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  1. Article: Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli.

    Jojoa-Cruz, Sebastian / Dubin, Adrienne E / Lee, Wen-Hsin / Ward, Andrew

    bioRxiv : the preprint server for biology

    2024  

    Abstract: The dimeric two-pore OSCA/TMEM63 family has recently been identified as mechanically activated ion channels. Previously, based on the unique features of the structure of OSCA1.2, we postulated the potential involvement of several structural elements in ... ...

    Abstract The dimeric two-pore OSCA/TMEM63 family has recently been identified as mechanically activated ion channels. Previously, based on the unique features of the structure of OSCA1.2, we postulated the potential involvement of several structural elements in sensing membrane tension
    Language English
    Publishing date 2024-03-04
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.10.03.560740
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Polynomial Fuzzy Observer-Based Feedback Control for Nonlinear Hyperbolic PDEs Systems.

    Tsai, Shun-Hung / Lee, Wen-Hsin / Tanaka, Kazuo / Chen, Ying-Jen / Lam, Hak-Keung

    IEEE transactions on cybernetics

    2024  Volume PP

    Abstract: This article explores the observer-based feedback control problem for a nonlinear hyperbolic partial differential equations (PDEs) system. Initially, the polynomial fuzzy hyperbolic PDEs (PFHPDEs) model is established through the utilization of the fuzzy ...

    Abstract This article explores the observer-based feedback control problem for a nonlinear hyperbolic partial differential equations (PDEs) system. Initially, the polynomial fuzzy hyperbolic PDEs (PFHPDEs) model is established through the utilization of the fuzzy identification approach, derived from the nonlinear hyperbolic PDEs model. Various types of state estimation and controller design problems for the polynomial fuzzy PDEs system are discussed concerning the state estimation problem. To investigate the relaxed stability problem, Euler's homogeneous theorem, Lyapunov-Krasovskii functional with polynomial matrices (LKFPM), and the sum-of-squares (SOSs) approach are adopted. The exponential stabilization condition is formulated in terms of the spatial-derivative-SOSs (SD-SOSs). Additionally, a segmental algorithm is developed to find the feasible solution for the SD-SOS condition. Finally, a hyperbolic PDEs system and several numerical examples are provided to illustrate the validity and effectiveness of the proposed results.
    Language English
    Publishing date 2024-02-07
    Publishing country United States
    Document type Journal Article
    ISSN 2168-2275
    ISSN (online) 2168-2275
    DOI 10.1109/TCYB.2024.3352656
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli.

    Jojoa-Cruz, Sebastian / Dubin, Adrienne E / Lee, Wen-Hsin / Ward, Andrew B

    eLife

    2024  Volume 12

    Abstract: The dimeric two-pore OSCA/TMEM63 family has recently been identified as mechanically activated ion channels. Previously, based on the unique features of the structure of OSCA1.2, we postulated the potential involvement of several structural elements in ... ...

    Abstract The dimeric two-pore OSCA/TMEM63 family has recently been identified as mechanically activated ion channels. Previously, based on the unique features of the structure of OSCA1.2, we postulated the potential involvement of several structural elements in sensing membrane tension (Jojoa-Cruz et al., 2018). Interestingly, while OSCA1, 2, and 3 clades are activated by membrane stretch in cell-attached patches (i.e. they are stretch-activated channels), they differ in their ability to transduce membrane deformation induced by a blunt probe (poking). Here, in an effort to understand the domains contributing to mechanical signal transduction, we used cryo-electron microscopy to solve the structure of
    MeSH term(s) Cryoelectron Microscopy ; Arabidopsis/genetics ; Cell Membrane ; Mechanotransduction, Cellular ; Mutagenesis
    Language English
    Publishing date 2024-04-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.93147
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain.

    Jojoa-Cruz, Sebastian / Burendei, Batuujin / Lee, Wen-Hsin / Ward, Andrew B

    Structure (London, England : 1993)

    2023  Volume 32, Issue 2, Page(s) 157–167.e5

    Abstract: Members of the OSCA/TMEM63 family are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are potentially involved in mechanosensation. However, these ... ...

    Abstract Members of the OSCA/TMEM63 family are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are potentially involved in mechanosensation. However, these structures are all in a similar state and information about the motion of different elements of the structure is limited, preventing a deeper understanding of how these channels work. Here, we used cryoelectron microscopy to determine high-resolution structures of Arabidopsis thaliana OSCA1.2 and OSCA2.3 in peptidiscs. The structure of OSCA1.2 matches previous structures of the same protein in different environments. Yet, in OSCA2.3, the TM6a-TM7 linker adopts a different conformation that constricts the pore on its cytoplasmic side. Furthermore, coevolutionary sequence analysis uncovered a conserved interaction between the TM6a-TM7 linker and the beam-like domain (BLD). Our results reveal conformational heterogeneity and differences in conserved interactions between the TMD and BLD among members of the OSCA family.
    MeSH term(s) Cryoelectron Microscopy ; Ion Channels/metabolism ; Arabidopsis/genetics ; Arabidopsis/metabolism ; Protein Domains ; Arabidopsis Proteins/chemistry ; Calcium Channels/metabolism
    Chemical Substances Ion Channels ; Arabidopsis Proteins ; OSCA1 protein, Arabidopsis ; Calcium Channels
    Language English
    Publishing date 2023-12-15
    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.2023.11.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain.

