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Last update 08 May 2025

CLEC4G

Last update 08 May 2025

Basic Info

Synonyms

C-type lectin domain family 4 member G, CLEC4G, Liver and lymph node sinusoidal endothelial cell C-type lectin

+ [2]

Introduction

Binds mannose, N-acetylglucosamine (GlcNAc) and fucose, but not galactose, in a Ca(2+)-dependent manner, in vitro. (Microbial infection) Acts as a receptor for Ebolavirus. (Microbial infection) Acts as a receptor for SARS-CoV. (Microbial infection) Acts as a receptor for Lassa virus and Lymphocytic choriomeningitis virus glycoprotein (PubMed:22156524, PubMed:22673088). (Microbial infection) Acts as a receptor for Japanese encephalitis virus.

Drugs associated with CLEC4G

WO2022167571

Patent Mining

Target

CLEC4G

Mechanism-

Active Org.

Imba Institut für Molekulare Biotechnologie GmbH

Originator Org.

Imba Institut für Molekulare Biotechnologie GmbH

Active Indication

Infectious Diseases

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with CLEC4G

100 Translational Medicine associated with CLEC4G

0 Patents (Medical) associated with CLEC4G

Literatures (Medical) associated with CLEC4G

01 Sep 2024·Phytomedicine

Reversible ON- and OFF-switch receptors Clec4G and Rab1A reveal the hormetic effects of a pectin polysaccharide in Aralia elata (Miq.) Seem

Article

Author: Zhu, Xin-Hua ; Zhang, Yi ; Kuang, Hai-Xue ; Shen, Yu ; Wang, Wen-Fei ; Xia, Yong-Gang ; Lü, Jia-Lu ; Liang, Jun ; Jing, Xiao-Jie ; Jiang, Si-Liang

BACKGROUNDNumerous studies indicate that natural polysaccharides have immune-enhancing effects as a host defense potentiator. Few reports are available on hormetic effects of natural polysaccharides, and the underlying mechanisms remain unclear.PURPOSEAELP-B6 (arabinose- and galactose-rich pectin polysaccharide) from Aralia elata (Miq.) Seem was taken as a case study to clarify the potential mechanism of hormetic effects of natural polysaccharides.METHODSThe pharmacodynamic effect of AELP-B6 was verified by constructing the CTX-immunosuppressive mouse model. The hormetic effects were explored by TMT-labeled proteomics, energy metabolism analysis, flow cytometry and western blot. The core-affinity target of AELP-B6 was determined by pull down, nanoLC-nanoESI⁺-MS, CETSA, immunoblot and SPR assay. The RAW264.7^Clec4G-RFP and RAW264.7^Rab1A-RFP cell lines were simultaneously constructed to determine the affinity difference between AELP-B6 and targets by confocal laser scanning live-cell imaging. Antibody blocking assays were further used to verify the mechanism of hormetic effects.RESULTSAELP-B6 at low and medium doses may maintain the structural integrity of thymus and spleen, increase the concentrations of TNF-α, IFN-γ, IL-3 and IL-8, and alleviate CTX-induced reduction of immune cell viability in vivo. Proteomics and energy metabolism analysis revealed that AELP-B6 regulate HIF-1α-mediated metabolic programming, causing Warburg effects in macrophages. AELP-B6 at low and medium doses promoted the release of intracellular immune factors, and driving M1-like polarization of macrophages. As a contrast, AELP-B6 at high dose enhanced the expression levels of apoptosis related proteins, indicating activation of the intrinsic apoptotic cascade. Two highly expressed transmembrane proteins in macrophages, Clec4G and Rab1A, were identified as the primary binding targets of AELP-B6 which co-localized with the cell membrane and directly impacted with immune cell activation and apoptosis. AELP-B6 exhibits affinity differences with Clec4G and Rab1A, which is the key to the hormetic effects.CONCLUSIONWe observed hormesis of natural polysaccharide (AELP-B6) for the first time, and AELP-B6 mediates the hormetic effects through two dose-related targets. Low dose of AELP-B6 targets Clec4G, thereby driving the M1-like polarization via regulating NF-κB signaling pathway and HIF-1α-mediated metabolic programming, whereas high dose of AELP-B6 targets Rab1A, leading to mitochondria-dependent apoptosis.

