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  1. Artikel ; Online: Protocol for analyzing antibody responses to glycoprotein antigens using electron-microscopy-based polyclonal epitope mapping.

    Turner, Hannah L / Jackson, Abigail M / Richey, Sara T / Sewall, Leigh M / Antanasijevic, Aleksandar / Hangartner, Lars / Ward, Andrew B

    STAR protocols

    2023  Band 4, Heft 3, Seite(n) 102476

    Abstract: Electron microscopy-based polyclonal epitope mapping (EMPEM) can delineate epitope specificities of serum antibodies to a given antigen following vaccination or infection. Here, we present a protocol for the EMPEM method for rapid high-throughput ... ...

    Abstract Electron microscopy-based polyclonal epitope mapping (EMPEM) can delineate epitope specificities of serum antibodies to a given antigen following vaccination or infection. Here, we present a protocol for the EMPEM method for rapid high-throughput assessment of antibody responses to glycoprotein antigens in vaccination and infection studies. We describe steps for antibody isolation and digestion, antigen complex and purification, and electron microscope imaging. We then detail procedures for processing and analysis of EMPEM data. For complete details on the use and execution of this protocol, please refer to Bianchi et al. (2018).
    Mesh-Begriff(e) Epitope Mapping ; Antibody Formation ; Electrons ; Microscopy, Electron ; Antibodies ; Glycoproteins
    Chemische Substanzen Antibodies ; Glycoproteins
    Sprache Englisch
    Erscheinungsdatum 2023-07-28
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 2666-1667
    ISSN (online) 2666-1667
    DOI 10.1016/j.xpro.2023.102476
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Increasing sensitivity of antibody-antigen interactions using photo-cross-linking.

    Torrents de la Peña, Alba / Sewall, Leigh M / de Paiva Froes Rocha, Rebeca / Jackson, Abigail M / Pratap, Payal P / Bangaru, Sandhya / Cottrell, Christopher A / Mohanty, Subhasis / Shaw, Albert C / Ward, Andrew B

    Cell reports methods

    2023  Band 3, Heft 6, Seite(n) 100509

    Abstract: Understanding antibody-antigen interactions in a polyclonal immune response in humans and animal models is critical for rational vaccine design. Current approaches typically characterize antibodies that are functionally relevant or highly abundant. Here, ...

    Abstract Understanding antibody-antigen interactions in a polyclonal immune response in humans and animal models is critical for rational vaccine design. Current approaches typically characterize antibodies that are functionally relevant or highly abundant. Here, we use photo-cross-linking and single-particle electron microscopy to increase antibody detection and unveil epitopes of low-affinity and low-abundance antibodies, leading to a broader structural characterization of polyclonal immune responses. We employed this approach across three different viral glycoproteins and showed increased sensitivity of detection relative to currently used methods. Results were most noticeable in early and late time points of a polyclonal immune response. Additionally, the use of photo-cross-linking revealed intermediate antibody binding states and demonstrated a distinctive way to study antibody binding mechanisms. This technique can be used to structurally characterize the landscape of a polyclonal immune response of patients in vaccination or post-infection studies at early time points, allowing for rapid iterative design of vaccine immunogens.
    Mesh-Begriff(e) Animals ; Humans ; Antibodies, Neutralizing ; Epitopes/chemistry ; Vaccination ; Vaccines
    Chemische Substanzen Antibodies, Neutralizing ; Epitopes ; Vaccines
    Sprache Englisch
    Erscheinungsdatum 2023-06-05
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 2667-2375
    ISSN (online) 2667-2375
    DOI 10.1016/j.crmeth.2023.100509
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Immune memory shapes human polyclonal antibody responses to H2N2 vaccination.

    Yang, Yuhe R / Han, Julianna / Perrett, Hailee R / Richey, Sara T / Rodriguez, Alesandra J / Jackson, Abigail M / Gillespie, Rebecca A / O'Connell, Sarah / Raab, Julie E / Cominsky, Lauren Y / Chopde, Ankita / Kanekiyo, Masaru / Houser, Katherine V / Chen, Grace L / McDermott, Adrian B / Andrews, Sarah F / Ward, Andrew B

    Cell reports

    2024  Band 43, Heft 5, Seite(n) 114171

    Abstract: Influenza A virus subtype H2N2, which caused the 1957 influenza pandemic, remains a global threat. A recent phase 1 clinical trial investigating a ferritin nanoparticle vaccine displaying H2 hemagglutinin (HA) in H2-naive and H2-exposed adults enabled us ...

