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  1. Article ; Online: Structures of Langya Virus Fusion Protein Ectodomain in Pre- and Postfusion Conformation.

    May, Aaron J / Pothula, Karunakar Reddy / Janowska, Katarzyna / Acharya, Priyamvada

    Journal of virology

    2023  Volume 97, Issue 6, Page(s) e0043323

    Abstract: Langya virus (LayV) is a paramyxovirus in ... ...

    Abstract Langya virus (LayV) is a paramyxovirus in the
    MeSH term(s) Animals ; Cryoelectron Microscopy ; Henipavirus/metabolism ; Peptides ; Protein Conformation ; Viral Fusion Proteins/metabolism ; Virus Internalization
    Chemical Substances Peptides ; Viral Fusion Proteins
    Language English
    Publishing date 2023-06-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.00433-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 609: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: Transient transfection and purification of SARS-CoV-2 spike protein from mammalian cells.

    Stalls, Victoria / Janowska, Katarzyna / Acharya, Priyamvada

    STAR protocols

    2022  Volume 3, Issue 3, Page(s) 101603

    Abstract: SARS-CoV-2 spike (S) protein ectodomain purification can be challenging, with engineered and natural variations often resulting in lower yields. Here, we present a detailed transfection and purification protocol for the SARS-CoV-2 S ectodomain. We ... ...

    Abstract SARS-CoV-2 spike (S) protein ectodomain purification can be challenging, with engineered and natural variations often resulting in lower yields. Here, we present a detailed transfection and purification protocol for the SARS-CoV-2 S ectodomain. We describe how to trace protein yields during purification using highly sensitive and characteristic changes in S ectodomain intrinsic fluorescence upon thermal denaturation. Additionally, we detail several optimized aspects of the purification including timing and temperature. This protocol facilitates consistent, high-quality preparations of the SARS-CoV-2 S ectodomain. For complete details on the use and execution of this protocol, please refer to Stalls et al. (2022), Gobeil et al. (2022), Edwards et al. (2021), and Henderson et al. (2020).
    MeSH term(s) Animals ; COVID-19 ; Humans ; Mammals/metabolism ; SARS-CoV-2/genetics ; Spike Glycoprotein, Coronavirus/genetics ; Transfection
    Chemical Substances Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Language English
    Publishing date 2022-07-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 2666-1667
    ISSN (online) 2666-1667
    DOI 10.1016/j.xpro.2022.101603
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Combined Nanofiltration and Thermocatalysis for the Simultaneous Degradation of Micropollutants, Fouling Mitigation and Water Purification.

    Janowska, Katarzyna / Ma, Xianzheng / Boffa, Vittorio / Jørgensen, Mads Koustrup / Candelario, Victor M

    Membranes

    2021  Volume 11, Issue 8

    Abstract: Due to progressive limitation of access to clean drinkable water, it is nowadays a priority to find an effective method of water purification from those emerging organic contaminants, which might have potentially harmful and irreversible effects on ... ...

    Abstract Due to progressive limitation of access to clean drinkable water, it is nowadays a priority to find an effective method of water purification from those emerging organic contaminants, which might have potentially harmful and irreversible effects on living organisms and environment. This manuscript reports the development of a new strategy for water purification, which combines a novel and recently developed Al
    Language English
    Publishing date 2021-08-19
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2614641-1
    ISSN 2077-0375
    ISSN 2077-0375
    DOI 10.3390/membranes11080639
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Structure-Based Stabilization of SOSIP Env Enhances Recombinant Ectodomain Durability and Yield.

    Wrapp, Daniel / Mu, Zekun / Thakur, Bhishem / Janowska, Katarzyna / Ajayi, Oluwatobi / Barr, Maggie / Parks, Robert / Mansouri, Katayoun / Edwards, Robert J / Hahn, Beatrice H / Acharya, Priyamvada / Saunders, Kevin O / Haynes, Barton F

    Journal of virology

    2023  Volume 97, Issue 1, Page(s) e0167322

    Abstract: The envelope glycoprotein (Env) is the main focus of human immunodeficiency virus type 1 (HIV-1) vaccine development due to its critical role in viral entry. Despite advances in protein engineering, many Env proteins remain recalcitrant to recombinant ... ...

