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  1. Article ; Online: A Common Polymorphism in

    Anguita, Raul / Prats-Ejarque, Guillem / Moussaoui, Mohammed / Becknell, Brian / Boix, Ester

    International journal of molecular sciences

    2024  Volume 25, Issue 1

    Abstract: Human Ribonuclease (RNase) 6 is a monocyte and macrophage-derived protein with potent antimicrobial activity toward uropathogenic bacteria. ... ...

    Abstract Human Ribonuclease (RNase) 6 is a monocyte and macrophage-derived protein with potent antimicrobial activity toward uropathogenic bacteria. The
    MeSH term(s) Humans ; Uropathogenic Escherichia coli/genetics ; Polymorphism, Single Nucleotide ; Alleles ; Ribonucleases ; Anti-Infective Agents
    Chemical Substances Ribonucleases (EC 3.1.-) ; Anti-Infective Agents
    Language English
    Publishing date 2024-01-03
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms25010604
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Host Defence RNases as Antiviral Agents against Enveloped Single Stranded RNA Viruses.

    Li, Jiarui / Boix, Ester

    Virulence

    2021  Volume 12, Issue 1, Page(s) 444–469

    Abstract: Owing to the recent outbreak of Coronavirus Disease of 2019 (COVID-19), it is urgent to develop effective and safe drugs to treat the present pandemic and prevent other viral infections that might come in the future. Proteins from our own innate immune ... ...

    Abstract Owing to the recent outbreak of Coronavirus Disease of 2019 (COVID-19), it is urgent to develop effective and safe drugs to treat the present pandemic and prevent other viral infections that might come in the future. Proteins from our own innate immune system can serve as ideal sources of novel drug candidates thanks to their safety and immune regulation versatility. Some host defense RNases equipped with antiviral activity have been reported over time. Here, we try to summarize the currently available information on human RNases that can target viral pathogens, with special focus on enveloped single-stranded RNA (ssRNA) viruses. Overall, host RNases can fight viruses by a combined multifaceted strategy, including the enzymatic target of the viral genome, recognition of virus unique patterns, immune modulation, control of stress granule formation, and induction of autophagy/apoptosis pathways. The review also includes a detailed description of representative enveloped ssRNA viruses and their strategies to interact with the host and evade immune recognition. For comparative purposes, we also provide an exhaustive revision of the currently approved or experimental antiviral drugs. Finally, we sum up the current perspectives of drug development to achieve successful eradication of viral infections.
    MeSH term(s) Endoribonucleases/metabolism ; Eosinophils/metabolism ; Humans ; Pathogen-Associated Molecular Pattern Molecules/metabolism ; RNA, Viral/metabolism ; Ribonuclease, Pancreatic/metabolism ; SARS-CoV-2/drug effects ; SARS-CoV-2/immunology ; Virus Replication/physiology ; COVID-19 Drug Treatment
    Chemical Substances Pathogen-Associated Molecular Pattern Molecules ; RNA, Viral ; Endoribonucleases (EC 3.1.-) ; 2-5A-dependent ribonuclease (EC 3.1.26.-) ; Ribonuclease, Pancreatic (EC 3.1.27.5)
    Language English
    Publishing date 2021-03-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2657572-3
    ISSN 2150-5608 ; 2150-5594
    ISSN (online) 2150-5608
    ISSN 2150-5594
    DOI 10.1080/21505594.2021.1871823
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: A Common Polymorphism in RNASE6 Impacts Its Antimicrobial Activity toward Uropathogenic Escherichia coli

    Raul Anguita / Guillem Prats-Ejarque / Mohammed Moussaoui / Brian Becknell / Ester Boix

    International Journal of Molecular Sciences, Vol 25, Iss 1, p

    2024  Volume 604

    Abstract: Human Ribonuclease (RNase) 6 is a monocyte and macrophage-derived protein with potent antimicrobial activity toward uropathogenic bacteria. The RNASE6 gene is heterogeneous in humans due to the presence of single nucleotide polymorphisms (SNPs). RNASE6 ... ...

