Effect of Galectins on Viral Transmission

Ouellet, Michel; St-Pierre, C.; Tremblay, Michel J.; Sato, Sachiko

doi:10.1007/978-1-4939-1396-1_26

Cited by 6 publications

(3 citation statements)

References 53 publications

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“…Within the complexes, both LNT and LNnT adopt an extended linear conformation very similar to that observed in the P[11] VP8*, suggesting a manner in which the core LNT and LNnT structures bound by VP8* could engage both galectins and P[11] VP8. Other studies have suggested that galectins may be exploited for transmission and replication of viruses, such as influenza viruses, HIV and Nepah viruses 37 38 . Clearly, the possible role of galectins and their ligands in affecting the cell entry and replication of RVs needs further studies.…”

Section: Discussionmentioning

confidence: 99%

Structural basis of glycan specificity in neonate-specific bovine-human reassortant rotavirus

Ramani

Czakó

et al. 2015

Nat Commun

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Strain-dependent variation of glycan recognition during initial cell attachment of viruses is a critical determinant of host specificity, tissue-tropism and zoonosis. Rotaviruses (RVs), which cause life-threatening gastroenteritis in infants and children, display significant genotype-dependent variations in glycan recognition resulting from sequence alterations in the VP8* domain of the spike protein VP4. The structural basis of this genotype-dependent glycan specificity, particularly in human RVs, remains poorly understood. Here, from crystallographic studies, we show how genotypic variations configure a novel binding site in the VP8* of a neonate-specific bovine-human reassortant to uniquely recognize either type I or type II precursor glycans, and to restrict type II glycan binding in the bovine counterpart. Such a distinct glycan-binding site that allows differential recognition of the precursor glycans, which are developmentally regulated in the neonate gut and abundant in bovine and human milk provides a basis for age-restricted tropism and zoonotic transmission of G10P[11] rotaviruses.

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Section: Discussionmentioning

confidence: 99%

Structural basis of glycan specificity in neonate-specific bovine-human reassortant rotavirus

Ramani

Czakó

et al. 2015

Nat Commun

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“…Recombinant Gal-1 (rGal-1) and Gal-3 production Recombinant (r) Gals were purified as previously described with minor modifications (61)(62)(63)(64)(65). Briefly, Terrific Broth containing ampicillin was inoculated with Escherichia coli BL21 (DE3), which carries the expression plasmid of either human Gal-1 or human Gal-3 [kindly provided by Dr. Jun Hirabayashi and Dr. Kenichi Kasai (Teikyo University, Tokyo, Japan)], and incubated overnight at 37°C.…”

Section: Primary Cells and Cell Linesmentioning

confidence: 99%

Galectin‐1 interacts with the human endogenous retroviral envelope protein syncytin‐2 and potentiates trophoblast fusion in humans

et al. 2019

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Syncytin (Syn)‐2 is an important fusogenic protein that contributes to the formation of the placental syncytiotrophoblast. Galectin (Gal)‐1, a soluble lectin, is also involved in trophoblast cell fusion and modulates the interaction of certain retroviral envelopes with their cellular receptor. This study aimed to investigate the association between Syn‐2 and Gal‐1 during human trophoblast cell fusion. This association was evaluated in vitro on primary villous cytotrophoblasts (vCTBs) and cell lines using recombinant Gal‐1 and Syn‐2‐pseudotyped viruses. Using lactose, a Gal antagonist, and Gal‐1‐specific small interfering RNA (siRNA) transfections, we confirmed the implication of Gal‐1 in vCTBs and BeWo cell fusion, although RT‐PCR and ELISA analyses suggested that Gal‐1 alone did not induce syncytialization. Infection assays showed a specific and significant effect of Gal‐1 on the infectivity of Syn‐2‐pseudotyped viruses that depended on the expression of major facilitator superfamily domain‐containing 2A (MFSD2a). Moreover, Gal‐3, another placental Gal, did not modulate the infectivity of Syn‐2‐positive viruses, strengthening the specific association between Gal‐1 and Syn‐2. Interestingly, Gal‐1 significantly reduced the infectivity of Syn‐1‐pseudotyped viruses, suggesting the opposite effects of Gal‐1 on Syn‐1 and ‐2. Finally, coimmunoprecipitation experiments showed a glycan‐dependent interaction between Syn‐2‐bearing virions and Gal‐1. We conclude that Gal‐1 specifically interacts with Syn‐2 and possibly regulates Syn‐2/MFSD2a interaction during syncytialization of trophoblastic cells.—Toudic, C., Vargas, A., Xiao, Y., St‐Pierre, G., Bannert, N., Lafond, J., Rassart, E., Sato, S., Barbeau, B. Galectin‐1 interacts with the human endogenous retroviral envelope protein syncytin‐2 and potentiates trophoblast fusion in humans. FASEB J. 33, 12873–12887 (2019). http://www.fasebj.org

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“…Galectin-1. It was postulated that galectin-1 increases HIV-1 infectivity of T cells and macrophages through a mechanism involving an initial interaction with gp120 (Ouellet et al 2015 ). Galectin-1 is the only galectin studied in the presence of illicit drugs (Reynolds et al 2012a , b ).…”

Section: Discussionmentioning

confidence: 99%

HIV-1 and methamphetamine alter galectins -1, -3, and -9 in human monocyte-derived macrophages

et al. 2022

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Macrophages are key elements of the innate immune system. Their HIV-1 infection is a complex process that involves multiple interacting factors and various steps and is further altered by exposure of infected cells to methamphetamine (Meth), a common drug of abuse in people living with HIV. This is reflected by dynamic changes in the intracellular and secreted proteomes of these cells. Quantification of these changes poses a challenge for experimental design and associated analytics. In this study, we measured the effect of Meth on expression of intracellular and secreted galectins-1, -3, and -9 in HIV-1 infected human monocyte-derived macrophages (hMDM) using SWATH-MS, which was further followed by MRM targeted mass spectrometry validation. Cells were exposed to Meth either prior to or after infection. Our results are the first to perform comprehensive quantifications of galectins in primary hMDM cells during HIV-1 infection and Meth exposure a building foundation for future studies on the molecular mechanisms underlying cellular pathology of hMDM resulting from viral infection and a drug of abuse—Meth.

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Effect of Galectins on Viral Transmission

Cited by 6 publications

References 53 publications

Structural basis of glycan specificity in neonate-specific bovine-human reassortant rotavirus

Structural basis of glycan specificity in neonate-specific bovine-human reassortant rotavirus

Galectin‐1 interacts with the human endogenous retroviral envelope protein syncytin‐2 and potentiates trophoblast fusion in humans

HIV-1 and methamphetamine alter galectins -1, -3, and -9 in human monocyte-derived macrophages

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