Viral glycoproteomes: technologies for characterization and outlook for vaccine design

Bagdonaite, Ieva; Vakhrushev, Sergey Y.; Joshi, Hiren J.; Wandall, Hans H.

doi:10.1002/1873-3468.13177

Cited by 26 publications

(20 citation statements)

References 237 publications

(354 reference statements)

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“…In fact, additionally to forming vital structural options, the sugar elements of glycoconjugates modulate or mediate a good form of functions in physiological and pathophysiological states. Glycoproteins and polysaccharides have vital functions in viral cells, and even glycoproteins have central roles within the biology of most viruses [10,12]. Glycoconjugates are measured by the addition of sugars to proteins and lipids.…”

Section: Glycosylation and Its Role In Onset Of Diseasementioning

confidence: 99%

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Glycan and Its Role in Combating COVID-19

Chatterjee¹,

Saha²

2022

Biotechnology to Combat COVID-19

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Newly identified beta-coronavirus i.e. the 2019 novel coronavirus is associated with a contagious transmittable respiratory disease called COVID-19. This disease has been declared as a “pandemic” by the World Health Organization (WHO). The entry of coronavirus in the human respiratory epithelial cells depends upon the interaction between host cell receptor ACE2 and viral S-glycoprotein. However, this type of molecular recognition in between cell surface receptors and envelope glycoproteins are mediated by specific glycan epitopes and attribute to viral entry through membrane fusion. Glycans are essential biomolecules made by all living organisms, have roles in serving structure, energy storage, and system regulatory purposes. The glycan shield plays a crucial role in concealing the surface S protein from molecular recognition. The immunomodulatory properties of Glycan-binding proteins (GBPs) like Lectins, build them as an attractive candidates for vaccine adjuvant. Investigations involving the complement system activation by the lectin pathway in COVID-19 and diseases are in need of the hour. The innate immune response involving complement system could have varied biological effects against an array of microbial infections. The advances in glycoprotein style methods especially immunomodulatory action of some lectins are necessary to boost the effectiveness of treatment of COVID-19 and other pandemics.

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Section: Glycosylation and Its Role In Onset Of Diseasementioning

confidence: 99%

“…The glycome is created in a non-templated manner and is in an elaborate way controlled at multiple levels within the ER and cyst, unlike exome or proteome [12,13].…”

Section: Glycosylation and Its Role In Onset Of Diseasementioning

confidence: 99%

Glycan and Its Role in Combating COVID-19

Chatterjee¹,

Saha²

2022

Biotechnology to Combat COVID-19

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“…Glycan mimetics can inhibit influenza escape (i.e., oseltamivir (Tamiflu) and zanamivir (Relenza)) [32], facilitate anticoagulation (i.e., heparin) [33], and block SARS-CoV-2 spike-ACE2 binding [34,35]. Human milk oligosaccharides are associated with increased survival in preterm infants [36] and decreased risk of necrotizing enterocolitis [37], and glycosylation is being incorporated into vaccine development [38]. The global impact of glycosylation is undeniable.…”

Section: Glossarymentioning

confidence: 99%

Big-Data Glycomics: Tools to Connect Glycan Biosynthesis to Extracellular Communication

