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  1. Article ; Online: pH-dependent conformation of multimeric von Willebrand factor.

    Smith, Ian W / Parker, Ernest T / Lollar, Pete

    Blood advances

    2023  Volume 7, Issue 11, Page(s) 2554–2557

    MeSH term(s) Humans ; von Willebrand Factor ; von Willebrand Diseases ; Factor VIII ; Molecular Conformation ; Hydrogen-Ion Concentration
    Chemical Substances von Willebrand Factor ; Factor VIII (9001-27-8)
    Language English
    Publishing date 2023-01-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2915908-8
    ISSN 2473-9537 ; 2473-9529
    ISSN (online) 2473-9537
    ISSN 2473-9529
    DOI 10.1182/bloodadvances.2022009359
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 7153: Show issues Location:
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  2. Article ; Online: Measurement of the Translational Diffusion Coefficient and Hydrodynamic Radius of Proteins by Dynamic Light Scattering.

    Parker, Ernest T / Lollar, Pete

    Bio-protocol

    2021  Volume 11, Issue 20, Page(s) e4195

    Abstract: Diffusion is a fundamental process in biological systems that governs the molecular collisions driving biochemical reactions and membrane and transport. Measurement of the diffusion coefficient and application of the Stokes-Einstein equation produces the ...

    Abstract Diffusion is a fundamental process in biological systems that governs the molecular collisions driving biochemical reactions and membrane and transport. Measurement of the diffusion coefficient and application of the Stokes-Einstein equation produces the hydrodynamic radius, which is a commonly used gauge of particle size. Additionally, measurement of the diffusion coefficient and the sedimentation coefficient, and application of the Svedberg equation, yields the molecular weight, which is particularly useful in the characterization of very large macromolecules. Dynamic light scattering (DLS) is the most common method to measure the diffusion coefficient of macromolecules. We describe a procedure to perform DLS measurements on monomeric bovine serum albumin (BSA) purified by size-exclusion chromatography using the Zetasizer Nano S particle size analyzer. We compare several analytical methods in existing software programs to estimate the diffusion coefficient of BSA (extrapolated to water at 20°C at infinite dilution,
    Language English
    Publishing date 2021-10-20
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2833269-6
    ISSN 2331-8325 ; 2331-8325
    ISSN (online) 2331-8325
    ISSN 2331-8325
    DOI 10.21769/BioProtoc.4195
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Conformation of the von Willebrand factor/factor VIII complex in quasi-static flow.

    Parker, Ernest T / Lollar, Pete

    The Journal of biological chemistry

    2021  Volume 296, Page(s) 100420

    Abstract: Von Willebrand factor (VWF) is a plasma glycoprotein that circulates noncovalently bound to blood coagulation factor VIII (fVIII). VWF is a population of multimers composed of a variable number of ∼280 kDa monomers that is activated in shear flow to bind ...

    Abstract Von Willebrand factor (VWF) is a plasma glycoprotein that circulates noncovalently bound to blood coagulation factor VIII (fVIII). VWF is a population of multimers composed of a variable number of ∼280 kDa monomers that is activated in shear flow to bind collagen and platelet glycoprotein Ibα. Electron microscopy, atomic force microscopy, small-angle neutron scattering, and theoretical studies have produced a model in which the conformation of VWF under static conditions is a compact, globular "ball-of-yarn," implying strong, attractive forces between monomers. We performed sedimentation velocity (SV) analytical ultracentrifugation measurements on unfractionated VWF/fVIII complexes. There was a 20% per mg/ml decrease in the weight-average sedimentation coefficient, s
    MeSH term(s) Blood Platelets/metabolism ; Collagen ; Drug Combinations ; Factor VIII/isolation & purification ; Factor VIII/metabolism ; Factor VIII/pharmacology ; Factor VIII/physiology ; Humans ; Molecular Conformation ; Molecular Weight ; Plasma/chemistry ; Scattering, Small Angle ; Ultracentrifugation ; von Willebrand Factor/isolation & purification ; von Willebrand Factor/metabolism ; von Willebrand Factor/pharmacology ; von Willebrand Factor/physiology
    Chemical Substances Drug Combinations ; factor VIII, von Willebrand factor drug combination ; von Willebrand Factor ; Factor VIII (9001-27-8) ; Collagen (9007-34-5)
    Language English
    Publishing date 2021-02-16
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2021.100420
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  4. Article ; Online: Fill 'er up? Fill what up?

