The Importance of Glycosylation in COVID-19 Infection

Petrović, Tea; Lauc, Gordan; Trbojević‐Akmačić, Irena

doi:10.1007/978-3-030-70115-4_12

Cited by 9 publications

(5 citation statements)

References 257 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, these glycosylation sites are rare in field RVA strains. Glycosylation determines viral immunogenicity by modulating virus receptor binding or masking antigenic sites, as in SARS-CoV-2 (Petrovic et al, 2021). Further studies should address whether these glycosylation sites alter the antigenicity of VP7 (Zeller et al, 2012;Harastani et al, 2020) The G4 and P[6] genotypes in this study displayed marked intra-genotypic variety and high homology to porcine strains, indicating spillover of G4 and P[6] from pigs to humans in China.…”

Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Phylogenetic analysis of the viral proteins VP4/VP7 of circulating human rotavirus strains in China from 2016 to 2019 and comparison of their antigenic epitopes with those of vaccine strains

Mao

Wang

et al. 2022

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

Group A rotaviruses (RVAs) are the most common etiological agents of severe acute diarrhea among children under 5 years old worldwide. At present, two live-attenuated RVA vaccines, LLR (G10P[15]) and RotaTeq (G1–G4, G6 P[8], P[5]), have been introduced to mainland China. Although RVA vaccines can provide homotypic and partially heterotypic protection against several strains, it is necessary to explore the genetic and antigenic variations between circulating RVAs and vaccine strains. In this study, we sequenced viral protein VP7 and VP4 outer capsid proteins of 50 RVA strains circulating in China from 2016 to 2019. The VP7 and VP4 sequences of almost all strains showed high homology to those of previously reported human strains and vaccine strains of the same genotype. However, in the presumed antigenic epitopes of the VP7 and VP4, multiple amino acid variations were found, regardless of the G and P genotypes of these strains. Moreover, all circulating G3 RVA strains in China potentially possess an extra N-linked glycosylation site compared with the G3 strain of RotaTeq. The potential N-linked glycosylation site at residues 69–71 was found in all G9 strains in China but not in the G9 strain of the Rotavac or Rotasill vaccine. These variations in antigenic sites might result in the selection of strains that escape the RVA neutralizing-antibody pressure imposed by vaccines. Furthermore, the G4 and P[6] genotypes in this study showed high homology to those of porcine strains, indicating the transmission of G4 and P[6] genotypes from pigs to humans in China. More genetic surveillance with antigenic evaluation in prevalent RVAs is necessary for developing and implementing rotavirus vaccines in China.

show abstract

Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 99%

Phylogenetic analysis of the viral proteins VP4/VP7 of circulating human rotavirus strains in China from 2016 to 2019 and comparison of their antigenic epitopes with those of vaccine strains

Mao

Wang

et al. 2022

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

show abstract

“…However, O-linked glycosylation has not been reported in immunoglobulin light chains; except in recombinant, therapeutic, antibodies engineered in order to alter their pharmacokinetic/pharmacodynamics properties [8], [28]. A distinct glycosylation profile of anti-SARS-CoV 2 IgG was previously reported, with changes associated with increasing COVID-19 disease severity [29]. Here we report the mass analysis of captured SARS-CoV2 specific, Ig light chains to observe disease dependent patterns.…”

Section: Discussionmentioning

confidence: 99%

Degree of immunoglobulin kappa light chain glycosylation of anti-spike SARS CoV-2 antibodies correlates with COVID-19 severity

