The role of galectins in virus infection - A systemic literature review

Wang, Wen Hung; Lin, Chia-Yang; Chang, Max R.; Urbina, Aspiro Nayim; Assavalapsakul, Wanchai; Thitithanyanont, Arunee; Chen, Yen Hsu; Liu, Fu Tong; Wang, Sheng-Fan

doi:10.1016/j.jmii.2019.09.005

Cited by 107 publications

(138 citation statements)

References 65 publications

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“…Mucin MUC5AC, which is glycosylated by HBGAs (Lewis b), can promote Helicobacter pylori infection, but mucin MUC6 glycosylated by GlcNAc-capped glycans, can inhibit H. pylori infection [16,33]. In general, protein glycosylation in host strongly impacts pathogen binding and invasion [70][71][72].…”

Section: Host-pathogen Interactionsmentioning

confidence: 99%

“…Besides, lectins can also be assigned based on the domain architecture, resulting merolectins (contain a single CBD), hololectins (contain two or more same CBDs), chimerolentins (contain CBD(s) and other domains independent from lectin domain) and superlectins (contain two different CBDs) [99]. Lectins have a variety of functions in vivo, such as participating in host-pathogen interaction [72,182], inhibiting nutrition absorption [189], intercellular recognition [190], cell migration [191] and signal transduction [111]. These functions rely on the sugar-binding activity of lectins.…”

Section: Lectin a Class Of Protein Entangled With Glycoprotein Affementioning

confidence: 99%

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Role of Protein Glycosylation in Host-Pathogen Interaction

Lin

Xue

Liao

et al. 2020

Cells

125

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Host-pathogen interactions are fundamental to our understanding of infectious diseases. Protein glycosylation is one kind of common post-translational modification, forming glycoproteins and modulating numerous important biological processes. It also occurs in host-pathogen interaction, affecting host resistance or pathogen virulence often because glycans regulate protein conformation, activity, and stability, etc. This review summarizes various roles of different glycoproteins during the interaction, which include: host glycoproteins prevent pathogens as barriers; pathogen glycoproteins promote pathogens to attack host proteins as weapons; pathogens glycosylate proteins of the host to enhance virulence; and hosts sense pathogen glycoproteins to induce resistance. In addition, this review also intends to summarize the roles of lectin (a class of protein entangled with glycoprotein) in host-pathogen interactions, including bacterial adhesins, viral lectins or host lectins. Although these studies show the importance of protein glycosylation in host-pathogen interaction, much remains to be discovered about the interaction mechanism.

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Section: Host-pathogen Interactionsmentioning

confidence: 99%

Section: Lectin a Class Of Protein Entangled With Glycoprotein Affementioning

confidence: 99%

Role of Protein Glycosylation in Host-Pathogen Interaction

Lin

Xue

Liao

et al. 2020

Cells

125

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“…LGALS3) 15,16 . In set 5, cell-cycle genes (CDK1, KIFs, PCNA, CCNA/B2), stress-associated genes (HSPD1, HSP90AA1, BIRC5) and chromatin re-modelling related genes (e.g., HMGB2, HMGB3, EZH2) were increased, suggesting that T-cells were largely adjusting to inflammation-driven stress (rather than mounting any discernible effector or auto-regulatory responses).…”

Section: Gene Expression Modelling Along the Cd8 + T Rm -And T Ex -Limentioning

confidence: 99%

Discriminating Mild from Critical COVID-19 by Innate and Adaptive Immune Single-cell Profiling of Bronchoalveolar Lavages

Wauters

Mol

Garg

et al. 2020

Preprint

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How innate and adaptive lung immune responses to SARS-CoV-2 synchronize during COVID-19 pneumonitis and regulate disease severity is poorly established. To address this, we applied single-cell profiling to bronchoalveolar lavages from 44 patients with mild or critical COVID-19 versus non-COVID-19 pneumonia as control. Viral RNA-tracking delineated the infection phenotype to epithelial cells, but positioned mainly neutrophils at the forefront of viral clearance activity during COVID-19. In mild disease, neutrophils could execute their antiviral function in an immunologically controlled fashion, regulated by fully-differentiated T-helper-17 (TH17)-cells, as well as T-helper-1 (TH1)-cells, CD8+ resident-memory (TRM) and partially-exhausted (TEX) T-cells with good effector functions. This was paralleled by orderly phagocytic disposal of dead/stressed cells by fully-differentiated macrophages, otherwise characterized by anti-inflammatory and antigen-presenting characteristics, hence facilitating lung tissue repair. In critical disease, CD4+ TH1- and CD8+ TEX-cells were characterized by inflammation-associated stress and metabolic exhaustion, while CD4+ TH17- and CD8+ TRM-cells failed to differentiate. Consequently, T-cell effector function was largely impaired thereby possibly facilitating excessive neutrophil-based inflammation. This was accompanied by impaired monocyte-to-macrophage differentiation, with monocytes exhibiting an ATP-purinergic signalling-inflammasome footprint, thereby enabling COVID-19 associated fibrosis and worsening disease severity. Our work represents a major resource for understanding the lung-localised immunity and inflammation landscape during COVID-19.

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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 role of galectins in virus infection - A systemic literature review

Cited by 107 publications

References 65 publications

Role of Protein Glycosylation in Host-Pathogen Interaction

Role of Protein Glycosylation in Host-Pathogen Interaction

Discriminating Mild from Critical COVID-19 by Innate and Adaptive Immune Single-cell Profiling of Bronchoalveolar Lavages

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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