    Lollar, Pete

    Blood

    2016  Volume 128, Issue 2, Page(s) 156–157

    Language English
    Publishing date 2016-07-13
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood-2016-05-713040
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Subunit Flexibility of Multimeric von Willebrand Factor/Factor VIII Complexes.

    Parker, Ernest T / Haberichter, Sandra L / Lollar, Pete

    ACS omega

    2022  Volume 7, Issue 35, Page(s) 31183–31196

    Abstract: Von Willebrand factor (VWF) is a plasma glycoprotein that participates in platelet adhesion and aggregation and serves as a carrier for blood coagulation factor VIII (fVIII). Plasma VWF consists of a population of multimers that range in molecular weight ...

    Abstract Von Willebrand factor (VWF) is a plasma glycoprotein that participates in platelet adhesion and aggregation and serves as a carrier for blood coagulation factor VIII (fVIII). Plasma VWF consists of a population of multimers that range in molecular weight from ∼ 0.55 MDa to greater than 10 MDa. The VWF multimer consists of a variable number of concatenated disulfide-linked ∼275 kDa subunits. We fractionated plasma-derived human VWF/fVIII complexes by size-exclusion chromatography at a pH of 7.4 and subjected them to analysis by sodium dodecyl sulfate agarose gel electrophoresis, sedimentation velocity analytical ultracentrifugation (SV AUC), dynamic light scattering (DLS), and multi-angle light scattering (MALS). Weight-average molecular weights,
    Language English
    Publishing date 2022-08-25
    Publishing country United States
    Document type Journal Article
    ISSN 2470-1343
    ISSN (online) 2470-1343
    DOI 10.1021/acsomega.2c03389
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  6. Article ; Online: High stakes immunology.

    Lollar, Pete

    Blood

    2011  Volume 118, Issue 13, Page(s) 3455–3456

    Language English
    Publishing date 2011-09-29
    Publishing country United States
    Document type Comment ; Journal Article
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood-2011-07-366161
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Mechanism of glycoform specificity and protection against antibody dependent enhancement by an anti-afucosylated IgG nanobody.

    Gupta, Aaron / Kao, Kevin / Yamin, Rachel / Oren, Deena A / Goldgur, Yehuda / Du, Jonathan / Lollar, Pete / Sundberg, Eric J / Ravetch, Jeffrey V

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Immunoglobulin G (IgG) antibodies contain a single, ... ...

    Abstract Immunoglobulin G (IgG) antibodies contain a single, complex
    Language English
    Publishing date 2023-01-24
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.01.23.525277
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Mechanism of glycoform specificity and in vivo protection by an anti-afucosylated IgG nanobody.

    Gupta, Aaron / Kao, Kevin S / Yamin, Rachel / Oren, Deena A / Goldgur, Yehuda / Du, Jonathan / Lollar, Pete / Sundberg, Eric J / Ravetch, Jeffrey V

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 2853

    Abstract: Immunoglobulin G (IgG) antibodies contain a complex N-glycan embedded in the hydrophobic pocket between its heavy chain protomers. This glycan contributes to the structural organization of the Fc domain and determines its specificity for Fcγ receptors, ... ...

    Abstract Immunoglobulin G (IgG) antibodies contain a complex N-glycan embedded in the hydrophobic pocket between its heavy chain protomers. This glycan contributes to the structural organization of the Fc domain and determines its specificity for Fcγ receptors, thereby dictating distinct cellular responses. The variable construction of this glycan structure leads to highly-related, but non-equivalent glycoproteins known as glycoforms. We previously reported synthetic nanobodies that distinguish IgG glycoforms. Here, we present the structure of one such nanobody, X0, in complex with the Fc fragment of afucosylated IgG1. Upon binding, the elongated CDR3 loop of X0 undergoes a conformational shift to access the buried N-glycan and acts as a 'glycan sensor', forming hydrogen bonds with the afucosylated IgG N-glycan that would otherwise be sterically hindered by the presence of a core fucose residue. Based on this structure, we designed X0 fusion constructs that disrupt pathogenic afucosylated IgG1-FcγRIIIa interactions and rescue mice in a model of dengue virus infection.
    MeSH term(s) Animals ; Mice ; Immunoglobulin G ; Glycosylation ; Receptors, IgG/metabolism ; Immunoglobulin Fc Fragments/metabolism ; Polysaccharides/chemistry
    Chemical Substances Immunoglobulin G ; Receptors, IgG ; Immunoglobulin Fc Fragments ; Polysaccharides
    Language English
    Publishing date 2023-05-18
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; 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/s41467-023-38453-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Factor VIII antibody immune complexes modulate the humoral response to factor VIII in an epitope-dependent manner.

