CLEC4M
CLEC4M (C-type lectin domain family 4 member M) is a C-type lectin receptor that functions in cell adhesion and pathogen recognition. It is also known as L-SIGN, DC-SIGNR, CD299 and CD209L, and is closely related to DC-SIGN. Browse Assay Genie's current range of CLEC4M research reagents below, or read on for the biology behind the target.
CLEC4M is a C-type lectin that functions in cell adhesion and pathogen recognition. The receptor recognises a wide range of evolutionarily divergent pathogens with a large impact on public health, including tuberculosis mycobacteria, and viruses such as Ebola, hepatitis C, HIV-1, influenza A, West Nile virus and SARS coronavirus. UniProt also notes that recognition of M. bovis by dendritic cells may occur partially via this molecule.
The CLEC4M protein is organised into four distinct domains: a C-terminal carbohydrate recognition domain, a flexible tandem-repeat neck domain of variable length, a transmembrane region and an N-terminal cytoplasmic domain involved in internalisation. UniProt records its subcellular location as the cell membrane and as a secreted form. The CLEC4M gene shows high expression in endothelial cells of the liver, lymph node and placenta.
CLEC4M is closely related in sequence and function to its neighbouring gene CD209, also known as DC-SIGN, although the two genes differ in viral recognition and expression patterns. This relationship explains the alternative names L-SIGN and DC-SIGNR (DC-SIGN related), as well as DC-SIGN2. HGNC classes the gene among the CD molecules, with the antigen name CD299. Polymorphisms in the tandem-repeat neck domain are associated with resistance to SARS infection.
CLEC4M recognises viruses including Ebola, hepatitis C, HIV-1, influenza A, West Nile virus and SARS coronavirus, making it a focus for host-virus interaction studies.
The receptor recognises tuberculosis mycobacteria, and dendritic cell recognition of M. bovis may occur partly through it.
High expression in endothelial cells of the liver, lymph node and placenta makes CLEC4M relevant to tissue-specific lectin function.
Polymorphisms in the tandem-repeat neck domain are associated with resistance to SARS infection, supporting genetic association research.
CLEC4M is a C-type lectin that functions in cell adhesion and pathogen recognition. Its C-terminal carbohydrate recognition domain engages a broad range of pathogens, including tuberculosis mycobacteria and several viruses, while its N-terminal cytoplasmic domain is involved in internalisation.
CLEC4M is also called L-SIGN, DC-SIGNR, DC-SIGN2, LSIGN, DCSIGNR, CD209L, CD209L1, HP10347 and CD299. The names reflect its close relationship to DC-SIGN (CD209), the neighbouring gene it resembles in sequence and function. Check the datasheet of any product for its validated reactivity.
The two genes are neighbours and closely related in sequence and function, but they differ in viral recognition and expression patterns. CLEC4M shows high expression in endothelial cells of the liver, lymph node and placenta, and its neck-domain polymorphisms are linked to SARS resistance.
Other C-type lectin domain family members involved in pathogen recognition and immune signalling.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9H2X3; product specifications from Assay Genie datasheets.