Grigaite

Iles

Harding³

et al. 2023

Preprint

View full text Add to dashboard Cite

Glycosylation of antibodies and the effects this has on inflammatory responses has concentrated predominately on the study of glycosylation moieties found in the Fc region of heavy chains. Light chain glycosylation and their ratios are relatively understudied. Nevertheless, variable glycosylation and ratio of κ and λ light chains have been associated with worse prognosis in myeloma and in tissue deposition – amyloidosis.The κ & λ light chains, of antibodies binding to SARS-CoV2 nucleocapsid and spike protein were analysed, using MALDI-ToF MS, in respect to their intensity, ratios, glycosylation patterns and any pattern changes correlating with COVID-19 severity. The molecular masses and signal intensity of κ and λ glycosylated and non-glycosylated light chains were measured for immunoglobulins isolated from plasma of sero-positive and sero-negative health care workers (HCW), and convalescent patients who had suffered from acute respiratory distress syndrome (ARDS).Overall, there was no significant changes in κ to λ ratio of total IgG (via protein G capture) antibodies between the groups. A non-statistically significant trend towards λ light chains was found in antibodies against SARS CoV-2 Nucleocapsid and Spike proteins. However, detailed analysis of the molecular forms found a significant increase and bias towards un-glycosylated light chains and in particular un-glycosylated κ light chains, in antibodies against SAR-CoV-2 spike protein, from convalescent COVID-ARDS patients.Here we have demonstrated a bias towards un-glycosylated κ chains in anti-spike antibodies in those who suffered from ARDS as a result of SARS-CoV2 infection 3 months after recovery. How this relates to the immunopathology of COVID-19 requires further study.

show abstract

“…[1183][1184][1185][1186][1187][1188] COVID-19 caused by SARS-CoV-2 is currently a major global health problem. 1189 Protein glycosylation affects the toxicity and viability of SARS-CoV-2, which utilizes its highly glycosylated modified spike (S) protein to interact with the glycosylated host receptor ACE2 and to facilitate SARS-CoV-2 invasion of host cells. 1127 Acquired immune deficiency syndrome caused by human immunodeficiency virus (HIV) seriously endangers human health.…”

Section: Glycosylation In Virusesmentioning

confidence: 99%

“…Protein glycosylation is involved in the regulation of host–pathogen interactions and mediates the adhesion, recognition, invasion and immune evasion of pathogens in host cells, which affects pathogen virulence or host cell resistance 1183–1188 . COVID‐19 caused by SARS‐CoV‐2 is currently a major global health problem 1189 . Protein glycosylation affects the toxicity and viability of SARS‐CoV‐2, which utilizes its highly glycosylated modified spike (S) protein to interact with the glycosylated host receptor ACE2 and to facilitate SARS‐CoV‐2 invasion of host cells 1127 …”

Section: Glycosylationmentioning

confidence: 99%

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong

Xiao

Xie

et al. 2023

MedComm

View full text Add to dashboard Cite

Protein posttranslational modifications (PTMs) refer to the breaking or generation of covalent bonds on the backbones or amino acid side chains of proteins and expand the diversity of proteins, which provides the basis for the emergence of organismal complexity. To date, more than 650 types of protein modifications, such as the most well‐known phosphorylation, ubiquitination, glycosylation, methylation, SUMOylation, short‐chain and long‐chain acylation modifications, redox modifications, and irreversible modifications, have been described, and the inventory is still increasing. By changing the protein conformation, localization, activity, stability, charges, and interactions with other biomolecules, PTMs ultimately alter the phenotypes and biological processes of cells. The homeostasis of protein modifications is important to human health. Abnormal PTMs may cause changes in protein properties and loss of protein functions, which are closely related to the occurrence and development of various diseases. In this review, we systematically introduce the characteristics, regulatory mechanisms, and functions of various PTMs in health and diseases. In addition, the therapeutic prospects in various diseases by targeting PTMs and associated regulatory enzymes are also summarized. This work will deepen the understanding of protein modifications in health and diseases and promote the discovery of diagnostic and prognostic markers and drug targets for diseases.

show abstract

The Importance of Glycosylation in COVID-19 Infection

Cited by 9 publications

References 257 publications

Phylogenetic analysis of the viral proteins VP4/VP7 of circulating human rotavirus strains in China from 2016 to 2019 and comparison of their antigenic epitopes with those of vaccine strains

Phylogenetic analysis of the viral proteins VP4/VP7 of circulating human rotavirus strains in China from 2016 to 2019 and comparison of their antigenic epitopes with those of vaccine strains

Degree of immunoglobulin kappa light chain glycosylation of anti-spike SARS CoV-2 antibodies correlates with COVID-19 severity

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Contact Info

Product

Resources

About