Abstract
Research to connect lipids with immunology is growing, but details about the specific roles of lipid transfer proteins (LTPs) in antigen presentation remain unclear. A single class of major histocompatibility class-like molecules, called CD1 molecules, can present lipids and glycolipids to the immune system. These molecules all have a common hydrophobic antigen-binding groove. The loading of this groove with various lipids throughout the life of a CD1 molecule defines the immune recognition of lipids by T cells. At each location of residence, CD1 molecules are exposed to particular physicochemical conditions, particular collections of lipids, and unique combinations of LTPs that will define which lipids bind to CD1 and which do not. The lipid transfer machinery that is used by CD1 molecules is entirely hijacked from the normal synthetic and catalytic pathways of lipids. The precise determinants that regulate the presentation of certain lipids over others with respect to chemistry, solubility, and abundance are still poorly defined and require investigation to allow the use of lipids as regular antigenic targets of immunotherapy and vaccine.
Highlights
Research to connect lipids with immunology is growing, but details about the specific roles of lipid transfer proteins (LTPs) in antigen presentation remain unclear
Studies looking at the cell biology and antigen presentation of lipids onto CD1 molecules are scarce, even if some of the most pressing issues have been at least partially answered: assembly of CD1 molecules in the endoplasmic reticulum (ER) [12]; trafficking to the cell surface [13]; cellular location of loading [13]; uptake of exogenous lipids [14]; and identification of endogenous ligands [15]
The ER is where CD1 molecules are assembled before export through the Golgi, following a succession of interactions with chaperones that is very similar to what has been described for major histocompatibility complex (MHC) class I molecules [12]
Summary
The ER is a very active, synthetic, and catalytic compartment for lipids and the main reserve of membranes in a cell. The ER is where CD1 molecules are assembled before export through the Golgi, following a succession of interactions with chaperones that is very similar to what has been described for MHC class I molecules [12]. One can assume, based on what classical MHC molecules do, that the CD1 groove is never empty and would unfold in the absence of a ligand Because it is so hydrophobic, the CD1 groove could collapse on itself in the absence of a bound lipid and prevent denaturation of the whole molecule [36]; there is currently no experimental data to support this observation
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