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  1. Article: Potential of a Bead-Based Multiplex Assay for SARS-CoV-2 Antibody Detection.

    Rottmayer, Karla / Schwarze, Mandy / Jassoy, Christian / Hoffmann, Ralf / Loeffler-Wirth, Henry / Lehmann, Claudia

    Biology

    2024  Volume 13, Issue 4

    Abstract: Serological assays for SARS-CoV-2 play a pivotal role in the definition of whether patients are infected, the understanding of viral epidemiology, the screening of convalescent sera for therapeutic and prophylactic purposes, and in obtaining a better ... ...

    Abstract Serological assays for SARS-CoV-2 play a pivotal role in the definition of whether patients are infected, the understanding of viral epidemiology, the screening of convalescent sera for therapeutic and prophylactic purposes, and in obtaining a better understanding of the immune response towards the virus. The aim of this study was to investigate the performance of a bead-based multiplex assay. This assay allowed for the simultaneous testing of IgG antibodies against SARS-CoV-2 spike, S1, S2, RBD, and nucleocapsid moieties and S1 of seasonal coronaviruses hCoV-22E, hCoV-HKU1, hCoV-NL63, and hCoV-OC43, as well as MERS and SARS-CoV. We compared the bead-based multiplex assay with commercial ELISA tests. We tested the sera of 27 SARS-CoV-2 PCR-positive individuals who were previously tested with different ELISA assays. Additionally, we investigated the reproducibility of the results by means of multiple testing of the same sera. Finally, the results were correlated with neutralising assays. In summary, the concordance of the qualitative results ranged between 78% and 96% depending on the ELISA assay and the specific antigen. Repeated freezing-thawing cycles resulted in reduced mean fluorescence intensity, while the storage period had no influence in this respect. In our test cohort, we detected up to 36% of sera positive for the development of neutralising antibodies, which is in concordance with the bead-based multiplex and IgG ELISA.
    Language English
    Publishing date 2024-04-18
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2661517-4
    ISSN 2079-7737
    ISSN 2079-7737
    DOI 10.3390/biology13040273
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Cross-Reactivity of IgG Antibodies and Virus Neutralization in mRNA-Vaccinated People Against Wild-Type SARS-CoV-2 and the Five Most Common SARS-CoV-2 Variants of Concern.

    Schwarze, Mandy / Krizsan, Andor / Brakel, Alexandra / Pohl, Fabian / Volke, Daniela / Hoffmann, Ralf

    Frontiers in immunology

    2022  Volume 13, Page(s) 915034

    Abstract: The rapid development, approval, and production of vaccines against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in less than 1 year after the first reports of a new infectious disease was a real game changer, providing 80%-90% ... ...

    Abstract The rapid development, approval, and production of vaccines against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in less than 1 year after the first reports of a new infectious disease was a real game changer, providing 80%-90% efficacy in preventing severe etiopathologies of the coronavirus disease 2019 (COVID-19). These vaccines induce an immune response against the SARS-CoV-2 spike (S) protein located on the surface of the virus particle. Antibodies (Abs) recognizing the S-protein can inhibit binding of the virus
    MeSH term(s) BNT162 Vaccine ; COVID-19/prevention & control ; Humans ; Immunoglobulin G ; RNA, Messenger ; SARS-CoV-2
    Chemical Substances Immunoglobulin G ; RNA, Messenger ; BNT162 Vaccine (N38TVC63NU)
    Language English
    Publishing date 2022-06-15
    Publishing country Switzerland
    Document type Journal Article ; 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.2022.915034
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Influence of Mutations and N-Glycosylation Sites in the Receptor-Binding Domain (RBD) and the Membrane Protein of SARS-CoV-2 Variants of Concern on Antibody Binding in ELISA.

    Schwarze, Mandy / Volke, Daniela / Rojas Echeverri, Juan Camilo / Schick, Robin / Lakowa, Nicole / Grünewald, Thomas / Wolf, Johannes / Borte, Stephan / Scholz, Markus / Krizsan, Andor / Hoffmann, Ralf

    Biology

    2024  Volume 13, Issue 4

    Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can infect human cells by first attaching to the ACE-2 receptor via its receptor-binding domain (RBD) in the spike protein. Here, we report the influence of N-glycosylation sites of the RBD and ...

    Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can infect human cells by first attaching to the ACE-2 receptor via its receptor-binding domain (RBD) in the spike protein. Here, we report the influence of N-glycosylation sites of the RBD and the membrane (M) protein on IgG antibody binding in serum samples from patients infected with the original SARS-CoV-2 strain in Germany. The RBDs of the wildtype, alpha, beta, gamma, and kappa variants expressed in HEK293S GnTI- cells were all N-glycosylated at Asn331, Asn334, Asn343, and Asn360 or Asn370, whereas the M-protein was glycosylated at Asn5. An ELISA using a coated RBD and probed with anti-RBD IgG antibodies gave a sensitivity of 96.3% and a specificity of 100% for the wildtype RBD, while the sensitivity decreased by 5% to 10% for the variants of concern, essentially in the order of appearance. Deglycosylation of the wildtype RBD strongly reduced antibody recognition by ~20%, considering the mean of the absorbances recorded for the ELISA. This effect was even stronger for the unglycosylated RBD expressed in
    Language English
    Publishing date 2024-03-23
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2661517-4
    ISSN 2079-7737
    ISSN 2079-7737
    DOI 10.3390/biology13040207
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Evaluation of S- and M-Proteins Expressed in

    Schwarze, Mandy / Luo, Ji / Brakel, Alexandra / Krizsan, Andor / Lakowa, Nicole / Grünewald, Thomas / Lehmann, Claudia / Wolf, Johannes / Borte, Stephan / Milkovska-Stamenova, Sanja / Gabert, Jörg / Scholz, Markus / Hoffmann, Ralf

    Pathogens (Basel, Switzerland)

    2022  Volume 11, Issue 12

    Abstract: This study investigated the IgG and IgA antibody response against recombinant S1 and receptor binding domains (RBD) of the spike (S-) protein and the membrane (M-) protein using a set of 115 serum samples collected from patients infected with SARS-CoV-2 ... ...

    Abstract This study investigated the IgG and IgA antibody response against recombinant S1 and receptor binding domains (RBD) of the spike (S-) protein and the membrane (M-) protein using a set of 115 serum samples collected from patients infected with SARS-CoV-2 in Germany before April 2021 using protein and peptide ELISA. As S1- and RBD-proteins expressed in
    Language English
    Publishing date 2022-12-10
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2695572-6
    ISSN 2076-0817
    ISSN 2076-0817
    DOI 10.3390/pathogens11121515
    Database MEDical Literature Analysis and Retrieval System OnLINE

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