    Abstract Influenza A virus subtype H2N2, which caused the 1957 influenza pandemic, remains a global threat. A recent phase 1 clinical trial investigating a ferritin nanoparticle vaccine displaying H2 hemagglutinin (HA) in H2-naive and H2-exposed adults enabled us to perform comprehensive structural and biochemical characterization of immune memory on the breadth and diversity of the polyclonal serum antibody response elicited. We temporally map the epitopes targeted by serum antibodies after vaccine prime and boost, revealing that previous H2 exposure results in higher responses to the variable HA head domain. In contrast, initial responses in H2-naive participants are dominated by antibodies targeting conserved epitopes. We use cryoelectron microscopy and monoclonal B cell isolation to describe the molecular details of cross-reactive antibodies targeting conserved epitopes on the HA head, including the receptor-binding site and a new site of vulnerability deemed the medial junction. Our findings accentuate the impact of pre-existing influenza exposure on serum antibody responses post-vaccination.
    Mesh-Begriff(e) Humans ; Antibodies, Viral/immunology ; Influenza Vaccines/immunology ; Immunologic Memory ; Vaccination ; Influenza A Virus, H2N2 Subtype/immunology ; Influenza, Human/immunology ; Influenza, Human/prevention & control ; Antibody Formation/immunology ; Hemagglutinin Glycoproteins, Influenza Virus/immunology ; Epitopes/immunology ; Adult ; B-Lymphocytes/immunology
    Chemische Substanzen Antibodies, Viral ; Influenza Vaccines ; Hemagglutinin Glycoproteins, Influenza Virus ; Epitopes
    Sprache Englisch
    Erscheinungsdatum 2024-05-07
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2024.114171
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Structural mapping of antibody landscapes to human betacoronavirus spike proteins.

    Bangaru, Sandhya / Antanasijevic, Aleksandar / Kose, Nurgun / Sewall, Leigh M / Jackson, Abigail M / Suryadevara, Naveenchandra / Zhan, Xiaoyan / Torres, Jonathan L / Copps, Jeffrey / de la Peña, Alba Torrents / Crowe, James E / Ward, Andrew B

    Science advances

    2022  Band 8, Heft 18, Seite(n) eabn2911

    Abstract: Preexisting immunity against seasonal coronaviruses (CoVs) represents an important variable in predicting antibody responses and disease severity to severe acute respiratory syndrome CoV-2 (SARS-CoV-2) infections. We used electron microscopy-based ... ...

    Abstract Preexisting immunity against seasonal coronaviruses (CoVs) represents an important variable in predicting antibody responses and disease severity to severe acute respiratory syndrome CoV-2 (SARS-CoV-2) infections. We used electron microscopy-based polyclonal epitope mapping (EMPEM) to characterize the antibody specificities against β-CoV spike proteins in prepandemic (PP) sera or SARS-CoV-2 convalescent (SC) sera. We observed that most PP sera had antibodies specific to seasonal human CoVs (HCoVs) OC43 and HKU1 spike proteins while the SC sera showed reactivity across all human β-CoVs. Detailed molecular mapping of spike-antibody complexes revealed epitopes that were differentially targeted by preexisting antibodies and SC serum antibodies. Our studies provide an antigenic landscape to β-HCoV spikes in the general population serving as a basis for cross-reactive epitope analyses in SARS-CoV-2-infected individuals.
    Mesh-Begriff(e) Antibodies, Viral ; COVID-19 ; Coronavirus OC43, Human ; Epitopes ; Humans ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus
    Chemische Substanzen Antibodies, Viral ; Epitopes ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Sprache Englisch
    Erscheinungsdatum 2022-05-04
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.abn2911
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: One dose of COVID-19 nanoparticle vaccine REVC-128 protects against SARS-CoV-2 challenge at two weeks post-immunization.

    Gu, Maggie / Torres, Jonathan L / Li, Yijia / Van Ry, Alex / Greenhouse, Jack / Wallace, Shannon / Chiang, Chi-I / Pessaint, Laurent / Jackson, Abigail M / Porto, Maciel / Kar, Swagata / Li, Yuxing / Ward, Andrew B / Wang, Yimeng

    Emerging microbes & infections

    2021  Band 10, Heft 1, Seite(n) 2016–2029

    Abstract: ... ...

