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  1. AU="Jaimes, Javier A."
  2. AU="Ennio?Ferrari"
  3. AU="Cane, Douglas"
  4. AU="Vasiliauskaite, Lina"
  5. AU="Fraczek, Paula M"
  6. AU="Fritz, Cassandra Dl"
  7. AU="Sommer, Norbert"
  8. AU="Brandão, Claudia Valeria S"
  9. AU="Jesky, Mark D"
  10. AU="Filipe de Oliveira"
  11. AU="Chang, Shantel"
  12. AU="Mbow, M Lamine"
  13. AU="Sekhon, M."
  14. AU="Song, Y-S"
  15. AU="Collins, Brooke"
  16. AU="Ali Al-Naji"
  17. AU="Bansal, Bhavtosh"
  18. AU="De Cremer, Kaat"
  19. AU="O'Neil, James"
  20. AU=White Tonya
  21. AU="Clark-Deener, Sherrie"
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  1. Artikel: Intrinsic furin-mediated cleavability of the spike S1/S2 site from SARS-CoV-2 variant B.1.1.529 (Omicron).

    Lubinski, Bailey / Jaimes, Javier A / Whittaker, Gary R

    bioRxiv : the preprint server for biology

    2022  

    Abstract: The ability of SARS-CoV-2 to be primed for viral entry by the host cell protease furin has become one of the most investigated of the numerous transmission and pathogenicity features of the virus. SARS-CoV-2 The variant B.1.1.529 (Omicron) emerged in ... ...

    Abstract The ability of SARS-CoV-2 to be primed for viral entry by the host cell protease furin has become one of the most investigated of the numerous transmission and pathogenicity features of the virus. SARS-CoV-2 The variant B.1.1.529 (Omicron) emerged in late 2020 and has continued to evolve and is now present in several distinct sub-variants. Here, we analyzed the "furin cleavage site" of the spike protein of SARS-CoV-2 B.1.1.529 (Omicron variant)
    Sprache Englisch
    Erscheinungsdatum 2022-07-26
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2022.04.20.488969
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: SARS-CoV-2 electrochemical immunosensor based on the spike-ACE2 complex.

    Vásquez, Viviana / Navas, Maria-Cristina / Jaimes, Javier A / Orozco, Jahir

    Analytica chimica acta

    2022  Band 1205, Seite(n) 339718

    Abstract: Rapid, straightforward, and massive diagnosis of coronavirus disease 2019 (COVID-19) is one of the more important measures to mitigate the current pandemics. This work reports on an immunosensor to rapidly detect the spike protein from the severe acute ... ...

    Abstract Rapid, straightforward, and massive diagnosis of coronavirus disease 2019 (COVID-19) is one of the more important measures to mitigate the current pandemics. This work reports on an immunosensor to rapidly detect the spike protein from the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The immunosensing device entraps the spike protein linked to angiotensin-converting enzyme host receptor (ACE2) protein in a sandwich between carboxylated magnetic beads functionalized with an anti-spike antibody and an anti-ACE2 antibody, further labeled with streptavidin (poly)horseradish peroxidase (HRP) reporter enzyme. The particles were confined at the surface of screen-printed gold electrodes, whose signal resulting from the interaction of the enzyme with a mediator was recorded in a portable potentiostat. The immunosensor showed a sensitivity of 0.83 μA∗mL/μg and a limit of detection of 22.5 ng/mL of spike protein, with high reproducibility. As a proof-of-concept, it detected commercial spike protein-supplemented buffer solutions, pseudovirions, isolated viral particles and ten nasopharyngeal swab samples from infected patients compared to samples from three healthy individuals paving the way to detect the virus closer to the patient.
    Mesh-Begriff(e) Angiotensin-Converting Enzyme 2 ; Biosensing Techniques/methods ; COVID-19/diagnosis ; Humans ; Immunoassay ; Protein Binding ; Reproducibility of Results ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus
    Chemische Substanzen Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Sprache Englisch
    Erscheinungsdatum 2022-03-23
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 1483436-4
    ISSN 1873-4324 ; 0003-2670
    ISSN (online) 1873-4324
    ISSN 0003-2670
    DOI 10.1016/j.aca.2022.339718
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Intrinsic furin-mediated cleavability of the spike S1/S2 site from SARS-CoV-2 variant B.1.529 (Omicron)

    Lubinski, Bailey / Jaimes, Javier A. / Whittaker, Gary

    bioRxiv

    Abstract: The ability of SARS-CoV-2 to be primed for viral entry by the host cell protease furin has become one of the most investigated of the numerous transmission and pathogenicity features of the virus. Here, we analyzed the S1/S2 cleavage site (also called ... ...

