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  1. Article ; Online: Sequencing, cloning, and antigen binding analysis of monoclonal antibodies isolated from single mouse B cells

    Charlotte Viant / Amelia Escolano / Spencer T. Chen / Michel C. Nussenzweig

    STAR Protocols, Vol 2, Iss 2, Pp 100389- (2021)

    2021  

    Abstract: Summary: The analysis of B cell receptors (BCR) from single B cells is crucial to understanding humoral immune responses. Here, we describe a protocol for the sequencing, cloning, and characterization of antibody genes that encode BCRs. We used this ... ...

    Abstract Summary: The analysis of B cell receptors (BCR) from single B cells is crucial to understanding humoral immune responses. Here, we describe a protocol for the sequencing, cloning, and characterization of antibody genes that encode BCRs. We used this method to analyze the BCRs of different mouse B cell populations for somatic hypermutations, clonal and phylogenic relationships, and their affinity for cognate antigen.For complete details on the use and execution of this protocol, please refer to Viant et al. (2020).
    Keywords Cell isolation ; Single cell ; Sequencing ; Immunology ; Molecular biology ; Antibody ; Science (General) ; Q1-390
    Language English
    Publishing date 2021-06-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Neutralizing antibodies induced in immunized macaques recognize the CD4-binding site on an occluded-open HIV-1 envelope trimer

    Zhi Yang / Kim-Marie A. Dam / Michael D. Bridges / Magnus A. G. Hoffmann / Andrew T. DeLaitsch / Harry B. Gristick / Amelia Escolano / Rajeev Gautam / Malcolm A. Martin / Michel C. Nussenzweig / Wayne L. Hubbell / Pamela J. Bjorkman

    Nature Communications, Vol 13, Iss 1, Pp 1-

    2022  Volume 14

    Abstract: Neutralizing antibodies (bNAbs) against HIV-1 are exclusively directed against the viral envelope protein (Env) and mainly target Env in a closed, prefusion state. Here, Yang et al. structurally characterize two heterologously-neutralizing CD4-binding ... ...

    Abstract Neutralizing antibodies (bNAbs) against HIV-1 are exclusively directed against the viral envelope protein (Env) and mainly target Env in a closed, prefusion state. Here, Yang et al. structurally characterize two heterologously-neutralizing CD4-binding site (CD4bs) antibodies isolated from sequentially immunized macaques, and show that these antibodies recognize the CD4bs on Env trimers in an „occluded-open‟ conformation between closed, as targeted by bNAbs, and fully-open, as recognized by CD4.
    Keywords Science ; Q
    Language English
    Publishing date 2022-02-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope

    Christopher O. Barnes / Harry B. Gristick / Natalia T. Freund / Amelia Escolano / Artem Y. Lyubimov / Harald Hartweger / Anthony P. West / Aina E. Cohen / Michel C. Nussenzweig / Pamela J. Bjorkman

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 12

    Abstract: Structure determination of glycosylated HIV-1 envelope (Env) trimers complexed with broadly neutralizing antibodies (bNAbs) promotes a better understanding of bNAb epitopes. Here the authors present the structures of natively-glycosylated Env in complex ... ...

    Abstract Structure determination of glycosylated HIV-1 envelope (Env) trimers complexed with broadly neutralizing antibodies (bNAbs) promotes a better understanding of bNAb epitopes. Here the authors present the structures of natively-glycosylated Env in complex with the highly-potent bNAb BG18, which is of interest for HIV-1 vaccine development.
    Keywords Science ; Q
    Language English
    Publishing date 2018-03-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope

    Christopher O. Barnes / Harry B. Gristick / Natalia T. Freund / Amelia Escolano / Artem Y. Lyubimov / Harald Hartweger / Anthony P. West / Aina E. Cohen / Michel C. Nussenzweig / Pamela J. Bjorkman

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 12

    Abstract: Structure determination of glycosylated HIV-1 envelope (Env) trimers complexed with broadly neutralizing antibodies (bNAbs) promotes a better understanding of bNAb epitopes. Here the authors present the structures of natively-glycosylated Env in complex ... ...

    Abstract Structure determination of glycosylated HIV-1 envelope (Env) trimers complexed with broadly neutralizing antibodies (bNAbs) promotes a better understanding of bNAb epitopes. Here the authors present the structures of natively-glycosylated Env in complex with the highly-potent bNAb BG18, which is of interest for HIV-1 vaccine development.
    Keywords Science ; Q
    Language English
    Publishing date 2018-03-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Comparative Analysis between the In Vivo Biodistribution and Therapeutic Efficacy of Adipose-Derived Mesenchymal Stromal Cells Administered Intraperitoneally in Experimental Colitis

    Mercedes Lopez-Santalla / Pablo Mancheño-Corvo / Amelia Escolano / Ramon Menta / Olga Delarosa / Juan M. Redondo / Juan A. Bueren / Wilfried Dalemans / Eleuterio Lombardo / Marina I. Garin

    International Journal of Molecular Sciences, Vol 19, Iss 7, p

    2018  Volume 1853

    Abstract: Mesenchymal stem cells (MSCs) have emerged as a promising treatment for inflammatory diseases. The immunomodulatory effect of MSCs takes place both by direct cell-to-cell contact and by means of soluble factors that leads to an increased accumulation of ... ...

