Utilization of Galectins by Pathogens for Infection

Ayona, Diyoly; Fournier, Pierre‐Edouard; Henrissat, Bernard; Desnues, Benoît

doi:10.3389/fimmu.2020.01877

Cited by 23 publications

(18 citation statements)

References 154 publications

(209 reference statements)

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“…Emerging evidences emphasize that in some cases, these galectin-glycan interactions may benefit the pathogen by providing the ability to adhere, by enhancing uptake as well as by modulating immune effector functions. 32 T. whipplei is an intracellular bacterium which replicates in alternatively activated macrophages. Although, it has been shown that T. whipplei glycoproteins are important for bacterial replication in macrophages, their contribution during the infection process is not well understood.…”

Section: Discussionmentioning

confidence: 99%

“…Several studies have demonstrated that external addition of soluble Gal-1 and Gal-3 either enhance or inhibit cell entry of some pathogens. 32 For example, soluble Gal-1 enhances C. trachomatis uptake in a dose-dependent manner in vitro 34 while for T. cruzi , cell adhesion is increased with the addition of soluble Gal-3. 37 In contrast, addition of Gal-1 inhibits the internalization of Dengue virus and Nipah Virus.…”

Section: Discussionmentioning

confidence: 99%

“… 31 However, some pathogens have evolved strategies to utilize host galectins to enhance host cell entry and/or to subvert immune responses. 32 For example, Gal-1 enhances adherence of HIV-1 and Chlamydia trachomatis to their target cells by bridging glycans on host cell, 33 , 34 while for Trichomonas vaginalis , Gal-1 not only enhances the adherence but also subverts immune responses in favor of the pathogen. 35 , 36 Similarly, Gal-3 interaction with glycans expressed on Trypanosoma cruzi favors parasite attachment to target cells as well as immune evasion.…”

Section: Introductionmentioning

confidence: 99%

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Human galectin-1 and galectin-3 promote Tropheryma whipplei infection

Ayona

Zarza

Landemarre³

et al. 2021

Gut Microbes

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Tropheryma whipplei , is an actinobacterium that causes different infections in humans, including Whipple’s disease. The bacterium infects and replicates in macrophages, leading to a Th2-biased immune response. Previous studies have shown that T. whipplei harbors complex surface glycoproteins with evidence of sialylation. However, the exact contribution of these glycoproteins for infection and survival remains obscure. To address this, we characterized the bacterial glycoprofile and evaluated the involvement of human β-galactoside-binding lectins, Galectin-1 (Gal-1) and Galectin-3 (Gal-3) which are highly expressed by macrophages as receptors for bacterial glycans. Tropheryma whipplei glycoproteins harbor different sugars including glucose, mannose, fucose, β-galactose and sialic acid. Mass spectrometry identification revealed that these glycoproteins were membrane- and virulence-associated glycoproteins. Most of these glycoproteins are highly sialylated and N-glycosylated while some of them are rich in poly-N-acetyllactosamine (Poly-LAcNAc) and bind Gal-1 and Gal-3. In vitro, T. whipplei modulates the expression and cellular distribution of Gal-1 and Gal-3. Although both galectins promote T. whipplei infection by enhancing bacterial cell entry, only Gal-3 is required for optimal bacterial uptake. Finally, we found that serum levels of Gal-1 and Gal-3 were altered in patients with T. whipplei infections as compared to healthy individuals, suggesting that galectins are also involved in vivo . Among T. whipplei membrane-associated proteins, poly-LacNAc rich-glycoproteins promote infection through interaction with galectins. T. whipplei modulates the expression of Gal-1 and Gal-3 both in vitro and in vivo . Drugs interfering with galectin–glycan interactions may provide new avenues for the treatment and diagnosis of T. whipplei infections.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Human galectin-1 and galectin-3 promote Tropheryma whipplei infection

Ayona

Zarza

Landemarre³

et al. 2021

Gut Microbes

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“…As is the case with many immunoregulatory proteins, galectin expression is modulated with EC activation in response to inflammatory mediators, pathogen exposure, and injury (22,(33)(34)(35). A concentration-dependent increase in expression of galectin-9 mRNA and protein was observed in vitro following treatment of primary HUVEC with double-stranded RNA viral mimetic, polyinosinic-polycytidylic acid [poly(I:C)], a Toll-like receptor (TLR) 3 ligand (33,34).…”

Section: Regulation Of Galectin Expression In Inflammationmentioning

confidence: 99%

Vascular Endothelial Galectins in Leukocyte Trafficking

2021

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Leukocyte recruitment to the site of injury is a crucial event in the regulation of an inflammatory response. Tight regulation of interactions between the endothelium and circulating leukocytes is necessary to ensure a protective response to injury does not result in inflammatory disease. Rising interest in the broad immunoregulatory roles displayed by members of the glycan-binding galectin family suggests that these proteins could be an attractive target for therapeutic intervention, since their expression is significantly altered in disease. The focus of this review is to summarize current knowledge on the role of galectins in leukocyte trafficking during inflammation and the clinical approaches being taken to target these interactions for treatment of inflammatory disease.

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“…Galectins are a family of small soluble proteins able to recognize glycans containing a β‐ d ‐galactopyranoside structural motif [1–4] . They are found both intracellularly and extracellularly, where they are involved in many physiological and pathological functions, such as metabolism, immunity, inflammation and cancer progression [4–8] …”

Section: Introductionmentioning

confidence: 99%

Selective Monovalent Galectin‐8 Ligands Based on 3‐Lactoylgalactoside

et al. 2021

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Galectin‐8 has gained attention as a potential new pharmacological target for the treatment of various diseases, including cancer, inflammation, and disorders associated with bone mass reduction. To that end, new molecular probes are needed in order to better understand its role and its functions. Herein we aimed to improve the affinity and target selectivity of a recently published galectin‐8 ligand, 3‐O‐[1‐carboxyethyl]‐β‐d‐galactopyranoside, by introducing modifications at positions 1 and 3 of the galactose. Affinity data measured by fluorescence polarization show that the most potent compound reached a KD of 12 μM. Furthermore, reasonable selectivity versus other galectins was achieved, making the highlighted compound a promising lead for the development of new selective and potent ligands for galectin‐8 as molecular probes to examine the protein's role in cell‐based and in vivo studies.

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Utilization of Galectins by Pathogens for Infection

Cited by 23 publications

References 154 publications

Human galectin-1 and galectin-3 promote Tropheryma whipplei infection

Human galectin-1 and galectin-3 promote Tropheryma whipplei infection

Vascular Endothelial Galectins in Leukocyte Trafficking

Selective Monovalent Galectin‐8 Ligands Based on 3‐Lactoylgalactoside

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