Functional analysis of Paracoccidioides brasiliensis 14-3-3 adhesin expressed in Saccharomyces cerevisiae
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Updated: Aug 26, 2026
Assay for Adhesion and Agar Invasion in S. cerevisiae
Published on: November 8, 2006
Patricia Akemi Assato1, Julhiany de Fátima da Silva2, Haroldo Cesar de Oliveira3
1Laboratório de Micologia Clínica - Núcleo de Proteômica - Faculdade de Ciências Farmacêuticas- Unesp - Campus Araraquara, Rodovia Araraquara - Jaú Km 1, 14801-902, Araraquara, SP, Brazil. patricia.assato@gmail.com.
Background:
14-3-3 proteins comprise a family of eukaryotic multifunctional proteins involved in several cellular processes. The Pb14-3-3 of Paracoccidioides brasiliensis seems to play an important role in the Paracoccidioides-host interaction. Paracoccidioides brasiliensis is an etiological agent of paracoccidioidomycosis, which is a systemic mycosis that is endemic in Latin America. In the initial steps of the infection, Paracoccidioides spp. synthetizes adhesins that allow it to adhere and invade host cells. Therefore, the aim of this work was to perform a functional analysis of Pb14-3-3 using Saccharomyces cerevisiae as a model.
Results:
The functional analysis of Pb14-3-3 was performed in S. cerevisiae, and it was found that Pb14-3-3 partially complemented S. cerevisiae proteins Bmh1p and Bmh2p, which are recognized as two yeast 14-3-3 homologues. When we evaluated the adhesion profile of S. cerevisiae transformants, Pb14-3-3 acted as an adhesin in S. cerevisiae; however, Bmh1p did not show this function. The influence of Pb14-3-3 in S. cerevisiae ergosterol pathway was also evaluated and our results showed that Pb14-3-3 up-regulates genes involved in ergosterol biosynthesis.
Conclusions:
Our data showed that Pb14-3-3 was able to partially complement Bmh1p and Bmh2p proteins in S. cerevisiae; however, we suggest that Pb14-3-3 has a differential role as an adhesin. In addition, Pb-14-3-3 may be involved in Paracoccidioides spp. ergosterol biosynthesis which makes it an interest as a therapeutic target.
Insights
The Paracoccidioides brasiliensis 14-3-3 protein (Pb14-3-3) functions as an adhesin in yeast and up-regulates ergosterol biosynthesis. This protein shows potential as a therapeutic target for paracoccidioidomycosis.
Area of Science:
- Mycology
- Molecular Biology
- Biochemistry
Background:
- 14-3-3 proteins are crucial eukaryotic multifunctional proteins involved in various cellular processes.
- The Pb14-3-3 protein from Paracoccidioides brasiliensis is implicated in host-pathogen interactions during paracoccidioidomycosis, a systemic mycosis prevalent in Latin America.
- Adhesins synthesized by Paracoccidioides spp. facilitate host cell adherence and invasion during early infection stages.
Purpose of the Study:
- To conduct a functional analysis of the Pb14-3-3 protein from Paracoccidioides brasiliensis.
- To investigate the role of Pb14-3-3 in host cell adhesion and invasion.
- To explore the involvement of Pb14-3-3 in the ergosterol biosynthesis pathway.
Main Methods:
- Functional analysis of Pb14-3-3 using Saccharomyces cerevisiae as a model organism.
- Complementation assays with S. cerevisiae 14-3-3 homologues (Bmh1p and Bmh2p).
- Evaluation of the adhesion profile of S. cerevisiae transformants expressing Pb14-3-3.
- Assessment of Pb14-3-3's influence on the ergosterol pathway in S. cerevisiae.
Main Results:
- Pb14-3-3 partially complemented the functions of Bmh1p and Bmh2p in S. cerevisiae.
- Pb14-3-3 demonstrated adhesive properties in S. cerevisiae, a function not observed with Bmh1p.
- Pb14-3-3 was found to up-regulate genes involved in ergosterol biosynthesis in S. cerevisiae.
Conclusions:
- Pb14-3-3 can partially substitute for yeast 14-3-3 proteins but exhibits distinct adhesive functions.
- Pb14-3-3 may play a role in the ergosterol biosynthesis of Paracoccidioides spp.
- Pb14-3-3 presents a potential therapeutic target for treating paracoccidioidomycosis.