Kellman

Lewis

2021

Trends in Biochemical Sciences

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Characteristically, cells must sense and respond to environmental cues. Despite the importance of cell-cell communication, our understanding remains limited and often lacks glycans. Glycans decorate proteins and cell membranes at the cell-environment interface, and modulate intercellular communication, from development to pathogenesis. Providing further challenges, glycan biosynthesis and cellular behavior are co-regulating systems. Here, we discuss how glycosylation contributes to extracellular responses and signaling. We further organize approaches for disentangling the roles of glycans in multicellular interactions using newly available datasets and tools, including glycan biosynthesis models, omics datasets, and systems-level analyses. Thus, emerging tools in big data analytics and systems biology are facilitating novel insights on glycans and their relationship with multicellular behavior. Extracellular Glycans Influence Intercellular BehaviorEvery cell and many viruses are wrapped in a sugar-coating of functional glycans (see Glossary) and glycoconjugates that helps modulate cell-cell communication, the glycocalyx. Glycans are bound to peptide or lipid glycoconjugates and matured in the endomembrane system. They then reside on the cell surface or diffuse into the extracellular matrix (ECM). The emergence, recycling, and dispersion of glycans is often slow, variable, and glycoconjugate dependent (2-1000 h); therefore, environmentally responsive nascent glycans do not transform the cell surface immediately [1,2]. Instead, the glycocalyx constitutes a composite memory of recent and current responses to intercellular exchanges. Together, the glycocalyx, the communication-modulating glycans and glycoconjugates between conversing cells form a rich resource that can be leveraged to improve our understanding of how cells communicate (Figure 1, Key Figure ).ECM glycans are voluminous, ubiquitous, and diverse, extending to 2-3 times the cell diameter [3]. With 4549 of 20 365 reviewed human proteins (UniProtKB) corresponding to~250 000 proteoforms per cell type [4], there are~50 glycoforms for every glycoprotein. Glycan metabolism uses 342 documented [5] human glycosyltransferases and glycosidases, each performing interdependent and distinct monosaccharide additions and removals. Borrowing from epigenetics, lectins, glycosyltransferases, and glycosidases have been described as the readers, writers, and erasers of the glycocalyx [6,7]. These encapsulating carbohydrates moderate many cellular responses, including development, growth, differentiation, migration, signaling, and morphogenesis (Table 1) making few biological discussions complete outside the glycan context (Figure 2) [8].Today, we are seeing glycan essentiality and neglect in the study of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the COVID-19 causative agent (Figure 2C). Because cells and viruses are wrapped in glycans, glycans moderate the first host-pathogen interactions, including immune evasion through viral glycosylation [9,10] and h...

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“…Different viruses have varying preferences for the two different types of glycans, with e.g. HIV-1, HCV and influenza virus having dense N-glycosylation on their surface proteins, whereas Ebola virus and herpesviruses additionally have many O-linked glycans [11]. Furthermore, both types of site-specific glycosylation have been shown to affect viral glycoprotein secretion or function [12].…”

Section: Introductionmentioning

confidence: 99%

Site-specific O-glycosylation analysis of SARS-CoV-2 spike protein produced in insect and human cells

Bagdonaite

Thompson

Wang

et al. 2021

Preprint

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Enveloped viruses hijack not only the host translation processes, but also its glycosylation machinery, and to a variable extent cover viral surface proteins with tolerogenic host-like structures. SARS-CoV-2 surface protein S presents as a trimer on the viral surface and is covered by a dense shield of N-linked glycans, and a few O-glycosites have been reported. The location of O-glycans is controlled by a large family of initiating enzymes with variable expression in cells and tissues and hence difficult to predict. Here, we used our well-established O-glycoproteomic workflows to map the precise positions of O-linked glycosylation sites on three different entities of protein S — insect cell or human cell-produced ectodomains, or insect cell derived receptor binding domain (RBD). In total 25 O-glycosites were identified, with similar patterns in the two ectodomains of different cell origin, and a distinct pattern of the monomeric RBD. Strikingly, 16 out of 25 O-glycosites were located within three amino acids from known N-glycosites. However, O-glycosylation was primarily found on peptides that were unoccupied by N-glycans, and otherwise had low overall occupancy. This suggests possible complimentary functions of O-glycans in immune shielding and negligible effects of O-glycosylation on subunit vaccine design for SARS-CoV-2.

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Viral glycoproteomes: technologies for characterization and outlook for vaccine design

Cited by 26 publications

References 237 publications

Glycan and Its Role in Combating COVID-19

Glycan and Its Role in Combating COVID-19

Big-Data Glycomics: Tools to Connect Glycan Biosynthesis to Extracellular Communication

Site-specific O-glycosylation analysis of SARS-CoV-2 spike protein produced in insect and human cells

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