Differences in Immunoglobulin G Glycosylation Between Influenza and COVID-19 Patients
The essential role of immunoglobulin G (IgG) in immune system regulation and combatting infectious diseases cannot be fully recognized without an understanding of the changes in its N-glycans attached to the asparagine 297 of the fragment crystallizable (Fc) domain that occur under such circumstance...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-07-01
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| Series: | Engineering |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2095809922006312 |
| _version_ | 1797672792420777984 |
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| author | Marina Kljaković-Gašpić Batinjan Tea Petrović Frano Vučković Irzal Hadžibegović Barbara Radovani Ivana Jurin Lovorka Đerek Eva Huljev Alemka Markotić Ivica Lukšić Irena Trbojević-Akmačić Gordan Lauc Ivan Gudelj Rok Čivljak |
| author_facet | Marina Kljaković-Gašpić Batinjan Tea Petrović Frano Vučković Irzal Hadžibegović Barbara Radovani Ivana Jurin Lovorka Đerek Eva Huljev Alemka Markotić Ivica Lukšić Irena Trbojević-Akmačić Gordan Lauc Ivan Gudelj Rok Čivljak |
| author_sort | Marina Kljaković-Gašpić Batinjan |
| collection | DOAJ |
| description | The essential role of immunoglobulin G (IgG) in immune system regulation and combatting infectious diseases cannot be fully recognized without an understanding of the changes in its N-glycans attached to the asparagine 297 of the fragment crystallizable (Fc) domain that occur under such circumstances. These glycans impact the antibody stability, half-life, secretion, immunogenicity, and effector functions. Therefore, in this study, we analyzed and compared the total IgG glycome—at the level of individual glycan structures and derived glycosylation traits (sialylation, galactosylation, fucosylation, and bisecting N-acetylglucosamine (GlcNAc))—of 64 patients with influenza, 77 patients with coronavirus disease 2019 (COVID-19), and 56 healthy controls. Our study revealed a significant decrease in IgG galactosylation, sialylation, and bisecting GlcNAc (where the latter shows the most significant decrease) in deceased COVID-19 patients, whereas IgG fucosylation was increased. On the other hand, IgG galactosylation remained stable in influenza patients and COVID-19 survivors. IgG glycosylation in influenza patients was more time-dependent: In the first seven days of the disease, sialylation increased and fucosylation and bisecting GlcNAc decreased; in the next 21 days, sialylation decreased and fucosylation increased (while bisecting GlcNAc remained stable). The similarity of IgG glycosylation changes in COVID-19 survivors and influenza patients may be the consequence of an adequate immune response to enveloped viruses, while the observed changes in deceased COVID-19 patients may indicate its deviation. |
| first_indexed | 2024-03-11T21:35:21Z |
| format | Article |
| id | doaj.art-f551fb25a4dc417181bd37d173bbffe6 |
| institution | Directory Open Access Journal |
| issn | 2095-8099 |
| language | English |
| last_indexed | 2024-03-11T21:35:21Z |
| publishDate | 2023-07-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Engineering |
| spelling | doaj.art-f551fb25a4dc417181bd37d173bbffe62023-09-27T04:42:44ZengElsevierEngineering2095-80992023-07-01265462Differences in Immunoglobulin G Glycosylation Between Influenza and COVID-19 PatientsMarina Kljaković-Gašpić Batinjan0Tea Petrović1Frano Vučković2Irzal Hadžibegović3Barbara Radovani4Ivana Jurin5Lovorka Đerek6Eva Huljev7Alemka Markotić8Ivica Lukšić9Irena Trbojević-Akmačić10Gordan Lauc11Ivan Gudelj12Rok Čivljak13University Hospital Centre Zagreb, Zagreb 10000, CroatiaGenos Glycoscience Research Laboratory, Zagreb 10000, CroatiaGenos Glycoscience Research Laboratory, Zagreb 10000, CroatiaDepartment of Cardiology, University Hospital Dubrava, Zagreb 10000, Croatia; Faculty of Dental Medicine and Health, Josip Juraj Strossmayer University, Osijek 31000, CroatiaDepartment of Biotechnology, University of Rijeka, Rijeka 51000, CroatiaDepartment of Cardiology, University Hospital Dubrava, Zagreb 10000, CroatiaDepartment for Laboratory Diagnostics, University Hospital Dubrava, Zagreb 