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      Structure-Specific N-Glycoproteomics Characterization of NIST Monoclonal Antibody Reference Material 8671

      Author(s): 1 , 2 , 1
      Publication date (Electronic):
      Journal: Journal of Proteome Research
      Publisher: American Chemical Society (ACS)

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          Abstract

          <p class="first" id="d7672610e77">The characteristics of monoclonal antibodies (mAbs) cohering various function effectors show great expectation in therapy. Glycosylation, one of the common post-translational modifications, deeply influences cohesion. It is necessary to grasp monosaccharide composition/sequence and glycan structures in mAbs. There has been comprehensive mass spectrometry characterization of N-glycosylation of mAbs, and monosaccharide compositions are deduced according to known biosynthetic rules. Our recently developed intact N-glycopeptide search engine GPSeeker has made structure-specific characterization of N-glycosylation possible with structure-diagnostic fragment ions from selective fragmentation of N-glycan moieties. Here, we report our structure-specific N-glycoproteomics characterization of NIST monoclonal antibody reference material 8671 using GPSeeker, and 59 N-glycan structures (including 16 pairs of isomers) are characterized. </p>

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          IgG Subclasses and Allotypes: From Structure to Effector Functions

          Gestur Vidarsson, Gillian Dekkers, Theo Rispens (2014)
          Of the five immunoglobulin isotypes, immunoglobulin G (IgG) is most abundant in human serum. The four subclasses, IgG1, IgG2, IgG3, and IgG4, which are highly conserved, differ in their constant region, particularly in their hinges and upper CH2 domains. These regions are involved in binding to both IgG-Fc receptors (FcγR) and C1q. As a result, the different subclasses have different effector functions, both in terms of triggering FcγR-expressing cells, resulting in phagocytosis or antibody-dependent cell-mediated cytotoxicity, and activating complement. The Fc-regions also contain a binding epitope for the neonatal Fc receptor (FcRn), responsible for the extended half-life, placental transport, and bidirectional transport of IgG to mucosal surfaces. However, FcRn is also expressed in myeloid cells, where it participates in both phagocytosis and antigen presentation together with classical FcγR and complement. How these properties, IgG-polymorphisms and post-translational modification of the antibodies in the form of glycosylation, affect IgG-function will be the focus of the current review.
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            A vaccine targeting the RBD of the S protein of SARS-CoV-2 induces protective immunity

            Jingyun Yang, Wei Wang, Zimin Chen … (2020)
            Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causes a respiratory disease called coronavirus disease 2019 (COVID-19), the spread of which has led to a pandemic. An effective preventive vaccine against this virus is urgently needed. As an essential step during infection, SARS-CoV-2 uses the receptor-binding domain (RBD) of the spike protein to engage with the receptor angiotensin-converting enzyme 2 (ACE2) on host cells1,2. Here we show that a recombinant vaccine that comprises residues 319-545 of the RBD of the spike protein induces a potent functional antibody response in immunized mice, rabbits and non-human primates (Macaca mulatta) as early as 7 or 14 days after the injection of a single vaccine dose. The sera from the immunized animals blocked the binding of the RBD to ACE2, which is expressed on the cell surface, and neutralized infection with a SARS-CoV-2 pseudovirus and live SARS-CoV-2 in vitro. Notably, vaccination also provided protection in non-human primates to an in vivo challenge with SARS-CoV-2. We found increased levels of RBD-specific antibodies in the sera of patients with COVID-19. We show that several immune pathways and CD4 T lymphocytes are involved in the induction of the vaccine antibody response. Our findings highlight the importance of the RBD domain in the design of SARS-CoV-2 vaccines and provide a rationale for the development of a protective vaccine through the induction of antibodies against the RBD domain.
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              Terminal sugars of Fc glycans influence antibody effector functions of IgGs.

              T. Shantha Raju (2008)
              IgG molecules contain glycans in the CH2 domain of the Fc fragment (N-glycosylation) which are highly heterogeneous, because of the presence of different terminal sugars. The heterogeneity of Fc glycans varies with species and expression system. Fc glycans influence the binding of IgG to Fc receptors and C1q, and are therefore important for IgG effector functions. Specifically, terminal sugars such as sialic acids, core fucose, bisecting N-acetylglucosamine, and mannose residues affect the binding of IgG to the FcgammaRIIIa receptor and thereby influence ADCC activity. By contrast, terminal galactose residues affect antibody binding to C1q and thereby modulate CDC activity. Structural studies indicate that the presence or absence of specific terminal sugars may affect hydrophilic and hydrophobic interactions between sugar residues and amino acid residues in the Fc fragment, which in turn may impact antibody effector functions.
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                Author and article information

                Contributors
                Journal
                Title: Journal of Proteome Research
                Abbreviated Title: J. Proteome Res.
                Publisher: American Chemical Society (ACS)
                ISSN (Print): 1535-3893
                ISSN (Electronic): 1535-3907
                Publication date Created: May 06 2022
                Publication date (Electronic): March 29 2022
                Publication date (Print): May 06 2022
                Volume: 21
                Issue: 5
                Pages: 1276-1284
                Affiliations
                [1 ]School of Chemical Science & Engineering, Tongji University, Shanghai 200092, China
                [2 ]Department of Laboratory Medicine, Center of Precision Medicine, Nanjing Drum Tower Hospital, the Affiliated Hospital of Nanjing University Medical School, Nanjing, Jiangsu 210008, China
                Article
                DOI: 10.1021/acs.jproteome.2c00027
                PubMed ID: 35349291
                SO-VID: dad8a448-3ad2-457a-8d95-436c81c9287c
                Copyright © © 2022
                License:

                https://doi.org/10.15223/policy-029

                https://doi.org/10.15223/policy-037

                https://doi.org/10.15223/policy-045

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