    Abstract Mesenchymal stem cells (MSCs) have emerged as a promising treatment for inflammatory diseases. The immunomodulatory effect of MSCs takes place both by direct cell-to-cell contact and by means of soluble factors that leads to an increased accumulation of regulatory immune cells at the sites of inflammation. Similar efficacy of MSCs has been described regardless of the route of administration used, the inflammation conditions and the major histocompatibility complex context. These observations raise the question of whether the migration of the MSCs to the inflamed tissues is a pre-requisite to achieve their beneficial effect. To address this, we examined the biodistribution and the efficacy of intraperitoneal luciferase-expressing human expanded adipose-derived stem cells (Luci-eASCs) in a mouse model of colitis. Luci-eASC-infused mice were stratified according to their response to the Luci-eASC treatment. According to the stratification criteria, there was a tendency to increase the bioluminescence signal in the intestine at the expense of a decrease in the bioluminescence signal in the liver in the “responder” mice. These data thus suggest that the accumulation of the eASCs to the inflamed tissues is beneficial for achieving an optimal modulation of inflammation.
    Keywords adipose-derived mesenchymal stem cells ; intraperitoneal therapy ; biodistribution ; efficacy ; colitis ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 570
    Language English
    Publishing date 2018-06-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: A broadly neutralizing macaque monoclonal antibody against the HIV-1 V3-Glycan patch

    Zijun Wang / Christopher O Barnes / Rajeev Gautam / Julio C Cetrulo Lorenzi / Christian T Mayer / Thiago Y Oliveira / Victor Ramos / Melissa Cipolla / Kristie M Gordon / Harry B Gristick / Anthony P West / Yoshiaki Nishimura / Henna Raina / Michael S Seaman / Anna Gazumyan / Malcolm Martin / Pamela J Bjorkman / Michel C Nussenzweig / Amelia Escolano

    eLife, Vol

    2020  Volume 9

    Abstract: A small fraction of HIV-1- infected humans develop broadly neutralizing antibodies (bNAbs) against HIV-1 that protect macaques from simian immunodeficiency HIV chimeric virus (SHIV). Similarly, a small number of macaques infected with SHIVs develop ... ...

    Abstract A small fraction of HIV-1- infected humans develop broadly neutralizing antibodies (bNAbs) against HIV-1 that protect macaques from simian immunodeficiency HIV chimeric virus (SHIV). Similarly, a small number of macaques infected with SHIVs develop broadly neutralizing serologic activity, but less is known about the nature of simian antibodies. Here, we report on a monoclonal antibody, Ab1485, isolated from a macaque infected with SHIVAD8 that developed broadly neutralizing serologic activity targeting the V3-glycan region of HIV-1 Env. Ab1485 neutralizes 38.1% of HIV-1 isolates in a 42-pseudovirus panel with a geometric mean IC50 of 0.055 µg/mLl and SHIVAD8 with an IC50 of 0.028 µg/mLl. Ab1485 binds the V3-glycan epitope in a glycan-dependent manner. A 3.5 Å cryo-electron microscopy structure of Ab1485 in complex with a native-like SOSIP Env trimer showed conserved contacts with the N332gp120 glycan and gp120 GDIR peptide motif, but in a distinct Env-binding orientation relative to human V3/N332gp120 glycan-targeting bNAbs. Intravenous infusion of Ab1485 protected macaques from a high dose challenge with SHIVAD8. We conclude that macaques can develop bNAbs against the V3-glycan patch that resemble human V3-glycan bNAbs.
    Keywords anti hiv-1 ; broadly neutralizing ; antibody ; rhesus macaque ; v3 glycan ; patch antibody ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2020-10-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article: Immunization for HIV-1 Broadly Neutralizing Antibodies in Human Ig Knockin Mice

    Dosenovic, Pia / Lotta von Boehmer / Amelia Escolano / Joseph Jardine / Natalia T. Freund / Alexander D. Gitlin / Andrew T. McGuire / Daniel W. Kulp / Thiago Oliveira / Louise Scharf / John Pietzsch / Matthew D. Gray / Albert Cupo / Marit J. van Gils / Kai-Hui Yao / Cassie Liu / Anna Gazumyan / Michael S. Seaman / Pamela J. Björkman /
    Rogier W. Sanders / John P. Moore / Leonidas Stamatatos / William R. Schief / Michel C. Nussenzweig

    Cell. 2015 June 18, v. 161

    2015  

    Abstract: A subset of individuals infected with HIV-1 develops broadly neutralizing antibodies (bNAbs) that can prevent infection, but it has not yet been possible to elicit these antibodies by immunization. To systematically explore how immunization might be ... ...

    Abstract A subset of individuals infected with HIV-1 develops broadly neutralizing antibodies (bNAbs) that can prevent infection, but it has not yet been possible to elicit these antibodies by immunization. To systematically explore how immunization might be tailored to produce them, we generated mice expressing the predicted germline or mature heavy chains of a potent bNAb to the CD4 binding site (CD4bs) on the HIV-1 envelope glycoprotein (Env). Immunogens specifically designed to activate B cells bearing germline antibodies are required to initiate immune responses, but they do not elicit bNAbs. In contrast, native-like Env trimers fail to activate B cells expressing germline antibodies but elicit bNAbs by selecting for a restricted group of light chains bearing specific somatic mutations that enhance neutralizing activity. The data suggest that vaccination to elicit anti-HIV-1 antibodies will require immunization with a succession of related immunogens.
    Keywords HIV infections ; Human immunodeficiency virus 1 ; antigens ; binding sites ; germ cells ; glycoproteins ; humans ; immune response ; mice ; neutralization ; neutralizing antibodies ; somatic mutation ; vaccination
    Language English
    Dates of publication 2015-0618
    Size p. 1505-1515.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2015.06.003
    Database NAL-Catalogue (AGRICOLA)

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