    Jojoa-Cruz, Sebastian / Burendei, Batuujin / Lee, Wen-Hsin / Ward, Andrew B

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Members of the OSCA/TMEM63 are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are potentially involved in mechanosensation. However, these structures ... ...

    Abstract Members of the OSCA/TMEM63 are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are potentially involved in mechanosensation. However, these structures are all in a similar state and information about the motion of different elements of the structure is limited, preventing a deeper understanding of how these channels work. Here, we used cryo-electron microscopy to determine high resolution structures of
    Language English
    Publishing date 2023-06-15
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.06.15.545135
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: HIV envelope trimers and gp120 as immunogens to induce broadly neutralizing antibodies in cows.

    Altman, Pilar X / Parren, Mara / Sang, Huldah / Ozorowski, Gabriel / Lee, Wen-Hsin / Smider, Vaughn V / Wilson, Ian A / Ward, Andrew B / Mwangi, Waithaka / Burton, Dennis R / Sok, Devin

    bioRxiv : the preprint server for biology

    2024  

    Abstract: The study of immunogens capable of eliciting broadly neutralizing antibodies (bnAbs) is crucial for the development of an HIV vaccine. To date, only cows, making use of their ultralong CDRH3 loops, have reliably elicited bnAbs following immunization with ...

    Abstract The study of immunogens capable of eliciting broadly neutralizing antibodies (bnAbs) is crucial for the development of an HIV vaccine. To date, only cows, making use of their ultralong CDRH3 loops, have reliably elicited bnAbs following immunization with HIV Envelope trimers. Antibody responses to the CD4 binding site have been readily elicited by immunization of cows with a stabilized Env trimer of the BG505 strain and, with more difficulty, to the V2-apex region of Env with a cocktail of trimers. Here, we sought to determine whether the BG505 Env trimer could be engineered to generate new bnAb specificities in cows. Since the cow CD4 binding site bnAbs bind to monomeric BG505 gp120, we also sought to determine whether gp120 immunization alone might be sufficient to induce bnAbs. We found that engineering the CD4 binding site by mutation of a key binding residue of BG505 HIV Env resulted in a reduced bnAb response that took more immunizations to develop. Monoclonal antibodies isolated from one animal were directed to the V2-apex, suggesting a re-focusing of the bnAb response. Immunization with monomeric BG505 g120 generated no serum bnAb responses, indicating that the ultralong CDRH3 bnAbs are only elicited in the context of the trimer in the absence of many other less restrictive epitopes presented on monomeric gp120. The results support the notion of a hierarchy of epitopes on HIV Env and suggest that, even with the presence in the cow repertoire of ultralong CDRH3s, bnAb epitopes are relatively disfavored.
    Language English
    Publishing date 2024-03-25
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.03.20.585065
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Conjugation of a Toll-Like Receptor Agonist to Glycans of an HIV Native-Like Envelope Trimer Preserves Neutralization Epitopes.

    Li, Zeshi / Derking, Ronald / Lee, Wen-Hsin / Bosman, Gerlof P / Ward, Andrew B / Sanders, Rogier W / Boons, Geert-Jan

    Chembiochem : a European journal of chemical biology

    2022  Volume 23, Issue 16, Page(s) e202200236

    Abstract: Small molecule adjuvants are attractive for enhancing broad protection and durability of immune responses elicited by subunit vaccines. Covalent attachment of an adjuvant to an immunogen is particularly attractive because it simultaneously delivers both ... ...

    Abstract Small molecule adjuvants are attractive for enhancing broad protection and durability of immune responses elicited by subunit vaccines. Covalent attachment of an adjuvant to an immunogen is particularly attractive because it simultaneously delivers both entities to antigen presenting cells resulting in more efficient immune activation. There is, however, a lack of methods to conjugate small molecule immune potentiators to viral glycoprotein immunogens without compromising epitope integrity. We describe herein a one-step enzymatic conjugation approach for the covalent attachment of small molecule adjuvants to N-linked glycans of viral glycoproteins. It involves the attachment of an immune potentiator to CMP-Neu5AcN
    MeSH term(s) Adjuvants, Immunologic ; Antibodies, Neutralizing ; Epitopes ; Glycoproteins ; HIV Antibodies ; HIV Infections ; HIV-1 ; Humans ; Polysaccharides/pharmacology ; Toll-Like Receptors/agonists ; env Gene Products, Human Immunodeficiency Virus/chemistry
    Chemical Substances Adjuvants, Immunologic ; Antibodies, Neutralizing ; Epitopes ; Glycoproteins ; HIV Antibodies ; Polysaccharides ; Toll-Like Receptors ; env Gene Products, Human Immunodeficiency Virus
    Language English
    Publishing date 2022-06-20
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2020469-3
    ISSN 1439-7633 ; 1439-4227
    ISSN (online) 1439-7633
    ISSN 1439-4227
    DOI 10.1002/cbic.202200236
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Defining bottlenecks and opportunities for Lassa virus neutralization by structural profiling of vaccine-induced polyclonal antibody responses.

