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Engineering 2023年第7期26卷 54-62,I0003页

作者： Marina Kljakovic-Gašpic Batinjan Tea Petrovic Frano Vuckovic irzal hadz ibegovic Barbara Radovani Ivana Jurin LovorkaÐerek Eva Huljev Alemka Markotic Ivica Lukšic Irena Trbojevic´-Akmacic Gordan Lauc Ivan Gudelj Rok Civljak University Hospital Centre Zagreb Zagreb 10000Croatia Genos Glycoscience Research Laboratory Zagreb 10000Croatia Department of Cardiology University Hospital DubravaZagreb 10000Croatia Faculty of Dental Medicine and Health Josip Juraj Strossmayer UniversityOsijek 31000Croatia Department of Biotechnology University of RijekaRijeka 51000Croatia Department for Laboratory Diagnostics University Hospital DubravaZagreb 10000Croatia Department for Acute Respiratory Infections University Hospital for Infectious Diseases“Dr.Fran Mihaljevic”Zagreb 10000Croatia Department for Urogenital Infections University Hospital for Infectious Diseases“Dr.Fran Mihaljevic”Zagreb 10000Croatia Department for Infectious Diseases School of MedicineCatholic University of Croatia10000 ZagrebCroatia Postdoctoral Study Faculty of MedicineUniversity of RijekaRijeka 51000Croatia Department of Maxillofacial Surgery University of Zagreb School of MedicineDubrava University HospitalZagreb 10000Croatia Faculty of Pharmacy and Biochemistry University of ZagrebZagreb 10000Croatia Department of Infectious Diseases University of Zagreb School of MedicineZagreb 10000Croatia

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 *** glycans impact the antibody stability,half-life,secretion,immunogenicity,and effector ***,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 Nacetylglucosamine(GlcNAc))—of 64 patients with influenza,77 patients with coronavirus disease 2019(COVID-19),and 56 healthy *** study revealed a significant decrease in IgG galactosylation,sialylation,and bisecting GlcNAc(where the latter shows the most significant decrease)in deceased COVID19 patients,whereas IgG fucosylation was *** the other hand,IgG galactosylation remained stable in influenza patients and COVID-19 *** 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.

关键词： Influenza COVID-19 Viral infection Glycosylation Immunoglobulin G Pneumonia

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流感与COVID-19患者的免疫球蛋白G糖基化差异（英文）

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Engineering 2023年第7期 54-62页

作者： Marina Kljakovi?-Ga?pi? Batinjan Tea Petrovi? Frano Vu?kovi? irzal Had?ibegovi? Barbara Radovani Ivana Jurin Lovorka Derek Eva Huljev Alemka Markoti? Ivica Luk?i? Irena Trbojevi?-Akma?i? Gordan Lauc Ivan Gudelj Rok ?ivljak University Hospital Centre Zagreb Genos Glycoscience Research Laboratory Department of Cardiology University Hospital Dubrava Faculty of Dental Medicine and Health Josip Juraj Strossmayer University Department of Biotechnology University of Rijeka Department for Laboratory Diagnostics University Hospital Dubrava Department for Acute Respiratory Infections University Hospital for Infectious Diseases “Dr. Fran Mihaljevi?” 8. Department for Urogenital Infections University Hospital for Infectious Diseases “Dr. Fran Mihaljevi?” 9. Department for Infectious Diseases School of Medicine Catholic University of Croatia Postdoctoral Study Faculty of Medicine University of Rijeka Department of Maxillofacial Surgery University of Zagreb School of Medicine Dubrava University Hospital Faculty of Pharmacy and Biochemistry University of Zagreb Department of Infectious Diseases University of Zagreb School of Medicine

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 *** glycans impact the antibody stability, half-life, secretion, immunogenicity, and effector ***, 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.

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