    Abstract Human Ribonuclease (RNase) 6 is a monocyte and macrophage-derived protein with potent antimicrobial activity toward uropathogenic bacteria. The RNASE6 gene is heterogeneous in humans due to the presence of single nucleotide polymorphisms (SNPs). RNASE6 rs1045922 is the most common non-synonymous SNP, resulting in a G to A substitution that determines an arginine (R) to glutamine (Q) transversion at position 66 in the protein sequence. By structural analysis we observed that R66Q substitution significantly reduces the positive electrostatic charge at the protein surface. Here, we generated both recombinant RNase 6-R66 and -Q66 protein variants and determined their antimicrobial activity toward uropathogenic Escherichia coli (UPEC), the most common cause of UTI. We found that the R66 variant, encoded by the major SNP rs1045922 allele, exhibited superior bactericidal activity in comparison to the Q66 variant. The higher bactericidal activity of R66 variant correlated with an increase in the protein lipopolysaccharide binding and bacterial agglutination abilities, while retaining the same enzymatic efficiency. These findings encourage further work to evaluate RNASE6 SNP distribution and its impact in UTI susceptibility.
    Keywords RNase ; RNase 6 ; RNase k6 ; single nucleotide polymorphisms ; antimicrobial peptides ; urinary tract infections ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 572
    Language English
    Publishing date 2024-01-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Structural determinants for tRNA selective cleavage by RNase 2/EDN.

    Li, Jiarui / Kang, Xincheng / Guidi, Irene / Lu, Lu / Fernández-Millán, Pablo / Prats-Ejarque, Guillem / Boix, Ester

    Structure (London, England : 1993)

    2024  Volume 32, Issue 3, Page(s) 328–341.e4

    Abstract: tRNA-derived fragments (tRFs) have emerged as key players of immunoregulation. Some RNase A superfamily members participate in the shaping of the tRFs population. By comparing wild-type and knockout macrophage cell lines, our previous work revealed that ... ...

    Abstract tRNA-derived fragments (tRFs) have emerged as key players of immunoregulation. Some RNase A superfamily members participate in the shaping of the tRFs population. By comparing wild-type and knockout macrophage cell lines, our previous work revealed that RNase 2 can selectively cleave tRNAs. Here, we confirm the in vitro protein cleavage pattern by screening of synthetic tRNAs, single-mutant variants, and anticodon-loop DNA/RNA hairpins. By sequencing of tRF products, we identified the cleavage selectivity of recombinant RNase 2 with base specificity at B
    MeSH term(s) Anticodon ; RNA, Transfer/chemistry ; Endoribonucleases/genetics ; RNA
    Chemical Substances ribonuclease U (EC 3.1.27.-) ; Anticodon ; RNA, Transfer (9014-25-9) ; Endoribonucleases (EC 3.1.-) ; RNA (63231-63-0)
    Language English
    Publishing date 2024-01-15
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2023.12.012
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4141: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Editorial: novel strategies for the design of therapeutic antimicrobial peptides.

    Boix, Ester

    Current drug targets

    2012  Volume 13, Issue 9, Page(s) 1119–1120

    MeSH term(s) Anti-Infective Agents/chemistry ; Anti-Infective Agents/pharmacology ; Biophysics ; Drug Design ; Drug Evaluation, Preclinical
    Chemical Substances Anti-Infective Agents
    Language English
    Publishing date 2012-04-28
    Publishing country United Arab Emirates
    Document type Editorial
    ZDB-ID 2064859-5
    ISSN 1873-5592 ; 1389-4501
    ISSN (online) 1873-5592
    ISSN 1389-4501
    DOI 10.2174/138945012802002429
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5578: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: Editorial: Role of Ribonucleases in Immune Response Regulation During Infection and Cancer.

    Boix, Ester / Acquati, Francesco / Leonidas, Demetres / Pulido, David

    Frontiers in immunology

    2020  Volume 11, Page(s) 236

    MeSH term(s) Animals ; Endoribonucleases/metabolism ; Humans ; Immunity, Innate ; Infections/metabolism ; Neoplasms/metabolism ; Ribonuclease, Pancreatic/metabolism
    Chemical Substances Endoribonucleases (EC 3.1.-) ; ribonuclease T(2) (EC 3.1.27.1) ; Ribonuclease, Pancreatic (EC 3.1.27.5)
    Language English
    Publishing date 2020-02-19
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2020.00236
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Synergism between Host Defence Peptides and Antibiotics Against Bacterial Infections.