10000, CroatiaDepartment for Acute Respiratory Infections, University Hospital for Infectious Diseases “Dr. Fran Mihaljević”, Zagreb 10000, CroatiaDepartment for Urogenital Infections, University Hospital for Infectious Diseases “Dr. Fran Mihaljević”, Zagreb 10000, Croatia; Department for Infectious Diseases, School of Medicine, Catholic University of Croatia, 10000 Zagreb, Croatia; Postdoctoral Study, Faculty of Medicine, University of Rijeka, Rijeka 51000, CroatiaDepartment of Maxillofacial Surgery, University of Zagreb School of Medicine, Dubrava University Hospital, Zagreb 10000, CroatiaGenos Glycoscience Research Laboratory, Zagreb 10000, CroatiaGenos Glycoscience Research Laboratory, Zagreb 10000, Croatia; Faculty of Pharmacy and Biochemistry, University of Zagreb, Zagreb 10000, CroatiaGenos Glycoscience Research Laboratory, Zagreb 10000, Croatia; Department of Biotechnology, University of Rijeka, Rijeka 51000, Croatia; Corresponding author.Department for Acute Respiratory Infections, University Hospital for Infectious Diseases “Dr. Fran Mihaljević”, Zagreb 10000, Croatia; Department of Infectious Diseases, University of Zagreb School of Medicine, Zagreb 10000, CroatiaThe essential role of immunoglobulin G (IgG) in immune system regulation and combatting infectious diseases cannot be fully recognized without an understanding of the changes in its N-glycans attached to the asparagine 297 of the fragment crystallizable (Fc) domain that occur under such circumstances. These glycans impact the antibody stability, half-life, secretion, immunogenicity, and effector functions. Therefore, in this study, we analyzed and compared the total IgG glycome—at the level of individual glycan structures and derived glycosylation traits (sialylation, galactosylation, fucosylation, and bisecting N-acetylglucosamine (GlcNAc))—of 64 patients with influenza, 77 patients with coronavirus disease 2019 (COVID-19), and 56 healthy controls. Our study revealed a significant decrease in IgG galactosylation, sialylation, and bisecting GlcNAc (where the latter shows the most significant decrease) in deceased COVID-19 patients, whereas IgG fucosylation was increased. On the other hand, IgG galactosylation remained stable in influenza patients and COVID-19 survivors. IgG glycosylation in influenza patients was more time-dependent: In the first seven days of the disease, sialylation increased and fucosylation and bisecting GlcNAc decreased; in the next 21 days, sialylation decreased and fucosylation increased (while bisecting GlcNAc remained stable). The similarity of IgG glycosylation changes in COVID-19 survivors and influenza patients may be the consequence of an adequate immune response to enveloped viruses, while the observed changes in deceased COVID-19 patients may indicate its deviation.http://www.sciencedirect.com/science/article/pii/S2095809922006312InfluenzaCOVID-19Viral infectionGlycosylationImmunoglobulin GPneumonia |
| spellingShingle | Marina Kljaković-Gašpić Batinjan Tea Petrović Frano Vučković Irzal Hadžibegović Barbara Radovani Ivana Jurin Lovorka Đerek Eva Huljev Alemka Markotić Ivica Lukšić Irena Trbojević-Akmačić Gordan Lauc Ivan Gudelj Rok Čivljak Differences in Immunoglobulin G Glycosylation Between Influenza and COVID-19 Patients Engineering Influenza COVID-19 Viral infection Glycosylation Immunoglobulin G Pneumonia |
| title | Differences in Immunoglobulin G Glycosylation Between Influenza and COVID-19 Patients |
| title_full | Differences in Immunoglobulin G Glycosylation Between Influenza and COVID-19 Patients |
| title_fullStr | Differences in Immunoglobulin G Glycosylation Between Influenza and COVID-19 Patients |
| title_full_unstemmed | Differences in Immunoglobulin G Glycosylation Between Influenza and COVID-19 Patients |
| title_short | Differences in Immunoglobulin G Glycosylation Between Influenza and COVID-19 Patients |
| title_sort | differences in immunoglobulin g glycosylation between influenza and covid 19 patients |
| topic | Influenza COVID-19 Viral infection Glycosylation Immunoglobulin G Pneumonia |
| url | http://www.sciencedirect.com/science/article/pii/S2095809922006312 |
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