Ana Gil de Bona

Ana Gil de Bona
The Forsyth Institute

PhD

About

13
Publications
2,231
Reads
How we measure 'reads'
A 'read' is counted each time someone views a publication summary (such as the title, abstract, and list of authors), clicks on a figure, or views or downloads the full-text. Learn more
259
Citations
Introduction
Dr. Ana Gil de Bona received her PhD in Microbiology and Proteomics from Complutense University of Madrid (Spain) in 2016. Her research mainly focused on the study of the proteomic profile of the extracellular vesicles and the secretome in a virulent strain of Candida albicans. After receiving her PhD, she was a postdoctoral associate at the University of Massachusetts Medical School working in yeast genetics and proteomics. Dr. Gil de Bona is currently a postdoctoral fellow in Dr. Felicitas Bidlack lab at the Forsyth Institute. Her research focuses on understanding how the enamel development and protein matrix composition are affected by the oral environment in healthy and defective teeth.
Additional affiliations
February 2019 - present
The Forsyth Institute
Position
  • PostDoc Position
June 2016 - February 2019
University of Massachusetts Medical School
Position
  • PostDoc Position
February 2016 - April 2016
Complutense University of Madrid
Position
  • PostDoc Position
Education
October 2010 - July 2011
Complutense University of Madrid
Field of study
  • Microbiology
September 2010 - February 2016
Complutense University of Madrid
Field of study
  • Molecular Biology and Microbiology
October 2009 - July 2010
Universidad de Sevilla
Field of study
  • Biotechnology and Microbiology

Publications

Publications (13)
Article
Full-text available
Bone biomineralization is a complex process in which type I collagen and associated non-collagenous proteins (NCPs), including glycoproteins and proteoglycans, interact closely with inorganic calcium and phosphate ions to control the precipitation of nanosized, non-stoichiometric hydroxyapatite (HAP, idealized stoichiometry Ca10(PO4)6(OH)2) within...
Article
Full-text available
Tooth enamel is the outer covering of tooth crowns, the hardest material in the mammalian body, yet fracture resistant. The extremely high content of 95 wt% calcium phosphate in healthy adult teeth is achieved through mineralization of a proteinaceous matrix that changes in abundance and composition. Enamel-specific proteins and proteases are known...
Poster
Full-text available
Background: In mammals, tooth crown formation completes before eruption, but enamel can harden or decay after eruption with saliva playing a critical role in these processes. However, the role of salivary proteases and peptides in post-eruptive enamel hardening is unresolved. The mechanism of enamel formation is highly conserved in mammals, althoug...
Article
Biological significance: Candida albicans extracellular proteins are involved in biofilm formation, cell nutrient acquisition and cell wall integrity maintenance. Furthermore, these proteins include virulence factors and immunogenic proteins. This review is of outstanding interest, not only because it extends knowledge of the C. albicans surface a...
Article
Macrophages may induce fungal apoptosis to fight against C. albicans , as previously hypothesized by our group. To confirm this hypothesis, proteins from C. albicans cells after 3h of interaction with macrophages were analyzed using two quantitative proteomic approaches. Fifty-one and 97 proteins were identified as differentially expressed by DIGE...
Thesis
Introduction: Candida albicans is a commensal fungus in humans which causes different infections ranging from superficial to systemic. Invasive candidiasis is an important cause of disease and mortality in immunocompromised patients. The ability to switch from yeast to hypha growth is essential for virulence in C. albicans which express distinct ce...
Article
Full-text available
Ecm33 is a glycosylphosphatidylinositol (GPI)-anchored protein in the human pathogen Candida albicans. This protein is known to be involved in fungal cell wall integrity and is also critical for normal virulence in the mouse model of hematogenously disseminated candidiasis, but its function remains unknown. In this work, several phenotypic analyses...
Article
Candida albicans secretes numerous proteins related to cell wall remodeling, adhesion, nutrient acquisition and host interactions. Also, extracellular vesicles containing cytoplasmic proteins are secreted into the medium. The C. albicans ecm33/ecm33 mutant (RML2U) presents an altered cell wall and is avirulent. The proteomic analysis of secreted pr...
Article
The ability to switch from yeast to hyphal growth is essential for virulence in Candida albicans. The cell surface is the initial point of contact between the fungus and the host. In this work, a free-gel proteomic strategy based on tryptic digestion of live yeast and hyphae cells and protein identification using LC-MS/MS methodology was used to id...
Article
The commensal fungus Candida albicans secretes a considerable number of proteins and, as in different fungal pathogens, extracellular vesicles (EVs) have also been observed. Our report contains the first proteomic analysis of EVs in C. albicans and a comparative proteomic study of the soluble secreted proteins. With this purpose, cell-free culture...
Presentation
Introduction and Objectives Candida albicans is a commensal fungus in healthy humans and may cause different type of infection mainly in immunocompromised patients. C. albicans secretes a considerable number of proteins involved in different processes. However, predicted cytosolic proteins have been detected in the extracellular medium of C. albica...

Questions

Questions (2)
Question
I am trying to find the best way to measure:
1. the peptide concentration from my peptidome straight from the initial body solution (after being separated from the whole proteome),
2. and the peptide concentration after using the C18 tips and before the MS analysis.
I want to be sure that the peptide concentration is adequate. Ideally I also would like to know the quality of the samples, to avoid any kind of contamination in the MS analysis.
I have been using Bradford assay for previous proteomics samples. I know that the BCA assay is highly recommended for proteomics and it can be used for peptide concentration. However, I have found a colorimetric assay in Thermo for peptide quantification ( Pierce™ Quantitative Colorimetric Peptide Assay). I am also studying the proteome from the same fluid. I want to minimize the amount of kits to use for protein and peptide quantification. If BCA assay could be used for protein and peptide quantification before and after trypsinization and C18 tips would be great.
Any recommendation?
Question
I am working with an initial volume of 20 mL* and using a 10 kDa filter to separate proteins from peptides. With this filter I am able to concentrate the proteins upstream of the membrane. However, I have still the peptides that I am interested in analyzing by Mass Spect in the filtrate (around 20 mL). I am thinking on the possibility to use another 1 kDa filter to concentrate them (it is the smallest I've found), but I am worried to lose some of the peptides with low MW. Any recommendation?
*The extraction buffer includes urea.

Network

Cited By

Projects

Projects (2)
Project
Understand the enamel development and saliva composition from the Proteomics perspective
Project
Member of the Benanti Lab in the Molecular, Cell and Cancer Biology Department at UMass Medical School. My project as postdoctoral associate is focus on the regulation of chromosome structure during the cell cycle. How condensin complexes are regulated throughout the cell cycle in Saccharomyces cerevisiae.