    Brouwer, Philip J M / Perrett, Hailee R / Beaumont, Tim / Nijhuis, Haye / Kruijer, Sabine / Burger, Judith A / Lee, Wen-Hsin / Müller-Kraüter, Helena / Sanders, Rogier W / Strecker, Thomas / van Gils, Marit J / Ward, Andrew B

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Lassa fever continues to be a major public health burden in endemic countries in West Africa, yet effective therapies or vaccines are lacking. The isolation of potent and protective neutralizing antibodies against the Lassa virus glycoprotein complex ( ... ...

    Abstract Lassa fever continues to be a major public health burden in endemic countries in West Africa, yet effective therapies or vaccines are lacking. The isolation of potent and protective neutralizing antibodies against the Lassa virus glycoprotein complex (GPC) justifies the development of vaccines that can elicit strong neutralizing antibody responses. However, Lassa vaccines candidates have generally been unsuccessful in doing so and the associated antibody responses to these vaccines remain poorly characterized. Here, we establish an electron-microscopy based epitope mapping pipeline that enables high-resolution structural characterization of polyclonal antibodies to GPC. By applying this method to rabbits vaccinated with a recombinant GPC vaccine and a GPC-derived virus-like particle, we reveal determinants of neutralization which involve epitopes of the GPC-C, GPC-A, and GP1-A competition clusters. Furthermore, by identifying previously undescribed immunogenic off-target epitopes, we expose challenges that recombinant GPC vaccines face. By enabling detailed polyclonal antibody characterization, our work ushers in a next generation of more rational Lassa vaccine design.
    Language English
    Publishing date 2023-12-23
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.12.21.572918
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Conformational antigenic heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.

    Colin, Philippe / Ringe, Rajesh P / Yasmeen, Anila / Ozorowski, Gabriel / Ketas, Thomas J / Lee, Wen-Hsin / Ward, Andrew B / Moore, John P / Klasse, P J

    Research square

    2023  

    Abstract: ... ...

    Abstract Background
    Language English
    Publishing date 2023-02-24
    Publishing country United States
    Document type Preprint
    DOI 10.21203/rs.3.rs-2613503/v1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Structural basis of epitope selectivity and potent protection from malaria by PfCSP antibody L9.

    Martin, Gregory M / Fernández-Quintero, Monica L / Lee, Wen-Hsin / Pholcharee, Tossapol / Eshun-Wilson, Lisa / Liedl, Klaus R / Pancera, Marie / Seder, Robert A / Wilson, Ian A / Ward, Andrew B

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 2815

    Abstract: A primary objective in malaria vaccine design is the generation of high-quality antibody responses against the circumsporozoite protein of the malaria parasite, Plasmodium falciparum (PfCSP). To enable rational antigen design, we solved a cryo-EM ... ...

    Abstract A primary objective in malaria vaccine design is the generation of high-quality antibody responses against the circumsporozoite protein of the malaria parasite, Plasmodium falciparum (PfCSP). To enable rational antigen design, we solved a cryo-EM structure of the highly potent anti-PfCSP antibody L9 in complex with recombinant PfCSP. We found that L9 Fab binds multivalently to the minor (NPNV) repeat domain, which is stabilized by a unique set of affinity-matured homotypic, antibody-antibody contacts. Molecular dynamics simulations revealed a critical role of the L9 light chain in integrity of the homotypic interface, which likely impacts PfCSP affinity and protective efficacy. These findings reveal the molecular mechanism of the unique NPNV selectivity of L9 and emphasize the importance of anti-homotypic affinity maturation in protective immunity against P. falciparum.
    MeSH term(s) Humans ; Epitopes ; Protozoan Proteins/chemistry ; Malaria/prevention & control ; Malaria, Falciparum/prevention & control ; Malaria Vaccines ; Plasmodium falciparum ; Antibodies, Protozoan
    Chemical Substances Epitopes ; Protozoan Proteins ; Malaria Vaccines ; Antibodies, Protozoan
    Language English
    Publishing date 2023-05-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-38509-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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