    Abstract The envelope glycoprotein (Env) is the main focus of human immunodeficiency virus type 1 (HIV-1) vaccine development due to its critical role in viral entry. Despite advances in protein engineering, many Env proteins remain recalcitrant to recombinant expression due to their inherent metastability, making biochemical and immunological experiments impractical or impossible. Here, we report a novel proline stabilization strategy to facilitate the production of prefusion Env trimers. This approach, termed "2P," works synergistically with previously described SOSIP mutations and dramatically increases the yield of recombinantly expressed Env ectodomains without altering the antigenic or conformational properties of near-native Env. We determined that the 2P mutations function by enhancing the durability of the prefusion conformation and that this stabilization strategy is broadly applicable to evolutionarily and antigenically diverse Env constructs. These findings provide a new Env stabilization platform to facilitate biochemical research and expand the number of Env variants that can be developed as future HIV-1 vaccine candidates.
    MeSH term(s) Humans ; env Gene Products, Human Immunodeficiency Virus/genetics ; Glycoproteins/genetics ; HIV Infections ; Molecular Conformation ; Protein Engineering ; Protein Multimerization ; Recombinant Proteins/genetics ; HIV-1/genetics
    Chemical Substances env Gene Products, Human Immunodeficiency Virus ; Glycoproteins ; Recombinant Proteins
    Language English
    Publishing date 2023-01-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.01673-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 609: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article: Surfactant-Assisted Fabrication of Alumina-Doped Amorphous Silica Nanofiltration Membranes with Enhanced Water Purification Performances.

    Ma, Xianzheng / Janowska, Katarzyna / Boffa, Vittorio / Fabbri, Debora / Magnacca, Giuliana / Calza, Paola / Yue, Yuanzheng

    Nanomaterials (Basel, Switzerland)

    2019  Volume 9, Issue 10

    Abstract: Surfactant-templated 5 mol% ... ...

    Abstract Surfactant-templated 5 mol% Al
    Language English
    Publishing date 2019-09-24
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2662255-5
    ISSN 2079-4991
    ISSN 2079-4991
    DOI 10.3390/nano9101368
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: SARS-CoV-2 Omicron XBB lineage spike structures, conformations, antigenicity, and receptor recognition.

    Zhang, Qianyi E / Lindenberger, Jared / Parsons, Ruth / Thakur, Bhishem / Parks, Rob / Park, Chan Soo / Huang, Xiao / Sammour, Salam / Janowska, Katarzyna / Spence, Taylor N / Edwards, Robert J / Martin, Mitchell / Williams, Wilton B / Gobeil, Sophie / Montefiori, David C / Korber, Bette / Saunders, Kevin O'Neil / Haynes, Barton F / Henderson, Rory /
    Acharya, Priyamvada

    bioRxiv : the preprint server for biology

    2024  

    Abstract: A recombinant lineage of the SARS-CoV-2 Omicron variant, named XBB, appeared in late 2022 and evolved descendants that successively swept local and global populations. XBB lineage members were noted for their improved immune evasion and transmissibility. ...