01 Sep 2024·Medicine & Science in Sports & Exercise

Urinary Proteomic Biomarkers of Trabecular Bone Volume Change during Army Basic Combat Training

Article

Author: Matheny, Ronald W. ; Taylor, Kathryn M ; Matheny, Ronald W ; Foulis, Stephen A ; Nindl, Bradley C ; Sterczala, Adam J ; Hughes, Julie M. ; Beckner, Meaghan E. ; Hougland, Juliana R ; Cantrell, Pamela S ; Sterczala, Adam J. ; Sun, Mai ; Beckner, Meaghan E ; Connaboy, Chris ; Canino, Maria C ; Guerriere, Katelyn I. ; CONNABOY, CHRIS ; Flanagan, Shawn D ; Zeng, Xuemei ; Nindl, Bradley C. ; Hougland, Juliana R. ; Taylor, Kathryn M. ; Flanagan, Shawn D. ; Canino, Maria C. ; Walker, Leila A ; Cantrell, Pamela S. ; Guerriere, Katelyn I ; Walker, Leila A. ; HOUGLAND, JULIANA R. ; Foulis, Stephen A. ; FLANAGAN, SHAWN D. ; Jones-Laughner, Jackie ; Hughes, Julie M

ABSTRACTChanges in bone microarchitecture resulting from chronic physical stress such as that experienced during U.S. Army Basic Combat Training (BCT) underscore its adaptive potential. There is a need for noninvasive biomarkers of adaptive bone formation that can be obtained at scale in real-world settings. Differential mass spectrometry (dMS), a label-free quantitative proteomics technique, may provide useful information about bone adaptation based on the proteomic features of urine.PurposeThe purpose of this study is to optimize a dMS-based urinary proteomic technique and evaluate the relationship between urinary proteome content and adaptive changes in bone microarchitecture during BCT.MethodsUrinary proteomes were analyzed with an optimized dMS technique in two groups of 13 recruits (N = 26) at the beginning (Pre) and end (Post) of BCT. Matched by age (21 ± 4 yr), sex (16 W), and baseline tibial trabecular bone volume fractions (Tb.BV/TV), these groups were distinguished by the most substantial (High) and minimal (Low) improvements in Tb.BV/TV. Differential protein expression was analyzed with mixed permutation ANOVA and false discovery proportion-based adjustment for multiple comparisons.ResultsTibial Tb.BV/TV increased from pre- to post-BCT in High (3.30 ± 1.64%, P < 0.0001) but not Low (−0.35 ± 1.25%, P = 0.4707). The optimized dMS technique identified 10,431 peptides from 1368 protein groups that represented 165 integrative biological processes. Seventy-four urinary proteins changed from pre- to post-BCT (P = 0.0019), and neutrophil-mediated immunity was the most prominent ontology. Two proteins (immunoglobulin heavy constant gamma 4 and C-type lectin domain family 4 member G) differed from pre- to post-BCT in High and Low (P = 0.0006).ConclusionsThe dMS technique can identify more than 1000 urinary proteins. At least 74 proteins are responsive to BCT, and other principally immune system–related proteins show differential expression patterns that coincide with adaptive bone formation.

17 Jul 2024·Nano Letters

Antibody-Decorated Nanoplatform to Reprogram Macrophage and Block Immune Checkpoint LSECtin for Effective Cancer Immunotherapy

Article

Author: Li, Rong ; Liu, Xiangya ; Xu, Rui ; Xu, Xiaoding ; Huang, Linzhuo ; Wu, Guo ; Zhang, Yuxuan

Repolarizing tumor-associated macrophages (TAMs) into tumor-inhibiting M1 macrophages has been considered a promising strategy for enhanced cancer immunotherapy. However, several immunosuppressive ligands (e.g., LSECtin) can still be highly expressed on M1 macrophages, inducing unsatisfactory therapeutic outcomes. We herein developed an antibody-decorated nanoplatform composed of PEGylated iron oxide nanoparticles (IONPs) and LSECtin antibody conjugated onto the surface of IONPs via the hydrazone bond for enhanced cancer immunotherapy. After intravenous administration, the tumor microenvironment (TME) pH could trigger the hydrazone bond breakage and induce the disassociation of the nanoplatform into free LSECtin antibodies and IONPs. Consequently, the IONPs could repolarize TAMs into M1 macrophages to remodel immunosuppressive TME and provide an additional anticancer effect via secreting tumoricidal factors (e.g., interlukin-12). Meanwhile, the LSECtin antibody could further block the activity of LSECtin expressed on M1 macrophages and relieve its immunosuppressive effect on CD8⁺ T cells, ultimately leading to significant inhibition of tumor growth.

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CLEC4G

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