Pregled bibliografske jedinice broj: 1212605
Differences in immunoglobulin G glycosylation between influenza and COVID-19 patients
Differences in immunoglobulin G glycosylation between influenza and COVID-19 patients // Engineering (2022) doi:10.1016/j.eng.2022.08.007 (znanstveni, online first)
CROSBI ID: 1212605 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Differences in immunoglobulin G glycosylation
between influenza and COVID-19 patients
Autori
Kljaković-Gašpić Batinjan, Marina ; Petrović, Tea ; Vučković, Frano ; Hadžibegović, Irzal ; Radovani, Barbara ; Jurin, Ivana ; Đerek, Lovorka ; Huljev, Eva ; Markotić, Alemka ; Lukšić, Ivica ; Trbojević-Akmačić, Irena ; Lauc, Gordan ; Gudelj, Ivan ; Čivljak, Rok
Vrsta, podvrsta
Radovi u časopisima,
znanstveni
Izvornik
Engineering (2022)
Status rada
Online first
Ključne riječi
influenza ; COVID-19 ; viral infection ; glycosylation ; immunoglobulin G ; pneumonia
Sažetak
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 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.
Izvorni jezik
Engleski
Znanstvena područja
Biologija, Interdisciplinarne prirodne znanosti
POVEZANOST RADA
Ustanove:
Farmaceutsko-biokemijski fakultet, Zagreb,
Medicinski fakultet, Rijeka,
Medicinski fakultet, Zagreb,
Klinika za infektivne bolesti "Dr Fran Mihaljević",
Klinička bolnica "Dubrava",
GENOS d.o.o.,
Hrvatsko katoličko sveučilište, Zagreb,
Sveučilište u Rijeci - Odjel za biotehnologiju,
Fakultet za dentalnu medicinu i zdravstvo, Osijek
Profili:
Alemka Markotić
(autor)
Tea Petrović
(autor)
Gordan Lauc
(autor)
Rok Čivljak
(autor)
Irzal Hadžibegović
(autor)
Ivan Gudelj
(autor)
Lovorka Đerek
(autor)
IRENA TRBOJEVIĆ AKMAČIĆ
(autor)
Barbara Radovani
(autor)
Frano Vučković
(autor)
Ivica Lukšić
(autor)
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus