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  1. Article ; Online: Ebolavirus VP40 redux. Or rather, redox.

    Zinzula, Luca

    Structure (London, England : 1993)

    2023  Volume 31, Issue 9, Page(s) 1008–1010

    Abstract: The virion protein 40 (VP40) forms the viral matrix, mediates budding, and downregulates viral RNA synthesis in ebolaviruses. In this issue of Structure, Werner et al. present a structure of VP40 from Sudan ebolavirus with a previously unresolved ... ...

    Abstract The virion protein 40 (VP40) forms the viral matrix, mediates budding, and downregulates viral RNA synthesis in ebolaviruses. In this issue of Structure, Werner et al. present a structure of VP40 from Sudan ebolavirus with a previously unresolved disulfide bridge that enables regulation of VP40 functions via human thioredoxin.
    MeSH term(s) Humans ; Ebolavirus/genetics ; Oxidation-Reduction ; Cell Division ; Disulfides ; Virion
    Chemical Substances Disulfides
    Language English
    Publishing date 2023-09-08
    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.2023.08.010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Lost in deletion: The enigmatic ORF8 protein of SARS-CoV-2.

    Zinzula, Luca

    Biochemical and biophysical research communications

    2020  Volume 538, Page(s) 116–124

    Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) genome contains nine open reading frames (ORFs) that encode for accessory proteins which, although dispensable for viral replication, are important for the modulation of the host infected ... ...

    Abstract The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) genome contains nine open reading frames (ORFs) that encode for accessory proteins which, although dispensable for viral replication, are important for the modulation of the host infected cell metabolism and innate immunity evasion. Among those, the ORF8 gene encodes for the homonymous multifunctional, highly immunogenic, immunoglobulin-like protein that was recently found to inhibit presentation of viral antigens by class I major histocompatibility complex, suppress the type I interferon antiviral response and interact with host factors involved in pulmonary inflammation and fibrogenesis. Moreover, the ORF8 is a hypervariable gene rapidly evolving among SARS-related coronaviruses, with a tendency to recombine and undergo deletions that are deemed to facilitate the virus adaptation to the human host. Intriguingly, SARS-CoV-2 variants isolated in the beginning of the coronavirus disease 2019 (Covid-19) pandemic that were deleted of the ORF8 gene have been associated to milder symptoms and better disease outcome. This minireview summarizes the current knowledge on the SARS-CoV-2 ORF8 protein in perspective to its potential as antiviral target and with special emphasis on the biochemical, biophysical and structural aspects of its molecular biology.
    MeSH term(s) Antiviral Agents/pharmacology ; Host-Pathogen Interactions/physiology ; Humans ; Immunity, Innate ; Mutation ; SARS-CoV-2/genetics ; SARS-CoV-2/metabolism ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Viral Proteins/metabolism
    Chemical Substances Antiviral Agents ; ORF8 protein, SARS-CoV-2 ; Viral Proteins
    Language English
    Publishing date 2020-10-21
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2020.10.045
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Lost in deletion

    Zinzula, Luca

    Biochemical and Biophysical Research Communications ; ISSN 0006-291X

    The enigmatic ORF8 protein of SARS-CoV-2

    2020  

    Keywords Biophysics ; Cell Biology ; Biochemistry ; Molecular Biology ; covid19
    Language English
    Publisher Elsevier BV
    Publishing country us
    Document type Article ; Online
    DOI 10.1016/j.bbrc.2020.10.045
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Brucella ceti and Brucella pinnipedialis genome characterization unveils genetic features that highlight their zoonotic potential.

    Orsini, Massimiliano / Ianni, Andrea / Zinzula, Luca

    MicrobiologyOpen

    2022  Volume 11, Issue 5, Page(s) e1329

    Abstract: The Gram-negative bacteria Brucella ceti and Brucella pinnipedialis circulate in marine environments primarily infecting marine mammals, where they cause an often-fatal disease named brucellosis. The increase of brucellosis among several species of ... ...