    Li, Jiarui / Fernández-Millán, Pablo / Boix, Ester

    Current topics in medicinal chemistry

    2020  Volume 20, Issue 14, Page(s) 1238–1263

    Abstract: Background: Antimicrobial resistance (AMR) to conventional antibiotics is becoming one of the main global health threats and novel alternative strategies are urging. Antimicrobial peptides (AMPs), once forgotten, are coming back into the scene as ... ...

    Abstract Background: Antimicrobial resistance (AMR) to conventional antibiotics is becoming one of the main global health threats and novel alternative strategies are urging. Antimicrobial peptides (AMPs), once forgotten, are coming back into the scene as promising tools to overcome bacterial resistance. Recent findings have attracted attention to the potentiality of AMPs to work as antibiotic adjuvants.
    Methods: In this review, we have tried to collect the currently available information on the mechanism of action of AMPs in synergy with other antimicrobial agents. In particular, we have focused on the mechanisms of action that mediate the inhibition of the emergence of bacterial resistance by AMPs.
    Results and conclusion: We find in the literature many examples where AMPs can significantly reduce the antibiotic effective concentration. Mainly, the peptides work at the bacterial cell wall and thereby facilitate the drug access to its intracellular target. Complementarily, AMPs can also contribute to permeate the exopolysaccharide layer of biofilm communities, or even prevent bacterial adhesion and biofilm growth. Secondly, we find other peptides that can directly block the emergence of bacterial resistance mechanisms or interfere with the community quorum-sensing systems. Interestingly, the effective peptide concentrations for adjuvant activity and inhibition of bacterial resistance are much lower than the required for direct antimicrobial action. Finally, many AMPs expressed by innate immune cells are endowed with immunomodulatory properties and can participate in the host response against infection. Recent studies in animal models confirm that AMPs work as adjuvants at non-toxic concentrations and can be safely administrated for novel combined chemotherapies.
    MeSH term(s) Animals ; Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; Antimicrobial Cationic Peptides/chemistry ; Antimicrobial Cationic Peptides/pharmacology ; Bacteria/drug effects ; Bacterial Infections/drug therapy ; Biofilms/drug effects ; Cell Membrane Permeability ; Drug Resistance, Microbial ; Drug Synergism ; Drug Therapy, Combination ; Humans ; Polysaccharides, Bacterial/metabolism
    Chemical Substances Anti-Bacterial Agents ; Antimicrobial Cationic Peptides ; Polysaccharides, Bacterial
    Language English
    Publishing date 2020-03-02
    Publishing country United Arab Emirates
    Document type Journal Article ; Review
    ZDB-ID 2064823-6
    ISSN 1873-4294 ; 1568-0266
    ISSN (online) 1873-4294
    ISSN 1568-0266
    DOI 10.2174/1568026620666200303122626
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5572: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  8. Article: Exploring the RNase A scaffold to combine catalytic and antimicrobial activities. Structural characterization of RNase 3/1 chimeras.

    Fernández-Millán, Pablo / Vázquez-Monteagudo, Sergi / Boix, Ester / Prats-Ejarque, Guillem

    Frontiers in molecular biosciences

    2022  Volume 9, Page(s) 964717

    Abstract: Design of novel antibiotics to fight antimicrobial resistance is one of the first global health priorities. Novel protein-based strategies come out as alternative therapies. Based on the structure-function knowledge of the RNase A superfamily we have ... ...

    Abstract Design of novel antibiotics to fight antimicrobial resistance is one of the first global health priorities. Novel protein-based strategies come out as alternative therapies. Based on the structure-function knowledge of the RNase A superfamily we have engineered a chimera that combines RNase 1 highest catalytic activity with RNase 3 unique antipathogen properties. A first construct (RNase 3/1-v1) was successfully designed with a catalytic activity 40-fold higher than RNase 3, but alas in detriment of its anti-pathogenic activity. Next, two new versions of the original chimeric protein were created showing improvement in the antimicrobial activity. Both second generation versions (RNases 3/1-v2 and -v3) incorporated a loop characteristic of RNase 3 (L7), associated to antimicrobial activity. Last, removal of an RNase 1 flexible loop (L1) in the third version enhanced its antimicrobial properties and catalytic efficiency. Here we solved the 3D structures of the three chimeras at atomic resolution by X-ray crystallography. Structural analysis outlined the key functional regions. Prediction by molecular docking of the protein chimera in complex with dinucleotides highlighted the contribution of the C-terminal region to shape the substrate binding cavity and determine the base selectivity and catalytic efficiency. Nonetheless, the structures that incorporated the key features related to RNase 3 antimicrobial activity retained the overall RNase 1 active site conformation together with the essential structural elements for binding to the human ribonuclease inhibitor (RNHI), ensuring non-cytotoxicity. Results will guide us in the design of the best RNase pharmacophore for anti-infective therapies.
    Language English
    Publishing date 2022-09-14
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2814330-9
    ISSN 2296-889X
    ISSN 2296-889X
    DOI 10.3389/fmolb.2022.964717
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Psychosocial stress moderates the relationship between cerebrospinal fluid lactate dehydrogenase and the duration of untreated psychosis in first-episode psychosis.

