans</i> response to DVL lectin, emphasizing the intricate cellular mechanisms underlying stress adaptation. These results provided new insight into the mechanisms of action of DVL against <i>C. albicans</i>. They may facilitate the development of more effective and innovative antifungal therapies by providing a comprehensive understanding of fungal pathogenesis.

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Publication Details

Journal
ACS Omega
Published
2025-08-29
DOI
https://doi.org/10.1021/acsomega.5c04868
Citations
1
Primary Topic
Antifungal resistance and susceptibility
Type
article
Field-Weighted Citation Impact
1.40

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article

Proteomic Analysis Revealed that DVL, a Lectin Purified from Dioclea violacea Seeds, Induced a Change in the Protein Profile of Candida albicans

Rômulo Farias Carneiro, Celso Shiniti Nagano, Maria H.C. Santos, Claudener Souza Teixeira et al.
1 citations
ACS Omega
Antifungal resistance and susceptibility
1.40
article

Proteomic Analysis Revealed that DVL, a Lectin Purified from Dioclea violacea Seeds, Induced a Change in the Protein Profile of Candida albicans

Rômulo Farias Carneiro, Celso Shiniti Nagano, Maria H.C. Santos, Claudener Souza Teixeira, Cleverson D. T. Freitas, Romério Rodrigues dos Santos Silva, Felipe Pantoja Mesquita, Pedro Filho Noronha Souza, Ana L.E. Santos
article en
1 citations

Abstract

<i>Candida albicans</i> is an important opportunistic fungal pathogen, and its resistance to conventional treatments poses a substantial challenge. Previous research by our group demonstrated that the anticandidal activity of <i>Dioclea violacea</i> seed lectin (DVL) involves multiple mechanisms of action. Our current objective is to analyze changes in the proteome of <i>C. albicans</i> cells after treatment with the DVL lectin. The proteomic analysis corroborated the previously observed mechanisms with greater specificity, encompassing processes such as cell wall integrity, expression of transport proteins, proteins related to metabolism and energy, DNA repair proteins, and proteins related to defense and stress, and downregulated cell cycle proteins affecting cell viability. Our findings provide novel insights into <i>C. albicans</i> response to DVL lectin, emphasizing the intricate cellular mechanisms underlying stress adaptation. These results provided new insight into the mechanisms of action of DVL against <i>C. albicans</i>. They may facilitate the development of more effective and innovative antifungal therapies by providing a comprehensive understanding of fungal pathogenesis.

ACS OmegaVol. 10(35)
Universidade Federal do Ceará (BR), Cebu Technological University (PH), Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico (BR), Universidade Federal do Cariri (BR), PharmacoGenetics (China) (CN), Health and Human Development (2HD) Research Network (CM), National Institute of Science and Technology (ID)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Conselho Nacional de Desenvolvimento Científico e Tecnológico, Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico
Openalex Percentile: Top 17%
Antifungal resistance and susceptibility
1.40
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