Galectin Regulation of Host Microbial Interactions

Robinson, Brian; Arthur, Connie M.; Stowell, Sean R.

doi:10.4052/tigg.1738.1se

Cited by 11 publications

(4 citation statements)

References 145 publications

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“…It is also known that laminins interact with members of the galectin family 42 . Galectins are involved in the regulation of a broad range of host-microbial interactions and may facilitate virus infections 43 . Our siRNA library screening identified the LGALS1 gene, encoding galectin-1, as a putative top activators of H-1PV life cycle.…”

Section: Discussionmentioning

confidence: 99%

Oncolytic H-1 parvovirus binds to sialic acid on laminins for cell attachment and entry

et al. 2021

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H-1 parvovirus (H-1PV) is a promising anticancer therapy. However, in-depth understanding of its life cycle, including the host cell factors needed for infectivity and oncolysis, is lacking. This understanding may guide the rational design of combination strategies, aid development of more effective viruses, and help identify biomarkers of susceptibility to H-1PV treatment. To identify the host cell factors involved, we carry out siRNA library screening using a druggable genome library. We identify one crucial modulator of H-1PV infection: laminin γ1 (LAMC1). Using loss- and gain-of-function studies, competition experiments, and ELISA, we validate LAMC1 and laminin family members as being essential to H-1PV cell attachment and entry. H-1PV binding to laminins is dependent on their sialic acid moieties and is inhibited by heparin. We show that laminins are differentially expressed in various tumour entities, including glioblastoma. We confirm the expression pattern of laminin γ1 in glioblastoma biopsies by immunohistochemistry. We also provide evidence of a direct correlation between LAMC1 expression levels and H-1PV oncolytic activity in 59 cancer cell lines and in 3D organotypic spheroid cultures with different sensitivities to H-1PV infection. These results support the idea that tumours with elevated levels of γ1 containing laminins are more susceptible to H-1PV-based therapies.

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Section: Discussionmentioning

confidence: 99%

Oncolytic H-1 parvovirus binds to sialic acid on laminins for cell attachment and entry

et al. 2021

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“…The immune response against pathogens is one of the important biological functions mediated by galectins. The pathogen recognition and killing abilities of galectin-1, -3, and -8 have been extensively investigated; however, data on Gal-2 is lacking [15]. In this study, we observed that Gal-2 could be involved in host immunity against H. pylori infection.…”

Section: Discussionmentioning

confidence: 62%

“…These LPS can be crosslinked by galectins. Notably, some galectin family proteins such as galectin-3 (Gal-3), -4, and -9 are expressed in the gastrointestinal tract, recognize pathogens, and kill them [15]. Gal-3 is involved in innate immunity by inducing the aggregation of H. pylori and then killing the bacteria in an O-antigen-dependent manner [16,17].…”

Section: Introductionmentioning

confidence: 99%

Galectin-2 Has Bactericidal Effects against Helicobacter pylori in a β-galactoside-Dependent Manner

Sasaki

Saito

Oyama

et al. 2020

IJMS

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Helicobacter pylori is associated with the onset of gastritis, peptic ulcers, and gastric cancer. Galectins are a family of β-galactoside-binding proteins involved in diverse biological phenomena. Galectin-2 (Gal-2), a member of the galectin family, is predominantly expressed in the gastrointestinal tract. Although some galectin family proteins are involved in immunoreaction, the role of Gal-2 against H. pylori infection remains unclear. In this study, the effects of Gal-2 on H. pylori morphology and survival were examined. Gal-2 induced H. pylori aggregation depending on β-galactoside and demonstrated a bactericidal effect. Immunohistochemical staining of the gastric tissue indicated that Gal-2 existed in the gastric mucus, as well as mucosa. These results suggested that Gal-2 plays a role in innate immunity against H. pylori infection in gastric mucus.

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“…Galectins are carbohydrate binding proteins (known commonly as lectins) that bind to a diverse range of β‐galactose‐containing glycoconjugates and are attributed with a variety of biological activities based on their ability to engage carbohydrates (Arthur et al., 2015; Cummings, Fu‐Tong, & Vasta, 2017; Elola et al., 2018; Robinson et al., 2019; Robinson, Arthur, Kamili, & Stowell, 2018; Sundblad, Morosi, Geffner, & Rabinovich, 2017). The synthesis of galectins is known to occur in the cytosol in a reduced environment.…”

Section: Commentarymentioning

confidence: 99%

Generation and Use of Recombinant Galectins

Paul

et al. 2021

Current Protocols

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Galectins are soluble carbohydrate binding proteins that can bind β-galactosecontaining glycoconjugates by means of a conserved carbohydrate recognition domain (CRD). In mammalian systems, galectins have been shown to mediate very important roles in innate and adaptive immunity as well as facilitating host-pathogen relationships. Many of these studies have relied on purified recombinant galectins to uncover key features of galectin biology. A major limitation to this approach is that certain recombinant galectins purified using standard protocols are easily susceptible to loss of glycan-binding activity. As a result, biochemical studies that employ recombinant galectins can be misleading if the overall activity of a galectin remains unknown in a given assay condition. This article examines fundamental considerations when purifying galectins by lactosyl-sepharose and nickel-NTA affinity chromatography using human galectin-4N and-7 as examples, respectively. As other approaches are also commonly applied to galectin purification, we also discuss alternative strategies to galectin purification, using human galectin-1 and-9 as examples.

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Galectin Regulation of Host Microbial Interactions

Cited by 11 publications

References 145 publications

Oncolytic H-1 parvovirus binds to sialic acid on laminins for cell attachment and entry

Oncolytic H-1 parvovirus binds to sialic acid on laminins for cell attachment and entry

Galectin-2 Has Bactericidal Effects against Helicobacter pylori in a β-galactoside-Dependent Manner

Generation and Use of Recombinant Galectins

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