D. Phamdinh et al., MYELIN OLIGODENDROCYTE GLYCOPROTEIN IS A MEMBER OF A SUBSET OF THE IMMUNOGLOBULIN SUPERFAMILY ENCODED WITHIN THE MAJOR HISTOCOMPATIBILITY COMPLEX, Proceedings of the National Academy of Sciences of the United Statesof America, 90(17), 1993, pp. 7990-7994
Myelin/oligodendrocyte glycoprotein (MOG) is found on the surface of m
yelinating oligodendrocytes and external lamellae of myelin sheaths in
the central nervous system, and it is a target antigen in experimenta
l autoimmune encephalomyelitis and multiple sclerosis. We have isolate
d bovine, mouse, and rat MOG cDNA clones and shown that the developmen
tal pattern of MOG expression in the rat central nervous system coinci
des with the late stages of myelination. The amino-terminal, extracell
ular domain of MOG has characteristics of an immunoglobulin variable d
omain and is 46% and 41 % identical with the amino terminus of bovine
butyrophilin (expressed in the lactating mammary gland) and B-G antige
ns of the chicken major histocompatibility complex (MHC), respectively
; these proteins thus form a subset of the immunoglobulin superfamily.
The homology between MOG and B-G extends beyond their structure and g
enetic mapping to their ability to induce strong antibody responses an
d has implications for the role of MOG in pathological, autoimmune con
ditions. We colocalized the MOG and BT genes to the human MHC on chrom
osome 6p21.3-p22. The mouse MOG gene was mapped to the homologous band
C of chromosome 17, within the M region of the mouse MHC.