    Abstract A recombinant lineage of the SARS-CoV-2 Omicron variant, named XBB, appeared in late 2022 and evolved descendants that successively swept local and global populations. XBB lineage members were noted for their improved immune evasion and transmissibility. Here, we determine cryo-EM structures of XBB.1.5, XBB.1.16, EG.5 and EG.5.1 spike (S) ectodomains to reveal reinforced 3-RBD-down receptor inaccessible closed states mediated by interprotomer receptor binding domain (RBD) interactions previously observed in BA.1 and BA.2. Improved XBB.1.5 and XBB.1.16 RBD stability compensated for stability loss caused by early Omicron mutations, while the F456L substitution reduced EG.5 RBD stability. S1 subunit mutations had long-range impacts on conformation and epitope presentation in the S2 subunit. Our results reveal continued S protein evolution via simultaneous optimization of multiple parameters including stability, receptor binding and immune evasion, and the dramatic effects of relatively few residue substitutions in altering the S protein conformational landscape.
    Language English
    Publishing date 2024-03-12
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.02.12.580004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Conformational flexibility of HIV-1 envelope glycoproteins modulates transmitted / founder sensitivity to broadly neutralizing antibodies.

    Parthasarathy, Durgadevi / Pothula, Karunakar Reddy / Dam, Kim-Marie A / Ratnapriya, Sneha / Benet, Héctor Cervera / Parsons, Ruth / Huang, Xiao / Sammour, Salam / Janowska, Katarzyna / Harris, Miranda / Sacco, Samuel / Sodroski, Joseph / Bridges, Michael D / Hubbell, Wayne L / Acharya, Priyamvada / Herschhorn, Alon

    bioRxiv : the preprint server for biology

    2023  

    Abstract: HIV-1 envelope glycoproteins (Envs) mediate viral entry and are the sole target of neutralizing antibodies. Envs of most primary HIV-1 strains exist in a closed conformation and occasionally sample more open states. Thus, current knowledge guides ... ...

    Abstract HIV-1 envelope glycoproteins (Envs) mediate viral entry and are the sole target of neutralizing antibodies. Envs of most primary HIV-1 strains exist in a closed conformation and occasionally sample more open states. Thus, current knowledge guides immunogen design to mimic the closed Env conformation as the preferred target for eliciting broadly neutralizing antibodies (bnAbs) to block HIV-1 entry. Here we show that Env-preferred conformations of 6 out of 13 (46%) transmitted/founder (T/F) strains tested are incompletely closed. As a result, entry of these T/Fs into target cells is sensitive to antibodies that recognize internal epitopes exposed on open Env conformations. A cryo-electron microscopy structure of unliganded, incompletely closed T/F Envs (1059-SOSIP) at 3.6 Å resolution exhibits an asymmetric configuration of Env protomers with increased sampling of states with incompletely closed trimer apex. Double electron-electron resonance spectroscopy provided further evidence for enriched occupancy of more open Env conformations. Consistent with conformational flexibility, 1059 Envs were associated with resistance to most bnAbs that exhibit reduced potency against functional Env intermediates. To follow the fate of incompletely closed Env in patients, we reconstructed
    Language English
    Publishing date 2023-12-05
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.09.13.557082
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Glycans on the SARS-CoV-2 Spike Control the Receptor Binding Domain Conformation.

    Henderson, Rory / Edwards, Robert J / Mansouri, Katayoun / Janowska, Katarzyna / Stalls, Victoria / Kopp, Megan / Haynes, Barton F / Acharya, Priyamvada

    bioRxiv : the preprint server for biology

    2020  

    Abstract: The glycan shield of the beta-coronavirus (β-CoV) Spike (S) glycoprotein provides protection from host immune responses, acting as a steric block to potentially neutralizing antibody responses. The conformationally dynamic S-protein is the primary ... ...

    Abstract The glycan shield of the beta-coronavirus (β-CoV) Spike (S) glycoprotein provides protection from host immune responses, acting as a steric block to potentially neutralizing antibody responses. The conformationally dynamic S-protein is the primary immunogenic target of vaccine design owing to its role in host-cell fusion, displaying multiple receptor binding domain (RBD) 'up' and 'down' state configurations. Here, we investigated the potential for RBD adjacent, N-terminal domain (NTD) glycans to influence the conformational equilibrium of these RBD states. Using a combination of antigenic screens and high-resolution cryo-EM structure determination, we show that an N-glycan deletion at position 234 results in a dramatically reduced population of the 'up' state RBD position. Conversely, glycan deletion at position N165 results in a discernable increase in 'up' state RBDs. This indicates the glycan shield acts not only as a passive hinderance to antibody meditated immunity but also as a conformational control element. Together, our results demonstrate this highly dynamic conformational machine is responsive to glycan modification with implications in viral escape and vaccine design.
    Keywords covid19
    Language English
    Publishing date 2020-06-30
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2020.06.26.173765
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Effect of natural mutations of SARS-CoV-2 on spike structure, conformation and antigenicity.