    Abstract ABSTRACT
    Mesh-Begriff(e) Animals ; Antibodies, Neutralizing ; Antibodies, Viral/blood ; Antibody Formation ; COVID-19/prevention & control ; COVID-19 Vaccines/administration & dosage ; COVID-19 Vaccines/immunology ; Cricetinae ; Humans ; Immunization ; Immunization Schedule ; Immunogenicity, Vaccine ; Mesocricetus ; Mice ; Nanoparticles/chemistry ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Vaccination ; Viral Load
    Chemische Substanzen Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines ; Spike Glycoprotein, Coronavirus
    Sprache Englisch
    Erscheinungsdatum 2021-10-12
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2681359-2
    ISSN 2222-1751 ; 2222-1751
    ISSN (online) 2222-1751
    ISSN 2222-1751
    DOI 10.1080/22221751.2021.1994354
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Structural definition of a pan-sarbecovirus neutralizing epitope on the spike S2 subunit.

    Hurlburt, Nicholas K / Homad, Leah J / Sinha, Irika / Jennewein, Madeleine F / MacCamy, Anna J / Wan, Yu-Hsin / Boonyaratanakornkit, Jim / Sholukh, Anton M / Jackson, Abigail M / Zhou, Panpan / Burton, Dennis R / Andrabi, Raiees / Ozorowski, Gabriel / Ward, Andrew B / Stamatatos, Leonidas / Pancera, Marie / McGuire, Andrew T

    Communications biology

    2022  Band 5, Heft 1, Seite(n) 342

    Abstract: Three betacoronaviruses have crossed the species barrier and established human-to-human transmission causing significant morbidity and mortality in the past 20 years. The most current and widespread of these is SARS-CoV-2. The identification of CoVs with ...

    Abstract Three betacoronaviruses have crossed the species barrier and established human-to-human transmission causing significant morbidity and mortality in the past 20 years. The most current and widespread of these is SARS-CoV-2. The identification of CoVs with zoonotic potential in animal reservoirs suggests that additional outbreaks could occur. Monoclonal antibodies targeting conserved neutralizing epitopes on diverse CoVs can form the basis for prophylaxis and therapeutic treatments and enable the design of vaccines aimed at providing pan-CoV protection. We previously identified a neutralizing monoclonal antibody, CV3-25 that binds to the SARS-CoV-2 spike, neutralizes the SARS-CoV-2 Beta variant comparably to the ancestral Wuhan Hu-1 strain, cross neutralizes SARS-CoV-1 and binds to recombinant proteins derived from the spike-ectodomains of HCoV-OC43 and HCoV-HKU1. Here, we show that the neutralizing activity of CV3-25 is maintained against the Alpha, Delta, Gamma and Omicron variants of concern as well as a SARS-CoV-like bat coronavirus with zoonotic potential by binding to a conserved linear peptide in the stem-helix region. Negative stain electron microscopy and a 1.74 Å crystal structure of a CV3-25/peptide complex demonstrates that CV3-25 binds to the base of the stem helix at the HR2 boundary to an epitope that is distinct from other stem-helix directed neutralizing mAbs.
    Mesh-Begriff(e) Animals ; Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 ; Epitopes ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/chemistry
    Chemische Substanzen Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Sprache Englisch
    Erscheinungsdatum 2022-04-11
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-022-03262-7
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel ; Online: mRNA-LNP HIV-1 trimer boosters elicit precursors to broad neutralizing antibodies.

    Xie, Zhenfei / Lin, Ying-Cing / Steichen, Jon M / Ozorowski, Gabriel / Kratochvil, Sven / Ray, Rashmi / Torres, Jonathan L / Liguori, Alessia / Kalyuzhniy, Oleksandr / Wang, Xuesong / Warner, John E / Weldon, Stephanie R / Dale, Gordon A / Kirsch, Kathrin H / Nair, Usha / Baboo, Sabyasachi / Georgeson, Erik / Adachi, Yumiko / Kubitz, Michael /
    Jackson, Abigail M / Richey, Sara T / Volk, Reid M / Lee, Jeong Hyun / Diedrich, Jolene K / Prum, Thavaleak / Falcone, Samantha / Himansu, Sunny / Carfi, Andrea / Yates, John R / Paulson, James C / Sok, Devin / Ward, Andrew B / Schief, William R / Batista, Facundo D

    Science (New York, N.Y.)

