The Sweet-Side of Leukocytes: Galectins as Master Regulators of Neutrophil Function

Robinson, Brian; Arthur, Connie M.; Evavold, Birk; Roback, Ethan; Kamili, Nourine A.; Stowell, Caleb S; Vallecillo-Zúniga, Mary L.; Ry, Pam M. Van; Dias‐Baruffi, Marcelo; Cummings, Richard D.; Stowell, Sean R.

doi:10.3389/fimmu.2019.01762

Cited by 51 publications

(35 citation statements)

References 197 publications

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“…Glycans also play crucial and multifaceted roles in B cell and T cell differentiation via cell-surface or secreted proteins, including selectins, galectins, and siglecs, which can further connect SARS-CoV-2 to immune response and immune regulation (27). In particular, the complex N-glycans are ligands for galectins, which are able to engage different glycoproteins to regulate immune cell infiltration and activation upon virus infection (33,34). These mechanisms underlying SARS-CoV-2 infection and spread are worth further clarification based on a detailed analysis of clinical characteristics in humoral and cellular immunity.…”

Section: Discussionmentioning

confidence: 99%

Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins

Zhang

Zhao

Mao

et al. 2020

Preprint

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SummaryThe glycoprotein spike (S) on the surface of SARS-CoV-2 is a determinant for viral invasion and host immune response. Herein, we characterized the site-specific N-glycosylation of S protein at the level of intact glycopeptides. All 22 potential N-glycosites were identified in the S-protein protomer and were found to be preserved among the 753 SARS-CoV-2 genome sequences. The glycosites exhibited glycoform heterogeneity as expected for a human cell-expressed protein subunits. We identified masses that correspond to 157 N-glycans, primarily of the complex type. In contrast, the insect cell-expressed S protein contained 38 N-glycans, primarily of the high-mannose type. Our results revealed that the glycan types were highly determined by the differential processing of N-glycans among human and insect cells. This N-glycosylation landscape and the differential N-glycan patterns among distinct host cells are expected to shed light on the infection mechanism and present a positive view for the development of vaccines and targeted drugs.

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Section: Discussionmentioning

confidence: 99%

Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins

Zhang

Zhao

Mao

et al. 2020

Preprint

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“…Galectins are another key family of GBPs implicated in virtually all aspects of the immune system (Brinchmann et al, 2018;Elola et al, 2018;Robinson et al, 2019). Galectins are expressed in many cell types including those of squamous epithelia, gastrointestinal tract, adipocytes, immune cells, and even erythrocytes (Thiemann and Baum, 2016).…”

Section: Galectinsmentioning

confidence: 99%

Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins

et al. 2019

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Glycans and glycan binding proteins (GBPs or lectins) are essential components in almost every aspect of immunology. Investigations of the interactions between glycans and GBPs have greatly advanced our understanding of the molecular basis of these fundamental immunological processes. In order to better study the glycan-GBP interactions, microscope glass slide-based glycan microarrays were conceived and proved to be an incredibly useful and successful tool. A variety of methods have been developed to better present the glycans so that they mimic natural presentations. Breakthroughs in chemical biology approaches have also made available glycans with sophisticated structures that were considered practically impossible just a few decade ago. Glycan microarrays provide a wealth of valuable information in immunological studies. They allow for discovery of detailed glycan binding preferences or novel binding epitopes of known endogenous immune receptors, which can potentially lead to the discovery of natural ligands that carry the glycans. Glycan microarrays also serve as a platform to discover new GBPs that are vital to the process of infection and invasion by microorganisms. This review summarizes the construction strategies and the immunological applications of glycan microarrays, particularly focused on those with the most comprehensive sets of glycan structures. We also review new methods and technologies that have evolved. We believe that glycan microarrays will continue to benefit the growing research community with various interests in the field of immunology.

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“…On the other hand, protein glycosylation can also facilitate immune response by sensor molecules or antibodies specific for glycan recognition. N-glycans are known ligands for galectins, which triggers inflammation events such as cytokine release, immune cell infiltration (Robinson et al, 2019; Wang et al, 2019), of which may contribute to the HCoV-19 pathogenesis and correlated with the disease severity. Moreover, epidemiological studies have shown that ABO polymorphism are linked to different susceptibility to both HCoV-19 and SARS-CoV infections (Cheng et al, 2005; Zhao et al, 2020).…”

Section: Discussionmentioning

confidence: 99%

Mass spectrometry analysis of newly emerging coronavirus HCoV-19 spike S protein and human ACE2 reveals camouflaging glycans and unique post-translational modifications

Sun

Ren

Zhang

et al. 2020

Preprint

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The pneumonia-causing COVID-19 pandemia has prompt worldwide efforts to understand its biological and clinical traits of newly identified HCoV-19 virus. In this study, post-translational modification (PTM) of recombinant HCoV-19 S and hACE2 were characterized by LC-MSMS. We revealed that both proteins were highly decorated with specific proportions of N-glycan subtypes. Out of 21 possible glycosites in HCoV-19 S protein, 20 were confirmed completely occupied by N-glycans, with oligomannose glycans being the most abundant type. All 7 possible glycosylation sites in hACE2 were completely occupied mainly by complex type N-glycans. However, we showed that glycosylation did not directly contribute to the binding affinity between SARS-CoV spike protein and hACE2. Additionally, we also identified multiple sites methylated in both proteins, and multiple prolines in hACE2 were converted to hydroxylproline. Refined structural models were built by adding N-glycan and PTMs to recently published cryo-EM structure of the HCoV-19 S and hACE2 generated with glycosylation sites in the vicinity of binding surface. The PTM and glycan maps of both HCoV-19 S and hACE2 provide additional structural details to study mechanisms underlying host attachment, immune response mediated by S protein and hACE2, as well as knowledge to develop remedies and vaccines desperately needed nowadays.

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The Sweet-Side of Leukocytes: Galectins as Master Regulators of Neutrophil Function

Cited by 51 publications

References 197 publications

Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins

Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins

Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins

Mass spectrometry analysis of newly emerging coronavirus HCoV-19 spike S protein and human ACE2 reveals camouflaging glycans and unique post-translational modifications

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