    Abstract The Gram-negative bacteria Brucella ceti and Brucella pinnipedialis circulate in marine environments primarily infecting marine mammals, where they cause an often-fatal disease named brucellosis. The increase of brucellosis among several species of cetaceans and pinnipeds, together with the report of sporadic human infections, raises concerns about the zoonotic potential of these pathogens on a large scale and may pose a threat to coastal communities worldwide. Therefore, the characterization of the B. ceti and B. pinnipedialis genetic features is a priority to better understand the pathological factors that may impact global health. Moreover, an in-depth functional analysis of the B. ceti and B. pinnipedialis genome in the context of virulence and pathogenesis was not undertaken so far. Within this picture, here we present the comparative whole-genome characterization of all B. ceti and B. pinnipedialis genomes available in public resources, uncovering a collection of genetic tools possessed by these aquatic bacterial species compared to their zoonotic terrestrial relatives. We show that B. ceti and B. pinnipedialis genomes display a wide host-range infection capability and a polyphyletic phylogeny within the genus, showing a genomic structure that fits the canonical definition of closeness. Functional genome annotation led to identifying genes related to several pathways involved in mechanisms of infection, others conferring pan-susceptibility to antimicrobials and a set of virulence genes that highlight the similarity of B. ceti and B. pinnipedialis genotypes to those of Brucella spp. displaying human-infecting phenotypes.
    MeSH term(s) Animals ; Humans ; Brucella/genetics ; Brucellosis/microbiology ; Caniformia/microbiology ; Cetacea/microbiology
    Language English
    Publishing date 2022-10-31
    Publishing country England
    Document type Journal Article
    ZDB-ID 2661368-2
    ISSN 2045-8827 ; 2045-8827
    ISSN (online) 2045-8827
    ISSN 2045-8827
    DOI 10.1002/mbo3.1329
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Biophysical characterization of the cetacean morbillivirus haemagglutinin glycoprotein.

    Zinzula, Luca / Scholz, Judith / Nagy, István / Di Guardo, Giovanni / Orsini, Massimiliano

    Virus research

    2023  Volume 336, Page(s) 199231

    Abstract: Cetacean morbillivirus (CeMV) is an enveloped, non-segmented, negative-stranded RNA virus that infects marine mammals, spreading across species and causing lethal disease outbreaks worldwide. Among the eight proteins encoded by the CeMV genome, the ... ...

    Abstract Cetacean morbillivirus (CeMV) is an enveloped, non-segmented, negative-stranded RNA virus that infects marine mammals, spreading across species and causing lethal disease outbreaks worldwide. Among the eight proteins encoded by the CeMV genome, the haemagglutinin (H) glycoprotein is responsible for the virus attachment to host cell receptors. CeMV H represents an attractive target for antiviral and diagnostic research, yet the elucidation of the molecular mechanisms underlying its role in infection and inter-species transmission was hampered thus far due to the unavailability of recombinant versions of the protein. Here we present the cloning, expression and purification of a recombinant CeMV H ectodomain (rH-ecto), providing an initial characterization of its biophysical and structural properties. Sodium dodecyl sulphate - polyacrylamide gel electrophoresis (PAGE) combined to Western blot analysis and periodic acid Schiff assay showed that CeMV rH-ecto is purifiable at homogeneity from insect cells as a secreted, soluble and glycosylated protein. Miniaturized differential scanning fluorimetry, Blue Native PAGE and size exclusion chromatography coupled to multiangle light scattering revealed that CeMV rH-ecto is globularly folded, thermally stable and exists in solution in the oligomeric states of dimer and multiple of dimers. Furthermore, negative stain electron microscopy single particle analysis allowed us to delineate a low-resolution molecular architecture of the CeMV rH-ecto dimer, which recapitulates native assemblies from other morbilliviral H proteins, such as those from measles virus and canine distemper virus. This set of experiments by orthogonal techniques validates the CeMV rH-ecto as an experimental model for future biochemical studies on its structure and functions.
    Language English
    Publishing date 2023-09-28
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 605780-9
    ISSN 1872-7492 ; 0168-1702
    ISSN (online) 1872-7492
    ISSN 0168-1702
    DOI 10.1016/j.virusres.2023.199231
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Molecular signatures in cetacean morbillivirus and host species proteomes: Unveiling the evolutionary dynamics of an enigmatic pathogen?

    Zinzula, Luca / Mazzariol, Sandro / Di Guardo, Giovanni

    Microbiology and immunology

    2021  Volume 66, Issue 2, Page(s) 52–58

    Abstract: Cetacean morbillivirus (CeMV) infects marine mammals often causing a fatal respiratory and neurological disease. Recently, CeMV has expanded its geographic and host species range, with cases being reported worldwide among dolphins, whales, seals, and ... ...