    Abstract The ability of SARS-CoV-2 to be primed for viral entry by the host cell protease furin has become one of the most investigated of the numerous transmission and pathogenicity features of the virus. Here, we analyzed the S1/S2 cleavage site (also called furin cleavage site) of the spike protein of SARS-CoV-2 B.1.529 (Omicron variant) in vitro, to assess the role of two key mutations (spike gene, N679K and P681H) compared to the ancestral B.1 virus. We observed significantly increased intrinsic cleavability with furin compared to an original B lineage virus (Wuhan-Hu-1) and two variants, B.1.1.7 (Alpha) and B.1.617 (Delta), that subsequently had wide circulation. Increased furin-mediated cleavage was attributed to the N679K mutation, which lies outside the conventional furin binding pocket. Our findings suggest that B.1.529 (Omicron variant) has gained genetic features linked to intrinsic furin cleavability, in line with its evolution within the population as the COVID-19 pandemic has proceeded.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2022-04-22
    Verlag Cold Spring Harbor Laboratory
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2022.04.20.488969
    Datenquelle COVID19

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  4. Artikel ; Online: Feline coronavirus: Insights into viral pathogenesis based on the spike protein structure and function.

    Jaimes, Javier A / Whittaker, Gary R

    Virology

    2018  Band 517, Seite(n) 108–121

    Abstract: Feline coronavirus (FCoV) is an etiological agent that causes a benign enteric illness and the fatal systemic disease feline infectious peritonitis (FIP). The FCoV spike (S) protein is considered the viral regulator for binding and entry to the cell. ... ...

    Abstract Feline coronavirus (FCoV) is an etiological agent that causes a benign enteric illness and the fatal systemic disease feline infectious peritonitis (FIP). The FCoV spike (S) protein is considered the viral regulator for binding and entry to the cell. This protein is also involved in FCoV tropism and virulence, as well as in the switch from enteric disease to FIP. This regulation is carried out by spike's major functions: receptor binding and virus-cell membrane fusion. In this review, we address important aspects in FCoV genetics, replication and pathogenesis, focusing on the role of S. To better understand this, FCoV S protein models were constructed, based on the human coronavirus NL63 (HCoV-NL63) S structure. We describe the specific structural characteristics of the FCoV S, in comparison with other coronavirus spikes. We also revise the biochemical events needed for FCoV S activation and its relation to the structural features of the protein.
    Mesh-Begriff(e) Animals ; Cats ; Coronavirus, Feline/genetics ; Coronavirus, Feline/metabolism ; Coronavirus, Feline/pathogenicity ; Feline Infectious Peritonitis/pathology ; Feline Infectious Peritonitis/virology ; Gene Expression Regulation, Viral/physiology ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; Virus Replication
    Chemische Substanzen Spike Glycoprotein, Coronavirus ; spike protein, feline infectious peritonitis virus
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2018-01-10
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 200425-2
    ISSN 1096-0341 ; 0042-6822
    ISSN (online) 1096-0341
    ISSN 0042-6822
    DOI 10.1016/j.virol.2017.12.027
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Proteolytic Cleavage of the SARS-CoV-2 Spike Protein and the Role of the Novel S1/S2 Site.

    Jaimes, Javier A / Millet, Jean K / Whittaker, Gary R

    iScience

    2020  Band 23, Heft 6, Seite(n) 101212

    Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 19 (COVID-19) has rapidly spread to the entire world within a few months. The origin of SARS-CoV-2 has been related to the lineage B Betacoronavirus ... ...

    Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 19 (COVID-19) has rapidly spread to the entire world within a few months. The origin of SARS-CoV-2 has been related to the lineage B Betacoronavirus SARS-CoV and SARS-related coronaviruses found in bats. Early characterizations of the SARS-CoV-2 genome revealed the existence of a distinct four amino acid insert within the spike (S) protein (underlined, SPRRAR↓S), at the S1/S2 site located at the interface between the S1 receptor binding subunit and the S2 fusion subunit. Notably, this insert appears to be a distinguishing feature among SARS-related sequences and introduces a potential cleavage site for the protease furin. Here, we investigate the potential role of this novel S1/S2 cleavage site and present direct biochemical evidence for proteolytic processing by a variety of proteases. We discuss these findings in the context of the origin of SARS-CoV-2, viral stability, and transmission.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-05-28
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2020.101212
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Proteolytic cleavage of the SARS-CoV-2 spike protein and the role of the novel S1/S2 site.

