Mario González Carracedo

Mario González Carracedo
Universidad de La Laguna | ULL · Department of Biochemistry and Molecular Biology

Biology
Teaching and research about conservation genetics and biomedicine.

About

28
Publications
2,543
Reads
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233
Citations
Additional affiliations
October 2019 - present
Universidad de La Laguna
Position
  • Professor (Assistant)
October 2017 - October 2019
Universidad de La Laguna
Position
  • Laboratory Manager
June 2015 - October 2017
Universidad de La Laguna
Position
  • PostDoc Position
Description
  • Molecular Biology of phytopatogenic fungi and plant innmune response.

Publications

Publications (28)
Conference Paper
Full-text available
Introduction: The human microbiome of different body sites is related to asthma exacerbations, which are the major contributor to the global asthma burden. However, no study so far has investigated the role of the salivary microbiome in asthma exacerbations. Aims and objectives: To study whether changes in the salivary microbiome are associated wit...
Article
Banana cultivars of agronomic interest have been genetically characterized using two different molecular markers. On the one hand, a panel of 14 trinucleotide single sequence repeats (SSRs or microsatellites) was optimized for homogeneous PCR conditions. It was tested with 50 individuals from seven cultivars, yielding 76 alleles and 5.4 ± 1.8 allel...
Article
Full-text available
Asthma is a heterogeneous and multifactorial respiratory disease with an important impact on childhood. Difficult-to-treat asthma is not uncommon among children, and it causes a high burden to the patient, caregivers, and society. This review aims to summarize the recent findings on pediatric asthma treatment response revealed by different omic app...
Article
BcIEB is a small protein secreted by the phytopathogenic fungus Botrytis cinerea that acts as a PAMP in plants. This activity is mapped to a 35‐amino acid highly conserved region, the peptide ieb35. Moreover, it has been shown that the protein and the peptide induce systemic resistance to B. cinerea after their infiltration into tobacco leaves. In...
Article
Full-text available
Plants activate defense responses against a possible pathogen once pattern-recognition receptors (PRRs) perceive the presence of pathogen-associated molecular patterns (PAMPs). Glycosyl hydrolase family 11 (GH11) endoxylanases from Trichoderma, Fusarium and Botrytis species have been described as being able to induce the defense response in plants,...
Article
Full-text available
Heterologous protein expression in yeast, mostly in Saccharomyces cerevisiae and Pichia pastoris, is a well‐established and widely used technique. It typically requires the construction of an expression vector in Escherichia coli containing the foreign gene and its subsequent transformation into yeast. Although simple, this procedure has important...
Article
Full-text available
The endo-β-1,4-xylanase BcXyn11A is one of several plant cell-wall degrading enzymes that the phytopathogenic fungus Botrytis cinerea secretes during interaction with its hosts. In addition to its enzymatic activity, this protein also acts as an elicitor of the defense response in plants and has been identified as a virulence factor. In the present...
Article
The broad-range phytopathogenic fungus Botrytis cinerea secretes hundreds of proteins during infection of its plant hosts. One of these proteins, BcIEB1, is abundantly secreted and is able to elicit plant defenses, probably as a pathogen-associated molecular pattern, although its native function in B. cinerea biology remains unknown. Pull-down expe...
Article
Full-text available
BcSUN1 is a glycoprotein secreted by Botrytis cinerea, an important plant pathogen that causes severe losses in agriculture worldwide. In this work, the role of BcSUN1 in different aspects of the B. cinerea biology was studied by phenotypic analysis of Bcsun1 knockout strains. We identified BcSUN1 as the only member of the Group-I SUN family of pro...
Article
BcIEB1 is a very abundant protein in the secretome of _Botrytis cinerea_ but it has no known function and no similarity to any characterized protein family. Previous results suggested that this protein is an elicitor of the plant defense system. In this work we have generated loss-of-function _B. cinerea_ mutants lacking BcIEB1 and we have expresse...
Article
Full-text available
Background Botrytis cinerea secretes a high number of proteins that are predicted to have numerous O-glycosylation sites, frequently grouped in highly O-glycosylated regions, and analysis of mutants affected in O-glycosylation has shown, in B. cinerea and in other phytopathogenic fungi, that this process is important for fungal biology and virulenc...
Article
The generation of knock-out mutants in fungal pathogens by gene replacement and insertional mutagenesis is the classical method to validate virulence factors. An alternative strategy consists of silencing the candidate virulence gene by making use of the phenomenon of RNA interference (RNAi), adding features such as the possibility of generating kn...
Article
Cerato-platanin family proteins are secreted and have been found both in the fungal cell wall and in the extracellular medium. They elicit defence responses in a variety of plants and have been proposed to be perceived as PAMPs by the plant immune system, although in the case of the necrotroph Botrytis cinerea the cerato-platanin BcSpl1 contributes...
Article
Full-text available
Protein O-glycosylation is crucial in determining the structure and function of numerous secreted and membrane-bound proteins. In fungi, this process begins with the addition of a mannose residue by protein O-mannosyltransferases (PMTs) in the lumen side of the ER membrane. We have generated mutants of the three Botrytis cinerea pmt genes to study...
Data
Alignment of fungal PMTs. Proteins were aligned by PRALINE, making use of the transmembrane regions predicted by PHOBIUS (on green background). The regions homologous to the 7 experimentally-determined transmembrane domains of S. cerevisiae Pmt1p are marked with roman numerals. Question marks indicate that it is not clear which region is the last t...
Data
Partial degradation of the extracellular matrix by treatment with proteinase K. Mycelia were grown in liquid YGG medium without shaking, transferred to 0.5X phosphate buffer saline and incubated with 0.4 mg ml−1 proteinase K for 4 hours before staining with India ink. Controls received no proteinase K. (TIF)
Data
Full-text available
Protein sequences used in this work. Protein sequences used in the comparative studies displayed in Figures 1 and S2. (PDF)
Data
Putative topology of B. cinerea PMTs. The hydrophobicity of each BcPMT (thick line), calculated with the Kyte-Doolittle scale and a window of 15 residues, is plotted alongside the average hydrophobicity of the corresponding PMT subfamily (thin line) derived from the alignment (Figure S2). Black lines below plot indicate the transmembrane regions pr...
Data
Full-text available
Oligonucleotides used in this study. (PDF)
Data
Generation of the three bcpmt knockout mutants. A) Strategy used to generate the three Δbcpmts knock-out mutants. The DNA constructs used in the transformation, shown below each bcpmt gene, contain the hygromycin resistance cassette (Hyg-R) flanked by two regions of the target gene. The position of all primers used to generate the constructs and to...
Article
Full-text available
Background O-glycosylation of secretory proteins has been found to be an important factor in fungal biology and virulence. It consists in the addition of short glycosidic chains to Ser or Thr residues in the protein backbone via O-glycosidic bonds. Secretory proteins in fungi frequently display Ser/Thr rich regions that could be sites of extensive...
Data
Microsoft Excel spreadsheet with the macro XRR used in the search for Ser/Thr-rich regions and pHGRs (predicted Hyper- O -glycosylated Regions).
Data
List of SignalP-positive proteins for the eight fungal genomes with the O -glycosylation sites predicted by NetOGlyc.
Data
Comparison of experimental O-glycosylation sites found in fungal proteins with those predicted by NetOGlyc 3.1 (http://www.cbs.dtu.dk/services/NetOGlyc/).
Data
Full-text available
Results of the search for pHGRs (predicted Hyper- O -glycosylated Regions) in the SignalP-positive proteins coded by the eight fungal genomes.

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