Julian Fernández

Dr. Julian Fernández


Research Focus & Metrics

Academic Career Length

11Years (2016-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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29 September 2022 in Journal of Fungi
Verified
Journal Article
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PAPamela Alfaro-Vargas
Pamela Alfaro-Vargas
ABAlisson Bastos-Salas
Alisson Bastos-Salas
RMrodrigo muñoz
rodrigo muñoz
RPReinaldo Pereira-Reyes
Reinaldo Pereira-Reyes
MRMauricio Redondo
Mauricio Redondo
José Pablo López-GómezJosé Pablo López-Gómez
José Pablo López-Gómez
Peptaibols (Paib), are a class of biologically active peptides isolated from soil, fungi and molds, which have interesting properties as antimicrobial agents. Paib production was optimized in flasks by adding sucrose as a carbon source, 2-aminoisobutyric acid (Aib) as an additive amino acid, and F. oxysporum cell debris as an elicitor. Paib were purified, sequenced and identified by High-performance liquid chromatography (HPLC)coupled to mass spectrometry. Afterward, a Paib extract was obtained from the optimized fermentations. The biological activity of these extracts was evaluated using in vitro and in vivo methods. The extract inhibited the growth of specific plant pathogens, and it showed inhibition rates similar to those from commercially available fungicides. Growth inhibition rates were 92.2, 74.2, 58.4 and 36.2% against Colletotrichum gloeosporioides, Botrytis cinerea, Alternaria alternata and Fusarium oxysporum, respectively. Furthermore, the antifungal activity was tested in tomatoes inoculated with A. alternata, the incidence of the disease in tomatoes treated with the extract was 0%, while the untreated fruit showed a 92.5% incidence of infection Scanning electron microscopy images showed structural differences between the fungi treated with or without Paib. The most visual alterations were sunk and shriveled morphology in spores, while the hyphae appeared to be fractured, rough and dehydrated.

30 September 2021 in Scientific Reports
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Journal Article
Open access
PDF file
ALAlfredo Jesús López-Dávila
Alfredo Jesús López-Dávila
NWNatalie Weber
Natalie Weber
TKTheresia Kraft
Theresia Kraft
FMFaramarz Matinmehr
Faramarz Matinmehr
MAMariela Arias-Hidalgo
Mariela Arias-Hidalgo
José María GutiérrezJosé María Gutiérrez
José María Gutiérrez
Viperid snake venoms contain a unique family of cytotoxic proteins, the Lys49 PLA2 homologs, which are devoid of enzymatic activity but disrupt the integrity of cell membranes. They are known to induce skeletal muscle damage and are therefore named ‘myotoxins’. Single intact and skinned (devoid of membranes and cytoplasm but with intact sarcomeric proteins) rat cardiomyocytes were used to analyze the cytotoxic action of a myotoxin, from the venom of Bothrops asper. The toxin induced rapid hypercontraction of intact cardiomyocytes, associated with an increase in the cytosolic concentration of calcium and with cell membrane disruption. Hypercontraction of intact cardiomyocytes was abrogated by the myosin inhibitor para-aminoblebbistatin (AmBleb). No toxin-induced changes of key parameters of force development were observed in skinned cardiomyocytes. Thus, although myosin is a key effector of the observed hypercontraction, a direct effect of the toxin on the sarcomeric proteins -including the actomyosin complex- is not part of the mechanism of cytotoxicity. Owing to the sensitivity of intact cardiomyocytes to the cytotoxic action of myotoxin, this ex vivo model is a valuable tool to explore in further detail the mechanism of action of this group of snake venom toxins.

1 April 2019 in Journal of Proteomics
Verified
Journal Article
Closed access
ELEnikő Lippa
Enikő Lippa
FTFerenc Török
Ferenc Török
AGAarón Gómez
Aarón Gómez
GCGreivin Corrales
Greivin Corrales
DCDanilo Chacón
Danilo Chacón
JFJulian Fernández
Julian Fernández


1 July 2021 in Toxicon
Verified
Journal Article
Closed access
SVSofía Vargas-Valerio
Sofía Vargas-Valerio
JRJoby Robleto
Joby Robleto
SCStephanie Chaves-Araya
Stephanie Chaves-Araya
LMLaura Monturiol-Gross
Laura Monturiol-Gross
Bruno LomonteBruno Lomonte
Bruno Lomonte
JFJulian Fernández
Julian Fernández

12 February 2022 in Toxicon: X
Verified
Journal Article
Open access
GMGianni Mena
Gianni Mena
SCStephanie Chaves-Araya
Stephanie Chaves-Araya
JCJohelen Chacón
Johelen Chacón
ETEnikő Török
Enikő Török
FTFerenc Török
Ferenc Török
JFJulian Fernández
Julian Fernández
Coralsnakes belong to the family Elapidae and possess venoms which are lethal to humans and can be grouped based on the predominance of either three finger toxins (3FTxs) or phospholipases A2 (PLA2s). A proteomic and toxicological analysis of the venom of the coralsnake Micrurus yatesi was performed. This species, distributed in southeastern Costa Rica, was formerly considered a subspecies of M. alleni. Results showed that this venom is PLA2-rich, in contrast with the previously studied venom of Micrurus alleni. Toxicological evaluation of the venom, in accordance with proteomic data, revealed that it has a markedly higher in vitro PLA2 activity upon a synthetic substrate than M. alleni. The evaluation of in vivo myotoxicity in CD-1 mice using histological evaluation and plasma creatine kinase release also showed that M. yatesi venom caused muscle damage. A commercial equine antivenom prepared using the venom of Micrurus nigrocinctus displayed a similar recognition of the venoms of M. yatesi and M. nigrocinctus by enzyme immunoassay. This antivenom also immunorecognized the main fractions of the venom of M. yatesi and was able to neutralize its lethal effect in a murine model.