    Jaimes, Javier A / Millet, Jean K / Whittaker, Gary R

    SSRN

    2020  , Seite(n) 3581359

    Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 19 (COVID-19) has rapidly spread from an initial outbreak in Wuhan, China in December 2019 to the rest of the world within a few months. On March ... ...

    Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 19 (COVID-19) has rapidly spread from an initial outbreak in Wuhan, China in December 2019 to the rest of the world within a few months. On March 11
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-05-05
    Erscheinungsland United States
    Dokumenttyp Preprint
    ISSN 1556-5068
    ISSN (online) 1556-5068
    DOI 10.2139/ssrn.3581359
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel ; Online: Molecular diversity of coronavirus host cell entry receptors.

    Millet, Jean K / Jaimes, Javier A / Whittaker, Gary R

    FEMS microbiology reviews

    2020  Band 45, Heft 3

    Abstract: Coronaviruses are a group of viruses causing disease in a wide range of animals, and humans. Since 2002, the successive emergence of bat-borne severe acute respiratory syndrome coronavirus (SARS-CoV), Middle East respiratory syndrome coronavirus (MERS- ... ...

    Abstract Coronaviruses are a group of viruses causing disease in a wide range of animals, and humans. Since 2002, the successive emergence of bat-borne severe acute respiratory syndrome coronavirus (SARS-CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), swine acute diarrhea syndrome coronavirus (SADS-CoV) and SARS-CoV-2 has reinforced efforts in uncovering the molecular and evolutionary mechanisms governing coronavirus cell tropism and interspecies transmission. Decades of studies have led to the discovery of a broad set of carbohydrate and protein receptors for many animal and human coronaviruses. As the main determinant of coronavirus entry, the spike protein binds to these receptors and mediates membrane fusion. Prone to mutations and recombination, spike evolution has been studied extensively. The interactions between spike proteins and their receptors are often complex and despite many advances in the field, there remains many unresolved questions concerning coronavirus tropism modification and cross-species transmission, potentially leading to delays in outbreak responses. The emergence of SARS-CoV-2 underscores the need to address these outstanding issues in order to better anticipate new outbreaks. In this review, we discuss the latest advances in the field of coronavirus receptors emphasizing on the molecular and evolutionary processes that underlie coronavirus receptor usage and host range expansion.
    Mesh-Begriff(e) Animals ; Biodiversity ; COVID-19/metabolism ; COVID-19/virology ; Coronavirus/classification ; Coronavirus/physiology ; Coronavirus Infections/metabolism ; Coronavirus Infections/virology ; Genotype ; Host Specificity ; Host-Pathogen Interactions ; Humans ; Phylogeny ; Receptors, Coronavirus/chemistry ; Receptors, Coronavirus/classification ; Receptors, Coronavirus/metabolism ; SARS-CoV-2/classification ; SARS-CoV-2/physiology ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; Viral Tropism
    Chemische Substanzen Receptors, Coronavirus ; Spike Glycoprotein, Coronavirus
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-10-29
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 283740-7
    ISSN 1574-6976 ; 0168-6445
    ISSN (online) 1574-6976
    ISSN 0168-6445
    DOI 10.1093/femsre/fuaa057
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2165: Hefte anzeigen Standort:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  8. Artikel ; Online: SARS-CoV-2 serosurvey of healthy, privately owned cats presenting to a New York City animal hospital in the early phase of the COVID-19 pandemic (2020-2021)

    Choi, Annette / Stout, Alison E. / Rollins, Alicia / Wang, Kally / Guo, Qinghua / Jaimes, Javier A. / Kennedy, Monica / Wagner, Bettina / Whittaker, Gary R.

    bioRxiv

    Abstract: Both domestic and non-domestic cats are now established to be susceptible to infection by SARS-CoV-2, the cause of the ongoing COVID-19 pandemic. While serious disease in cats may occur in some instances, the majority of infections appear to be ... ...