    Giné-Servén, Eloi / Boix-Quintana, Ester / Daví-Loscos, Eva / Cepedello, Sandra / Moreno-Sancho, Lara / Niubó, Marta / Hernández-Antón, Rebeca / Cuesta, Manuel J / Labad, Javier

    Frontiers in psychiatry

    2024  Volume 15, Page(s) 1327928

    Abstract: Introduction: Previous research has shown that lower lactate dehydrogenase (LDH) concentrations in cerebrospinal fluid (CSF) are associated with longer prodromal symptoms in first-episode psychosis (FEP). We aimed to study whether there is a ... ...

    Abstract Introduction: Previous research has shown that lower lactate dehydrogenase (LDH) concentrations in cerebrospinal fluid (CSF) are associated with longer prodromal symptoms in first-episode psychosis (FEP). We aimed to study whether there is a relationship between the duration of untreated psychosis (DUP) and LDH and other CSF biomarkers in FEP and whether stressful life events moderate this association.
    Methods: Ninety-five inpatients with FEP and with less than 6 weeks of antipsychotic treatment were included in the study. All participants were informed about the nature of the study, which was approved by the local ethics committee, and signed an informed consent form. A lumbar puncture was performed at index admission (baseline) to measure CSF parameters (glucose, total protein, LDH). The DUP was assessed with the Quick Psychosis Onset and Prodromal Symptoms Inventory (Q-POPSI). Stressful life events (SLEs) in the previous 6 months were assessed with the List of Threatening Experiences. We dichotomized the SLE variable into having experienced at least one SLE or no experience of SLEs. Statistical analyses were performed with SPSS v. 25.0. Total protein and LDH concentrations were natural log transformed (ln) to reduce skewness. Multiple linear regression analyses were conducted to explore the association between the DUP and CSF parameters (considered the dependent variable). Age, sex, DUP and SLEs were considered independent variables. We tested the DUP by SLE interaction. Significant interactions were included in the final model. The threshold for significance was set at p<0.05.
    Results: Fifty-four FEP patients (56.8%) reported an SLE in the previous 6 months. There were no significant differences in the DUP between patients with or without SLEs. There were no significant differences in CSF biomarkers between the SLE groups. In the multiple linear regression analyses, we found a significant DUP by SLE interaction effect on CSF LDH concentrations (standardized beta= -0.320, t= -2.084, p= 0.040). In patients with SLEs, a shorter DUP was associated with higher CSF LDH concentrations and vice versa. No significant associations were found between the DUP or SLEs and other CSF biomarkers (glucose, total proteins).
    Conclusions: Our study suggests that psychosocial stress moderates the relationship between the onset of psychosis and CSF biomarkers related to bioenergetic systems.
    Language English
    Publishing date 2024-02-15
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2564218-2
    ISSN 1664-0640
    ISSN 1664-0640
    DOI 10.3389/fpsyt.2024.1327928
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Correction: Lu et al. Weighted Gene Co-Expression Network Analysis Identifies Key Modules and Hub Genes Associated with Mycobacterial Infection of Human Macrophages.

    Lu, Lu / Wei, Ran-Lei / Bhakta, Sanjib / Waddell, Simon J / Boix, Ester

    Antibiotics (Basel, Switzerland)

    2021  Volume 10, Issue 7

    Abstract: The authors wish to make the following corrections to this paper [ ... ]. ...

    Abstract The authors wish to make the following corrections to this paper [...].
    Language English
    Publishing date 2021-06-29
    Publishing country Switzerland
    Document type Published Erratum
    ZDB-ID 2681345-2
    ISSN 2079-6382
    ISSN 2079-6382
    DOI 10.3390/antibiotics10070792
    Database MEDical Literature Analysis and Retrieval System OnLINE

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