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  1. Article ; Online: Structural Characterization of Pan-Ebolavirus Antibody 6D6 Targeting the Fusion Peptide of the Surface Glycoprotein.

    Milligan, Jacob C / Parekh, Diptiben V / Fuller, Katherine M / Igarashi, Manabu / Takada, Ayato / Saphire, Erica Ollmann

    The Journal of infectious diseases

    2018  Volume 219, Issue 3, Page(s) 415–419

    Abstract: Ebola virus infection causes severe disease in humans and represents a global health threat. Candidates for immunotherapeutics and vaccines have shown promise in clinical trials, although they are ineffective against other members of the Ebolavirus genus ...

    Abstract Ebola virus infection causes severe disease in humans and represents a global health threat. Candidates for immunotherapeutics and vaccines have shown promise in clinical trials, although they are ineffective against other members of the Ebolavirus genus that also cause periodic, lethal outbreaks. In this study, we present a crystal structure of a pan-ebolavirus antibody, 6D6, as well as single-particle electron microscopy reconstructions of 6D6 in complex with Ebola and Bundibugyo virus glycoproteins. 6D6 binds to the conserved glycoprotein fusion peptide, implicating it as a site of immune vulnerability that could be exploited to reliably elicit a pan-ebolavirus neutralizing antibody response.
    MeSH term(s) Antibodies, Neutralizing/immunology ; Antibodies, Viral/chemistry ; Antibodies, Viral/immunology ; Cross Reactions/immunology ; Ebolavirus/immunology ; Glycoproteins/chemistry ; Glycoproteins/immunology ; Hemorrhagic Fever, Ebola/immunology ; Hemorrhagic Fever, Ebola/virology ; Immunotherapy, Active ; Membrane Glycoproteins/immunology ; Models, Molecular ; Peptides ; Viral Fusion Proteins/chemistry ; Viral Fusion Proteins/immunology
    Chemical Substances Antibodies, Neutralizing ; Antibodies, Viral ; Glycoproteins ; Membrane Glycoproteins ; Peptides ; Viral Fusion Proteins
    Language English
    Publishing date 2018-09-03
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 3019-3
    ISSN 1537-6613 ; 0022-1899
    ISSN (online) 1537-6613
    ISSN 0022-1899
    DOI 10.1093/infdis/jiy532
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Rac1 promotes kidney collecting duct integrity by limiting actomyosin activity.

    Bock, Fabian / Elias, Bertha C / Dong, Xinyu / Parekh, Diptiben V / Mernaugh, Glenda / Viquez, Olga M / Hassan, Anjana / Amara, Venkateswara Rao / Liu, Jiageng / Brown, Kyle L / Terker, Andrew S / Chiusa, Manuel / Gewin, Leslie S / Fogo, Agnes B / Brakebusch, Cord H / Pozzi, Ambra / Zent, Roy

    The Journal of cell biology

    2021  Volume 220, Issue 11

    Abstract: A polarized collecting duct (CD), formed from the branching ureteric bud (UB), is a prerequisite for an intact kidney. The small Rho GTPase Rac1 is critical for actin cytoskeletal regulation. We investigated the role of Rac1 in the kidney collecting ... ...

    Abstract A polarized collecting duct (CD), formed from the branching ureteric bud (UB), is a prerequisite for an intact kidney. The small Rho GTPase Rac1 is critical for actin cytoskeletal regulation. We investigated the role of Rac1 in the kidney collecting system by selectively deleting it in mice at the initiation of UB development. The mice exhibited only a mild developmental phenotype; however, with aging, the CD developed a disruption of epithelial integrity and function. Despite intact integrin signaling, Rac1-null CD cells had profound adhesion and polarity abnormalities that were independent of the major downstream Rac1 effector, Pak1. These cells did however have a defect in the WAVE2-Arp2/3 actin nucleation and polymerization apparatus, resulting in actomyosin hyperactivity. The epithelial defects were reversible with direct myosin II inhibition. Furthermore, Rac1 controlled lateral membrane height and overall epithelial morphology by maintaining lateral F-actin and restricting actomyosin. Thus, Rac1 promotes CD epithelial integrity and morphology by restricting actomyosin via Arp2/3-dependent cytoskeletal branching.
    MeSH term(s) Actin Cytoskeleton/metabolism ; Actins/metabolism ; Actomyosin/metabolism ; Animals ; Cell Adhesion/physiology ; Cell Polarity/physiology ; Cells, Cultured ; Cytoskeleton/metabolism ; Epithelial Cells/metabolism ; Kidney Tubules, Collecting/metabolism ; Mice ; Mice, Inbred C57BL ; Myosin Type II/metabolism ; Neuropeptides/metabolism ; Signal Transduction/physiology ; rac1 GTP-Binding Protein/metabolism
    Chemical Substances Actins ; Neuropeptides ; Rac1 protein, mouse ; Actomyosin (9013-26-7) ; Myosin Type II (EC 3.6.1.-) ; rac1 GTP-Binding Protein (EC 3.6.5.2)
    Language English
    Publishing date 2021-10-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202103080
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Non-neutralizing Antibodies from a Marburg Infection Survivor Mediate Protection by Fc-Effector Functions and by Enhancing Efficacy of Other Antibodies.