    2024  Band 384, Heft 6697, Seite(n) eadk0582

    Abstract: Germline-targeting (GT) HIV vaccine strategies are predicated on deriving broadly neutralizing antibodies (bnAbs) through multiple boost immunogens. However, as the recruitment of memory B cells (MBCs) to germinal centers (GCs) is inefficient and may be ... ...

    Abstract Germline-targeting (GT) HIV vaccine strategies are predicated on deriving broadly neutralizing antibodies (bnAbs) through multiple boost immunogens. However, as the recruitment of memory B cells (MBCs) to germinal centers (GCs) is inefficient and may be derailed by serum antibody-induced epitope masking, driving further B cell receptor (BCR) modification in GC-experienced B cells after boosting poses a challenge. Using humanized immunoglobulin knockin mice, we found that GT protein trimer immunogen N332-GT5 could prime inferred-germline precursors to the V3-glycan-targeted bnAb BG18 and that B cells primed by N332-GT5 were effectively boosted by either of two novel protein immunogens designed to have minimum cross-reactivity with the off-target V1-binding responses. The delivery of the prime and boost immunogens as messenger RNA lipid nanoparticles (mRNA-LNPs) generated long-lasting GCs, somatic hypermutation, and affinity maturation and may be an effective tool in HIV vaccine development.
    Mesh-Begriff(e) Animals ; Mice ; HIV-1/immunology ; HIV-1/genetics ; AIDS Vaccines/immunology ; Humans ; HIV Antibodies/immunology ; Nanoparticles ; Germinal Center/immunology ; Broadly Neutralizing Antibodies/immunology ; Immunization, Secondary ; RNA, Messenger/genetics ; RNA, Messenger/immunology ; Gene Knock-In Techniques ; Memory B Cells/immunology ; Antibodies, Neutralizing/immunology ; B-Lymphocytes/immunology ; Somatic Hypermutation, Immunoglobulin ; HIV Envelope Protein gp120/immunology ; HIV Envelope Protein gp120/chemistry ; HIV Envelope Protein gp120/genetics ; Receptors, Antigen, B-Cell/immunology ; Receptors, Antigen, B-Cell/genetics ; Cross Reactions ; HIV Infections/immunology ; HIV Infections/prevention & control ; Liposomes
    Chemische Substanzen Lipid Nanoparticles
    Sprache Englisch
    Erscheinungsdatum 2024-05-17
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.adk0582
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 27: Hefte anzeigen Standort:
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  8. Artikel: Immune memory shapes human polyclonal antibody responses to H2N2 vaccination.

    Yang, Yuhe R / Han, Julianna / Perrett, Hailee R / Richey, Sara T / Jackson, Abigail M / Rodriguez, Alesandra J / Gillespie, Rebecca A / O'Connell, Sarah / Raab, Julie E / Cominsky, Lauren Y / Chopde, Ankita / Kanekiyo, Masaru / Houser, Katherine V / Chen, Grace L / McDermott, Adrian B / Andrews, Sarah F / Ward, Andrew B

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Influenza A virus subtype H2N2, which caused the 1957 influenza pandemic, remains a global threat. A recent phase I clinical trial investigating a ferritin nanoparticle displaying H2 hemagglutinin in H2-naïve and H2-exposed adults. Therefore, we could ... ...

    Abstract Influenza A virus subtype H2N2, which caused the 1957 influenza pandemic, remains a global threat. A recent phase I clinical trial investigating a ferritin nanoparticle displaying H2 hemagglutinin in H2-naïve and H2-exposed adults. Therefore, we could perform comprehensive structural and biochemical characterization of immune memory on the breadth and diversity of the polyclonal serum antibody response elicited after H2 vaccination. We temporally map the epitopes targeted by serum antibodies after first and second vaccinations and show previous H2 exposure results in higher responses to the variable head domain of hemagglutinin while initial responses in H2-naïve participants are dominated by antibodies targeting conserved epitopes. We use cryo-EM and monoclonal B cell isolation to describe the molecular details of cross-reactive antibodies targeting conserved epitopes on the hemagglutinin head including the receptor binding site and a new site of vulnerability deemed the medial junction. Our findings accentuate the impact of pre-existing influenza exposure on serum antibody responses.
    Sprache Englisch
    Erscheinungsdatum 2023-08-24
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.08.23.554525
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  9. Artikel: Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants.

