Request ID: cfg_rRequest_278
Status
:
Approved
Project Description
:
The investigator wishes to determine the carbohydrate-binding specificity of murine Dectin-2.
CFG Member
:
C-Type Lectin
Requester First Name
:
Siamon
Requester Last Name
:
Gordon
Head of Lab First Name
:
Information not entered/not applicable.
Head of Lab Last Name
:
Information not entered/not applicable.
Assigned First Name
:
Siamon
Assigned Last Name
:
Gordon
Requester Email
:
philip.taylor@path.ox.ac.uk
Requester Interest
:
This laboratory studies lectin-like receptors expressed by macrophages and their roles in host defence against infection by bacteria, fungi and viruses, as well as in interactions with endogenous ligands in murine and human tissue.
Request Date [yyyy-mm-dd]
:
2005-05-26
Institution
:
Oxford University
Shipping Address
:
Sir William Dunn School of Pathology, Oxford University, South Parks Road, Oxford, OX1 3RE, United Kingdom. Tel: +44 (0) 1865 275522
Comments
:
Information not entered/not applicable.
CFG Core
:
H
Resource Type
:
Glycoarray
Amount Requested
:
Information not entered/not applicable.
Date that your RNA/GBP samples will be sent to the core [yyyy-mm-dd]
:
2005-06-13
Experiment to be conducted
:
Dectin-2, whilst largely considered dendritic cell restricted, I have made monoclonal antibodies against Dectin-2 and shown it is most abundantly expressed by macrophages in the naÔve mouse. I have also found a Ca2+ dependent mannose/fucose-like specificity for the carbohydrate recognition domain of Dectin-2 by expressing its extracellular domain as a human Fc chimeric protein. I ëcrudelyí estimate the affinity to mannose to be approximately 15-fold lower than the macrophage mannose receptor when assayed in the same way.
Significance: The chimeric protein derived from mouse Dectin-2 exhibits Ca2+ dependent binding to a variety of microbes, including mycobacteria and fungi. This binding is inhibited (but in high concentration) by mannose and yeast mannans suggesting that the natural ligand composition on the microbes is distinct/more complex. Thus Dectin-2 may play a role in the recognition of microbial carbohydrates by macrophages. Dectin-2 has also been suggested to bind to T-cells and its ligand is unknown. It is possible that interaction with its endogenous ligand may also involve a carbohydrate interaction. Specific Aim: To identify natural and synthetic ligands for Dectin-2, which will allow a better understanding of what types of carbohydrates (and hence pathogens/endogenous ligands) Dectin-2 may interact with and will provide tools to probe the role of Dectin-2 in the immune system.
Within Scope of Consortium
:
Y
If yes, indicate the person responsible for inputing data into core B
:
Rick Alvarez
GBP being Addressed
:
Dectin-2
Specifc aims being addressed
:
Define the specificity and affinity for carbohydrate ligands.