    Ilinykh, Philipp A / Huang, Kai / Santos, Rodrigo I / Gilchuk, Pavlo / Gunn, Bronwyn M / Karim, Marcus M / Liang, Jenny / Fouch, Mallorie E / Davidson, Edgar / Parekh, Diptiben V / Kimble, James B / Pietzsch, Colette A / Meyer, Michelle / Kuzmina, Natalia A / Zeitlin, Larry / Saphire, Erica Ollmann / Alter, Galit / Crowe, James E / Bukreyev, Alexander

    Cell host & microbe

    2020  Volume 27, Issue 6, Page(s) 976–991.e11

    Abstract: Marburg virus (MARV) and Ebola virus (EBOV) belong to the family Filoviridae. MARV causes severe disease in humans with high fatality. We previously isolated a large panel of monoclonal antibodies (mAbs) from B cells of a human survivor with previous ... ...

    Abstract Marburg virus (MARV) and Ebola virus (EBOV) belong to the family Filoviridae. MARV causes severe disease in humans with high fatality. We previously isolated a large panel of monoclonal antibodies (mAbs) from B cells of a human survivor with previous naturally acquired MARV infection. Here, we characterized functional properties of these mAbs and identified non-neutralizing mAbs targeting the glycoprotein (GP) 2 portion of the mucin-like domain (MLD) of MARV GP, termed the wing region. One mAb targeting the GP2 wing, MR228, showed therapeutic protection in mice and guinea pigs infected with MARV. The protection was mediated by the Fc fragment functions of MR228. Binding of another GP2 wing-specific non-neutralizing mAb, MR235, to MARV GP increased accessibility of epitopes in the receptor-binding site (RBS) for neutralizing mAbs, resulting in enhanced virus neutralization by these mAbs. These findings highlight an important role for non-neutralizing mAbs during natural human MARV infection.
    MeSH term(s) Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; B-Lymphocytes ; Chlorocebus aethiops ; Disease Models, Animal ; Ebolavirus/immunology ; Epitopes/immunology ; Female ; Glycoproteins/immunology ; Guinea Pigs ; HEK293 Cells ; Humans ; Male ; Marburg Virus Disease/immunology ; Marburgvirus/immunology ; Mice ; Mice, Inbred BALB C ; Survivors ; THP-1 Cells ; Vero Cells ; Viral Envelope Proteins/immunology
    Chemical Substances Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Glycoproteins ; Viral Envelope Proteins
    Language English
    Publishing date 2020-04-21
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2278004-X
    ISSN 1934-6069 ; 1931-3128
    ISSN (online) 1934-6069
    ISSN 1931-3128
    DOI 10.1016/j.chom.2020.03.025
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Cdc42 regulates epithelial cell polarity and cytoskeletal function during kidney tubule development.

    Elias, Bertha C / Das, Amrita / Parekh, Diptiben V / Mernaugh, Glenda / Adams, Rebecca / Yang, Zhufeng / Brakebusch, Cord / Pozzi, Ambra / Marciano, Denise K / Carroll, Thomas J / Zent, Roy

    Journal of cell science

    2015  Volume 128, Issue 23, Page(s) 4293–4305

    Abstract: The Rho GTPase Cdc42 regulates key signaling pathways required for multiple cell functions, including maintenance of shape, polarity, proliferation, migration, differentiation and morphogenesis. Although previous studies have shown that Cdc42 is required ...