    Abstract Cetacean morbillivirus (CeMV) infects marine mammals often causing a fatal respiratory and neurological disease. Recently, CeMV has expanded its geographic and host species range, with cases being reported worldwide among dolphins, whales, seals, and other aquatic mammalian species, and therefore has emerged as the most threatening nonanthropogenic factor affecting marine mammal's health and conservation. Extensive research efforts have aimed to understand CeMV epidemiology and ecology, however, the molecular mechanisms underlying its transmission and pathogenesis are still poorly understood. In particular, the field suffers from a knowledge gap on the structural and functional properties of CeMV proteins and their host interactors. Nevertheless, the body of scientific literature produced in recent years has inaugurated new investigational trends, driving future directions in CeMV molecular research. In this mini-review, the most recent literature has been summarized in the context of such research trends, and categorized into four priority research topics, such as (1) the interaction between CeMV glycoprotein and its host cell receptors across several species; (2) the CeMV molecular determinants responsible for different disease phenotype; (3) the host molecular determinants responsible for differential susceptibility to CeMV infection; (4) the CeMV molecular determinants responsible for difference virulence among circulating CeMV strains. Arguably, these are the most urgent topics that need to be investigated and that most promisingly will help to shed light on the details of CeMV evolutionary dynamics in the immediate future.
    MeSH term(s) Animals ; Cetacea ; Morbillivirus/genetics ; Morbillivirus Infections/veterinary ; Proteome
    Chemical Substances Proteome
    Language English
    Publishing date 2021-11-29
    Publishing country Australia
    Document type Journal Article ; Review
    ZDB-ID 224792-6
    ISSN 1348-0421 ; 0385-5600
    ISSN (online) 1348-0421
    ISSN 0385-5600
    DOI 10.1111/1348-0421.12949
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Suramin inhibits SARS-CoV-2 nucleocapsid phosphoprotein genome packaging function.

    Boniardi, Irene / Corona, Angela / Basquin, Jerome / Basquin, Claire / Milia, Jessica / Nagy, István / Tramontano, Enzo / Zinzula, Luca

    Virus research

    2023  Volume 336, Page(s) 199221

    Abstract: The coronavirus disease 2019 (COVID-19) pandemic is fading, however its etiologic agent severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues posing - despite the availability of licensed vaccines - a global health threat, due to the ... ...

    Abstract The coronavirus disease 2019 (COVID-19) pandemic is fading, however its etiologic agent severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues posing - despite the availability of licensed vaccines - a global health threat, due to the potential emergence of vaccine-resistant SARS-CoV-2 variants. This makes the development of new drugs against COVID-19 a persistent urgency and sets as research priority the validation of novel therapeutic targets within the SARS-CoV-2 proteome. Among these, a promising one is the SARS-CoV-2 nucleocapsid (N) phosphoprotein, a major structural component of the virion with indispensable role in packaging the viral genome into a ribonucleoprotein (RNP) complex, which also contributes to SARS-CoV-2 innate immune evasion by inhibiting the host cell type-I interferon (IFN-I) response. By combining miniaturized differential scanning fluorimetry with microscale thermophoresis, we found that the 100-year-old drug Suramin interacts with SARS-CoV-2 N-terminal domain (NTD) and C-terminal domain (CTD), thereby inhibiting their single-stranded RNA (ssRNA) binding function with low-micromolar K
    Language English
    Publishing date 2023-09-15
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 605780-9
    ISSN 1872-7492 ; 0168-1702
    ISSN (online) 1872-7492
    ISSN 0168-1702
    DOI 10.1016/j.virusres.2023.199221
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Ebola and Marburg virus VP35 coiled-coil validated as antiviral target by tripartite split-GFP complementation.

    Zinzula, Luca / Mereu, Angela Maria / Orsini, Massimiliano / Seeleitner, Christine / Bracher, Andreas / Nagy, István / Baumeister, Wolfgang

    iScience

    2022  Volume 25, Issue 11, Page(s) 105354

    Abstract: Ebola virus (EBOV) and Marburg virus (MARV) are highly pathogenic viruses in humans, against which approved antivirals are lacking. During EBOV and MARV infection, coiled-coil mediated oligomerization is essential for the virion protein 35 (VP35) ... ...