    Abstract Both domestic and non-domestic cats are now established to be susceptible to infection by SARS-CoV-2, the cause of the ongoing COVID-19 pandemic. While serious disease in cats may occur in some instances, the majority of infections appear to be subclinical. Differing prevalence data for SARS-CoV-2 infection of cats have been reported, and are highly context-dependent. Here, we report a retrospective serological survey of cats presented to an animal practice in New York City, located in close proximity to a large medical center that treated the first wave of COVID-19 patients in the US in the Spring of 2020. We sampled 79, mostly indoor, cats between June 2020 to May 2021, the early part of which time the community was under a strict public health lock-down. Using a highly sensitive and specific fluorescent bead-based multiplex assay, we found an overall prevalence of 13/79 (16%) serologically-positive animals for the study period; however, cats sampled in the Fall of 2020 had a confirmed positive prevalence of 44%. For SARS-CoV-2 seropositive cats, we performed viral neutralization test with live SARS-CoV-2 to additionally confirm presence of SARS-CoV-2 specific antibodies. Of the thirteen seropositive cats, 7/13 (54%) were also positive by virus neutralization, and 2 of seropositive cats had previously documented respiratory signs, with high neutralization titers of 1:1024 and 1:4096; overall however, there was no statistically significant association of SARS-CoV-2 seropositivity with respiratory signs, or with breed, sex or age of the animals. Follow up sampling of cats, while limited in scope, showed that positive serological titers were maintained over time. In comparison, we found an overall confirmed positive prevalence of 51% for feline coronavirus (FCoV), an endemic virus of cats, with 30% confirmed negative for FCoV. We demonstrate the impact of SARS-CoV in a defined feline population during the first wave of SARS-CoV-2 infection of humans, and suggest that human-cat transmission was substantial in our study group. Our data provide a new context for SARS-CoV-2 transmission events across species.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2024-02-15
    Verlag Cold Spring Harbor Laboratory
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2024.02.13.580068
    Datenquelle COVID19

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  9. Artikel ; Online: A Mechanistic Understanding of the Modes of Ca

    Carten, Juliana Debrito / Khelashvili, George / Bidon, Miya K / Straus, Marco R / Tang, Tiffany / Jaimes, Javier A / Whittaker, Gary R / Weinstein, Harel / Daniel, Susan

    ACS infectious diseases

    2024  Band 10, Heft 2, Seite(n) 398–411

    Abstract: The SARS-CoV-1 spike glycoprotein contains a fusion peptide (FP) segment that mediates the fusion of the viral and host cell membranes. Calcium ions are thought to position the FP optimally for membrane insertion by interacting with negatively charged ... ...

    Abstract The SARS-CoV-1 spike glycoprotein contains a fusion peptide (FP) segment that mediates the fusion of the viral and host cell membranes. Calcium ions are thought to position the FP optimally for membrane insertion by interacting with negatively charged residues in this segment (E801, D802, D812, E821, D825, and D830); however, which residues bind to calcium and in what combinations supportive of membrane insertion are unknown. Using biological assays and molecular dynamics studies, we have determined the functional configurations of FP-Ca
    Mesh-Begriff(e) Severe acute respiratory syndrome-related coronavirus ; Amino Acid Sequence ; Calcium/metabolism ; Membrane Fusion/physiology ; Peptides/chemistry ; Ions
    Chemische Substanzen Calcium (SY7Q814VUP) ; Peptides ; Ions
    Sprache Englisch
    Erscheinungsdatum 2024-01-25
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 2373-8227
    ISSN (online) 2373-8227
    DOI 10.1021/acsinfecdis.3c00260
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: Structural modeling of 2019-novel coronavirus (nCoV) spike protein reveals a proteolytically-sensitive activation loop as a distinguishing feature compared to SARS-CoV and related SARS-like coronaviruses.

    Jaimes, Javier A / Andre, Nicole M / Millet, Jean K / Whittaker, Gary R

    ArXiv

    2020  

    Abstract: The 2019 novel coronavirus (2019-nCoV) is currently causing a widespread outbreak centered on Hubei province, China and is a major public health concern. Taxonomically 2019-nCoV is closely related to SARS-CoV and SARS-related bat coronaviruses, and it ... ...

    Abstract The 2019 novel coronavirus (2019-nCoV) is currently causing a widespread outbreak centered on Hubei province, China and is a major public health concern. Taxonomically 2019-nCoV is closely related to SARS-CoV and SARS-related bat coronaviruses, and it appears to share a common receptor with SARS-CoV (ACE-2). Here, we perform structural modeling of the 2019-nCoV spike glycoprotein. Our data provide support for the similar receptor utilization between 2019-nCoV and SARS-CoV, despite a relatively low amino acid similarity in the receptor binding module. Compared to SARS-CoV, we identify an extended structural loop containing basic amino acids at the interface of the receptor binding (S1) and fusion (S2) domains, which we predict to be proteolytically-sensitive. We suggest this loop confers fusion activation and entry properties more in line with MERS-CoV and other coronaviruses, and that the presence of this structural loop in 2019-nCoV may affect virus stability and transmission.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-02-14
    Erscheinungsland United States
    Dokumenttyp Preprint
    ISSN 2331-8422
    ISSN (online) 2331-8422
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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