    Abstract The Rho GTPase Cdc42 regulates key signaling pathways required for multiple cell functions, including maintenance of shape, polarity, proliferation, migration, differentiation and morphogenesis. Although previous studies have shown that Cdc42 is required for proper epithelial development and maintenance, its exact molecular function in kidney development is not well understood. In this study, we define the specific role of Cdc42 during murine kidney epithelial tubulogenesis by deleting it selectively at the initiation of ureteric bud or metanephric mesenchyme development. Deletion in either lineage results in abnormal tubulogenesis, with profound defects in polarity, lumen formation and the actin cytoskeleton. Ultimately, these defects lead to renal failure. Additionally, in vitro analysis of Cdc42-null collecting duct cells shows that Cdc42 controls these processes by regulating the polarity Par complex (Par3-Par6-aPKC-Cdc42) and the cytoskeletal proteins N-Wasp and ezrin. Thus, we conclude that the principal role of Cdc42 in ureteric bud and metanephric mesenchyme development is to regulate epithelial cell polarity and the actin cytoskeleton.
    MeSH term(s) Animals ; Cell Polarity/physiology ; Cytoskeleton/genetics ; Cytoskeleton/metabolism ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Kidney Tubules/embryology ; Mice ; cdc42 GTP-Binding Protein/genetics ; cdc42 GTP-Binding Protein/metabolism
    Chemical Substances Cdc42 protein, mouse ; cdc42 GTP-Binding Protein (EC 3.6.5.2)
    Language English
    Publishing date 2015-12-01
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.164509
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Cdc42 promotes host defenses against fatal infection.

    Lee, Keunwook / Boyd, Kelli L / Parekh, Diptiben V / Kehl-Fie, Thomas E / Baldwin, H Scott / Brakebusch, Cord / Skaar, Eric P / Boothby, Mark / Zent, Roy

    Infection and immunity

    2013  Volume 81, Issue 8, Page(s) 2714–2723

    Abstract: The small Rho GTPase Cdc42 regulates key signaling pathways required for multiple cell functions, including maintenance of shape, polarity, proliferation, invasion, migration, differentiation, and morphogenesis. As the role of Cdc42-dependent signaling ... ...

    Abstract The small Rho GTPase Cdc42 regulates key signaling pathways required for multiple cell functions, including maintenance of shape, polarity, proliferation, invasion, migration, differentiation, and morphogenesis. As the role of Cdc42-dependent signaling in fibroblasts in vivo is unknown, we attempted to specifically delete it in these cells by crossing the Cdc42(fl/fl) mouse with an fibroblast-specific protein 1 (FSP1)-Cre mouse, which is thought to mediate recombination exclusively in fibroblasts. Surprisingly, the FSP1-Cre;Cdc42(fl/fl) mice died at 3 weeks of age due to overwhelming suppurative upper airway infections that were associated with neutrophilia and lymphopenia. Even though major aberrations in lymphoid tissue development were present in the mice, the principal cause of death was severe migration and killing abnormalities of the neutrophil population resulting in an inability to control infection. We also show that in addition to fibroblasts, FSP1-Cre deleted Cdc42 very efficiently in all leukocytes. Thus, by using this nonspecific Cre mouse, we inadvertently demonstrated the importance of Cdc42 in host protection from lethal infections and suggest a critical role for this small GTPase in innate immunity.
    MeSH term(s) Animals ; Chemotaxis, Leukocyte/immunology ; Fibroblasts/metabolism ; Flow Cytometry ; Immunity, Innate/immunology ; Immunoblotting ; Infections/immunology ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Neutrophils/immunology ; Neutrophils/metabolism ; cdc42 GTP-Binding Protein/immunology
    Chemical Substances cdc42 GTP-Binding Protein (EC 3.6.5.2)
    Language English
    Publishing date 2013-05-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 218698-6
    ISSN 1098-5522 ; 0019-9567
    ISSN (online) 1098-5522
    ISSN 0019-9567
    DOI 10.1128/IAI.01114-12
    Database MEDical Literature Analysis and Retrieval System OnLINE

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