Novel Role for Macrophage Galactose-Type Lectin-1 to Regulate Innate Immunity against<i>Mycobacterium tuberculosis</i>

Naqvi, Kubra F.; Huante, Matthew B.; Saito, Taís B.; Endsley, Mark; Gelman, Benjamin B.; Endsley, Janice J.

doi:10.4049/jimmunol.2001276

Cited by 11 publications

(11 citation statements)

References 69 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Here, the CRDs orientation makes both QPD and OS binding sites accessible for binding glycans assembled on a surface. The presence of these six binding sites highly increases the multivalency of the interaction and probably explains the very broad Pathogen Associated Molecular Patterns that MGL is capable to recognize, from both gram positive and negative bacteria, as well as M. tuberculosis (Mnich et al, 2019; Naqvi et al, 2021; van Sorge et al, 2009; Vliet et al, 2009). We can hypothesize that the mode of recognition by MGL of Teichoic Acids, that are polysaccharides assembled similarly as LPS at the surface of S. aureus (Mnich et al, 2019), resembles that of LPS.…”

Section: Discussionmentioning

confidence: 99%

“…So far MGL has been described to recognize S. aureus, C. jejuni, K. pneumonia, N. gonorrhea, B. pertussis and M. tuberculosis (Mnich et al, 2019;Naqvi et al, 2021;van Sorge et al, 2009;Vliet et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

“…Its main role appears to be an immunomodulatory activity, reducing excessive inflammatory responses. So far MGL has been described to recognize S. aureus, C. jejuni, K. pneumonia, N. gonorrhea, B. pertussis and M. tuberculosis (Mnich et al, 2019; Naqvi et al, 2021; van Sorge et al, 2009; Vliet et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The unique three-dimensional arrangement of Macrophage Galactose Lectin enablesE. coliLipoPolySaccharides recognition through two distinct interfaces

Abbas

Maalej

Nieto-Fabregat

et al. 2023

Preprint

View full text Add to dashboard Cite

LipoPolySaccharides are a hallmark of Gram-negative bacteria and their presence at the cell surface is key for bacterial integrity. As surface exposed components, they are recognized by immunity C-type lectin receptors present on Antigen Presenting Cells. Human Macrophage Galactose Lectin bindsE. colisurface that presents a specific glycan motif. Nevertheless, this high affinity interaction occurs regardless of the integrity of its canonical calcium-dependent glycan binding site. Nuclear Magnetic Resonance of MGL carbohydrate recognition domain and complete extracellular domain revealed a new glycan binding site opposite to the canonical site. A model of trimeric Macrophage Galactose Lectin was determined based on a combination of Small Angle X-ray scattering and Alphafold. A disulphide bond positions the Carbohydrate Recognition Domain perpendicular to the coiled-coil domain. This unique configuration for a C-type lectin orients the six glycan sites of MGL in an ideal position to bind LipoPolySaccharides at the bacterial surface with high avidity.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The unique three-dimensional arrangement of Macrophage Galactose Lectin enablesE. coliLipoPolySaccharides recognition through two distinct interfaces

Abbas

Maalej

Nieto-Fabregat

et al. 2023

Preprint

View full text Add to dashboard Cite

show abstract

“…[202] Notably, MGL is involved in the detection of various pathogens, including Staphylococcus aureus, Campylobacter jejuni, Klebsiella pneumoniae, Neisseria gonorrhoeae, Bordetella pertussis, and Mycobacterium tuberculosis. [203][204][205][206] MGL possesses a QPD motif for canonical Ca 2 + -dependent recognition of galactose-related glycans. While MGL typically features two Ca 2 + sites, X-ray crystallographic structures (e. g., PDB ID: 6PY1 and 6 W12) revealed additional Ca 2 + ions, postulated to enhance protein stability.…”

Section: Example 3: Mglmentioning

confidence: 99%

Secondary Sites of the C‐type Lectin‐Like Fold

Lefèbre,

Falk,

Ning

et al. 2024

Chemistry A European J

View full text Add to dashboard Cite

C‐type lectins are a large superfamily of proteins involved in a multitude of biological processes. In particular, their involvement in immunity and homeostasis has rendered them attractive targets for diverse therapeutic interventions. They share a characteristic C‐type lectin‐like domain whose adaptability enables them to bind a broad spectrum of ligands beyond the originally defined canonical Ca2+‐dependent carbohydrate binding. Together with variable domain architecture and high‐level conformational plasticity, this enables C‐type lectins to meet diverse functional demands. Secondary sites provide another layer of regulation and are often intricately linked to functional diversity. Located remote from the canonical primary binding site, secondary sites can accommodate ligands with other physicochemical properties and alter protein dynamics, thus enhancing selectivity and enabling fine‐tuning of the biological response. In this review, we outline the structural determinants allowing C‐type lectins to perform a large variety of tasks and to accommodate the ligands associated with it. Using the six well‐characterized Ca2+‐dependent and Ca2+‐independent C‐type lectin receptors DC‐SIGN, langerin, MGL, dectin‐1, CLEC‐2 and NKG2D as examples, we focus on the characteristics of non‐canonical interactions and secondary sites and their potential use in drug discovery endeavors.

show abstract

“…MGL rarely recognizes pathogens and modulates the response to them, due to the rarity of the recognized epitope in pathogen glycans, with few exceptions including Mycobacterium tuberculosis [ 101 ].…”

Section: Lectin–protein Receptors For Sugar Structures and Lectin–car...mentioning

confidence: 99%

Seminal Plasma Glycoproteins as Potential Ligands of Lectins Engaged in Immunity Regulation

Olejnik

Ferens-Sieczkowska

2022

IJERPH

View full text Add to dashboard Cite

Environmental pollution, chronic stress, and unhealthy lifestyle are factors that negatively affect reproductive potential. Currently, 15–20% of couples in industrialized countries face the problem of infertility. This growing health and social problem prompts researchers to explore the regulatory mechanisms that may be important for successful fertilization. In recent years, more attention has been paid to male infertility factors, including the impact of seminal plasma components on regulation of the female immune response to allogenic sperm, embryo and fetal antigens. Directing this response to the tolerogenic pathway is crucial to achieve a healthy pregnancy. According to the fetoembryonic defense hypothesis, the regulatory mechanism may be associated with the interaction of lectins and immunomodulatory glycoepitopes. Such interactions may involve lectins of dendritic cells and macrophages, recruited to the cervical region immediately after intercourse. Carbohydrate binding receptors include C type lectins, such as DC-SIGN and MGL, as well as galectins and siglecs among others. In this article we discuss the expression of the possible lectin ligands, highly fucosylated and high mannose structures, which may be recognized by DC-SIGN, glycans of varying degrees of sialylation, which may differ in their interaction with siglecs, as well as T and Tn antigens in O-glycans.

show abstract

Novel Role for Macrophage Galactose-Type Lectin-1 to Regulate Innate Immunity againstMycobacterium tuberculosis

Abstract: The RNA-sequencing data presented in this article have been submitted to the National Center for Biotechnology Information's Gene Expression Omnibus under accession number GSE168486 (https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE168486).

Cited by 11 publications

References 69 publications

The unique three-dimensional arrangement of Macrophage Galactose Lectin enablesE. coliLipoPolySaccharides recognition through two distinct interfaces

The unique three-dimensional arrangement of Macrophage Galactose Lectin enablesE. coliLipoPolySaccharides recognition through two distinct interfaces

Secondary Sites of the C‐type Lectin‐Like Fold

Seminal Plasma Glycoproteins as Potential Ligands of Lectins Engaged in Immunity Regulation

Contact Info

Product

Resources

About