    Gobeil, Sophie M-C / Janowska, Katarzyna / McDowell, Shana / Mansouri, Katayoun / Parks, Robert / Stalls, Victoria / Kopp, Megan F / Manne, Kartik / Saunders, Kevin / Edwards, Robert J / Haynes, Barton F / Henderson, Rory C / Acharya, Priyamvada

    bioRxiv : the preprint server for biology

    2021  

    Abstract: New SARS-CoV-2 variants that have accumulated multiple mutations in the spike (S) glycoprotein enable increased transmission and resistance to neutralizing antibodies. Here, we study the antigenic and structural impacts of the S protein mutations from ... ...

    Abstract New SARS-CoV-2 variants that have accumulated multiple mutations in the spike (S) glycoprotein enable increased transmission and resistance to neutralizing antibodies. Here, we study the antigenic and structural impacts of the S protein mutations from four variants, one that was involved in transmission between minks and humans, and three that rapidly spread in human populations and originated in the United Kingdom, Brazil or South Africa. All variants either retained or improved binding to the ACE2 receptor. The B.1.1.7 (UK) and B.1.1.28 (Brazil) spike variants showed reduced binding to neutralizing NTD and RBD antibodies, respectively, while the B.1.351 (SA) variant showed reduced binding to both NTD- and RBD-directed antibodies. Cryo-EM structural analyses revealed allosteric effects of the mutations on spike conformations and revealed mechanistic differences that either drive inter-species transmission or promotes viral escape from dominant neutralizing epitopes.
    Highlights: Cryo-EM structures reveal changes in SARS-CoV-2 S protein during inter-species transmission or immune evasion.Adaptation to mink resulted in increased ACE2 binding and spike destabilization.B.1.1.7 S mutations reveal an intricate balance of stabilizing and destabilizing effects that impact receptor and antibody binding.E484K mutation in B.1.351 and B.1.1.28 S proteins drives immune evasion by altering RBD conformation.S protein uses different mechanisms to converge upon similar solutions for altering RBD up/down positioning.
    Language English
    Publishing date 2021-03-15
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2021.03.11.435037
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Sequence and functional characterization of a public HIV-specific antibody clonotype.

    Murji, Amyn A / Raju, Nagarajan / Qin, Juliana S / Kaldine, Haajira / Janowska, Katarzyna / Fechter, Emilee Friedman / Mapengo, Rutendo / Scheepers, Cathrine / Setliff, Ian / Acharya, Priyamvada / Morris, Lynn / Georgiev, Ivelin S

    iScience

    2021  Volume 25, Issue 1, Page(s) 103564

    Abstract: Public antibody clonotypes shared among multiple individuals have been identified for several pathogens. However, little is known about the determinants of antibody "publicness". Here, we characterize the sequence and functional properties of antibodies ... ...

    Abstract Public antibody clonotypes shared among multiple individuals have been identified for several pathogens. However, little is known about the determinants of antibody "publicness". Here, we characterize the sequence and functional properties of antibodies from a public clonotype targeting the CD4 binding site on HIV-1 Env. Our results showed that HIV-1 specificity for the public antibodies studied here, comprising sequences from three individuals, was modulated by the V
    Language English
    Publishing date 2021-12-03
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2021.103564
    Database MEDical Literature Analysis and Retrieval System OnLINE

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