    Abstract Ebola virus (EBOV) and Marburg virus (MARV) are highly pathogenic viruses in humans, against which approved antivirals are lacking. During EBOV and MARV infection, coiled-coil mediated oligomerization is essential for the virion protein 35 (VP35) polymerase co-factor function and type I interferon antagonism, making VP35 coiled-coil an elective drug target. We established a tripartite split-green fluorescent protein (GFP) fluorescence complementation (FC) system based on recombinant GFP-tagged EBOV and MARV VP35, which probes VP35 coiled-coil assembly by monitoring fluorescence on
    Language English
    Publishing date 2022-10-13
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2022.105354
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: The oriental hornet (Vespa orientalis) as a potential vector of honey bee's pathogens and a threat for public health in North‐East Italy

    Paolo Zucca / Anna Granato / Franco Mutinelli / Eliana Schiavon / Fulvio Bordin / Marco Dimech / Roberto Andrea Balbo / David Mifsud / Maurizio Dondi / Claudio Cipolat‐Gotet / Marie Christin Rossmann / Metka Pislak Ocepek / Dino Scaravelli / Manlio Palei / Luca Zinzula / Kimberly Spanjol

    Veterinary Medicine and Science, Vol 10, Iss 1, Pp n/a-n/a (2024)

    2024  

    Abstract: Abstract Background Oriental hornets are large predatory hymenoptera that occur in the southern part of Asia and the southeastern Mediterranean. Among many pests of bee colonies, Vespa orientalis was recorded to be one of the most destructive. Objectives ...

    Abstract Abstract Background Oriental hornets are large predatory hymenoptera that occur in the southern part of Asia and the southeastern Mediterranean. Among many pests of bee colonies, Vespa orientalis was recorded to be one of the most destructive. Objectives The aim of this study was to: (1) monitor the presence of pathogens carried by V. orientalis that could potentially threaten honey bees and public health; (2) describe the hornet's predatory behavior on honey bee colonies and (3) collect the medical history of a V. orientalis sting suffered by a 36‐year‐old woman. Methods Observations of V. orientalis predatory behavior and the catches of hornets for parasitological and microbiological examination, using molecular and bacteriological analyses, were carried out in three experimental apiaries, both in spring in order to capture the foundress queens and during the summer to capture the workers. Furthermore, the medical history and photographic documentation of a V. orientalis sting suffered by a 36‐year‐old woman have been collected. Results The results obtained highlight that V. orientalis is capable of causing serious damage to beekeeping by killing bees, putting under stress the honey bee colonies and by potentially spreading honey bee pathogens among apiaries. These hornets may also become a public health concern, since they are capable of inflicting multiple, painful stings on humans. Conclusions Only the development of an Integrated Management Control Program will be able to contain the negative effects of anomalous population growth and the potentially negative impact on honey bees and public health of V. orientalis.
    Keywords Apis mellifera ; honey bee health ; oriental hornet ; public health ; vector ; Vespa orientalis ; Veterinary medicine ; SF600-1100
    Subject code 941
    Language English
    Publishing date 2024-01-01T00:00:00Z
    Publisher Wiley
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Trans-synaptic assemblies link synaptic vesicles and neuroreceptors.

    Martinez-Sanchez, Antonio / Laugks, Ulrike / Kochovski, Zdravko / Papantoniou, Christos / Zinzula, Luca / Baumeister, Wolfgang / Lučić, Vladan

    Science advances

    2021  Volume 7, Issue 10

    Abstract: Synaptic transmission is characterized by fast, tightly coupled processes and complex signaling pathways that require a precise protein organization, such as the previously reported nanodomain colocalization of pre- and postsynaptic proteins. Here, we ... ...

    Abstract Synaptic transmission is characterized by fast, tightly coupled processes and complex signaling pathways that require a precise protein organization, such as the previously reported nanodomain colocalization of pre- and postsynaptic proteins. Here, we used cryo-electron tomography to visualize synaptic complexes together with their native environment comprising interacting proteins and lipids on a 2- to 4-nm scale. Using template-free detection and classification, we showed that tripartite trans-synaptic assemblies (subcolumns) link synaptic vesicles to postsynaptic receptors and established that a particular displacement between directly interacting complexes characterizes subcolumns. Furthermore, we obtained de novo average structures of ionotropic glutamate receptors in their physiological composition, embedded in plasma membrane. These data support the hypothesis that synaptic function is carried by precisely organized trans-synaptic units. It provides a framework for further exploration of synaptic and other large molecular assemblies that link different cells or cellular regions and may require weak or transient interactions to exert their function.
    Language English
    Publishing date 2021-03-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.abe6204
    Database MEDical Literature Analysis and Retrieval System OnLINE

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