    Batsuli, Glaivy / Ito, Jasmine / York, Elizabeth S / Cox, Courtney / Baldwin, Wallace / Gill, Surinder / Lollar, Pete / Meeks, Shannon L

    Frontiers in immunology

    2023  Volume 14, Page(s) 1233356

    Abstract: Introduction: Soluble antigens complexed with immunoglobulin G (IgG) antibodies can induce robust adaptive immune responses : Methods: In this study, we analyzed internalization of FVIII complexed with epitope-mapped FVIII-specific IgG monoclonal ... ...

    Abstract Introduction: Soluble antigens complexed with immunoglobulin G (IgG) antibodies can induce robust adaptive immune responses
    Methods: In this study, we analyzed internalization of FVIII complexed with epitope-mapped FVIII-specific IgG monoclonal antibodies (MAbs) by murine bone marrow-derived dendritic cells (BMDCs)
    Results: FVIII complexed with 2-116 (A1 domain MAb), 2-113 (A3 domain MAb), and I55 (C2 domain MAb) significantly increased FVIII uptake by BMDC but only FVIII/2-116 enhanced antibody titers in FVIII
    Conclusion: These findings suggest that a subset of FVIII-IC modulates the humoral response to FVIII in an epitope-dependent manner, which may provide insight into the antibody response observed in some patients with hemophilia A.
    MeSH term(s) Animals ; Mice ; Factor VIII ; Antigen-Antibody Complex ; Hemophilia A ; Epitopes ; Hemostatics ; Immunoglobulin G
    Chemical Substances Factor VIII (9001-27-8) ; Antigen-Antibody Complex ; Epitopes ; Hemostatics ; Immunoglobulin G
    Language English
    Publishing date 2023-08-31
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2023.1233356
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Conformational activation and inhibition of von Willebrand factor by targeting its autoinhibitory module.

    Arce, Nicholas A / Markham-Lee, Zoe / Liang, Qian / Najmudin, Shabir / Legan, Emily R / Dean, Gabrielle / Su, Ally J / Wilson, Moriah S / Sidonio, Robert F / Lollar, Pete / Emsley, Jonas / Li, Renhao

    Blood

    2024  

    Abstract: Activation of von Willebrand factor (VWF) is a tightly controlled process governed primarily by local elements around its A1 domain. Recent studies suggest that the O-glycosylated sequences flanking the A1 domain constitute a discontinuous and force- ... ...

    Abstract Activation of von Willebrand factor (VWF) is a tightly controlled process governed primarily by local elements around its A1 domain. Recent studies suggest that the O-glycosylated sequences flanking the A1 domain constitute a discontinuous and force-sensitive autoinhibitory module (AIM), although its extent and conformation remains controversial. Here, we used a targeted screening strategy to identify two groups of nanobodies. One group, represented by clone 6D12, is conformation-insensitive and binds the N-terminal AIM (NAIM) sequence that is distal from A1. 6D12 activates human VWF and induces aggregation of platelet-rich plasma at submicromolar concentrations. The other group, represented by clones Nd4 and Nd6, is conformation-sensitive and targets the C-terminal AIM (CAIM). Nd4 and Nd6 inhibit ristocetin-induced platelet aggregation and reduce VWF-mediated platelet adhesion under flow. A crystal structure of Nd6 in complex with AIM-A1 shows a novel conformation of both CAIM and NAIM that are primed to interact, providing a model of steric hindrance stabilized by the AIM as the mechanism for regulating GPIbα binding to VWF. Hydrogen-deuterium exchange mass spectrometry analysis shows that binding of 6D12 induces the exposure of the GPIbα-binding site in the A1 domain, but binding of inhibitory nanobodies reduces it. Overall, these results suggest that the distal portion of NAIM is involved in specific interactions with CAIM, and that binding of nanobodies to the AIM could either disrupt its conformation to activate VWF or stabilize its conformation to upkeep VWF autoinhibition. These reported nanobodies could facilitate future studies of VWF functions and related pathologies.
    Language English
    Publishing date 2024-01-30
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood.2023022038
    Database MEDical Literature Analysis and Retrieval System OnLINE

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