    Yuan, Meng / Huang, Deli / Lee, Chang-Chun D / Wu, Nicholas C / Jackson, Abigail M / Zhu, Xueyong / Liu, Hejun / Peng, Linghang / van Gils, Marit J / Sanders, Rogier W / Burton, Dennis R / Reincke, S Momsen / Prüss, Harald / Kreye, Jakob / Nemazee, David / Ward, Andrew B / Wilson, Ian A

    bioRxiv : the preprint server for biology

    2021  

    Abstract: The protective efficacy of neutralizing antibodies (nAbs) elicited during natural infection with SARS-CoV-2 and by vaccination based on its spike protein has been compromised with emergence of the recent SARS-CoV-2 variants. Residues E484 and K417 in the ...

    Abstract The protective efficacy of neutralizing antibodies (nAbs) elicited during natural infection with SARS-CoV-2 and by vaccination based on its spike protein has been compromised with emergence of the recent SARS-CoV-2 variants. Residues E484 and K417 in the receptor-binding site (RBS) are both mutated in lineages first described in South Africa (B.1.351) and Brazil (B.1.1.28.1). The nAbs isolated from SARS-CoV-2 patients are preferentially encoded by certain heavy-chain germline genes and the two most frequently elicited antibody families (IGHV3-53/3-66 and IGHV1-2) can each bind the RBS in two different binding modes. However, their binding and neutralization are abrogated by either the E484K or K417N mutation, whereas nAbs to the cross-reactive CR3022 and S309 sites are largely unaffected. This structural and functional analysis illustrates why mutations at E484 and K417 adversely affect major classes of nAbs to SARS-CoV-2 with consequences for next-generation COVID-19 vaccines.
    Sprache Englisch
    Erscheinungsdatum 2021-02-17
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2021.02.16.430500
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants.

    Yuan, Meng / Huang, Deli / Lee, Chang-Chun D / Wu, Nicholas C / Jackson, Abigail M / Zhu, Xueyong / Liu, Hejun / Peng, Linghang / van Gils, Marit J / Sanders, Rogier W / Burton, Dennis R / Reincke, S Momsen / Prüss, Harald / Kreye, Jakob / Nemazee, David / Ward, Andrew B / Wilson, Ian A

    Science (New York, N.Y.)

    2021  Band 373, Heft 6556, Seite(n) 818–823

    Abstract: Neutralizing antibodies (nAbs) elicited against the receptor binding site (RBS) of the spike protein of wild-type severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are generally less effective against recent variants of concern. RBS residues ... ...

    Abstract Neutralizing antibodies (nAbs) elicited against the receptor binding site (RBS) of the spike protein of wild-type severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are generally less effective against recent variants of concern. RBS residues Glu
    Mesh-Begriff(e) Angiotensin-Converting Enzyme 2/metabolism ; Antibodies, Neutralizing/immunology ; Antibodies, Neutralizing/metabolism ; Antibodies, Viral/immunology ; Antibodies, Viral/metabolism ; Antigenic Variation ; Antigens, Viral/chemistry ; Antigens, Viral/genetics ; Antigens, Viral/immunology ; Antigens, Viral/metabolism ; Binding Sites ; Binding Sites, Antibody ; COVID-19/immunology ; COVID-19/virology ; Epitopes ; Humans ; Immune Evasion ; Mutation ; Protein Binding ; Protein Domains ; Receptors, Coronavirus/metabolism ; SARS-CoV-2/chemistry ; SARS-CoV-2/genetics ; SARS-CoV-2/immunology ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/immunology ; Spike Glycoprotein, Coronavirus/metabolism
    Chemische Substanzen Antibodies, Neutralizing ; Antibodies, Viral ; Antigens, Viral ; Epitopes ; Receptors, Coronavirus ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Sprache Englisch
    Erscheinungsdatum 2021-05-20
    Erscheinungsland United States
    Dokumenttyp 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 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.abh1139
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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