Molecular analysis of human class II transplantation antigens and their genes

Larhammar, Dan; Andersson, Gerhard; Andersson, Matilda; Bill, P.; Böhme, Jan; Claesson, Lena; Denaro, Maurizio; Emmoth, Eva; Gustafsson, Kenth; Hammarling, U.; Heldin, E; Hyldig‐Nielsen, J. J.; Lind, Peter; Schenning, L.; Servenius, B; Widmark, E; Rask, Lars; Peterson, Per A.

doi:10.1016/0198-8859(83)90087-3

Cited by 40 publications

(16 citation statements)

References 9 publications

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“…Such adjacent prolines frequently occur in flexible peptide segments that connect the extracellular portion of integral membrane proteins with the transmembrane domain (see e.g. Kimball and Coligan, 1983;Larhammar et al, 1983). Mutations introduced at this point may consequently leave the conformation of the lumenal domain intact.…”

Section: Discussionmentioning

confidence: 99%

Structural and functional dissection of an MHC class I antigen-binding adenovirus glycoprotein.

Pääbo¹,

Weber²,

Nilsson³

et al. 1986

The EMBO Journal

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The early transmembrane glycoprotein E19 of adenovirus-2 binds to class I antigens of the major histocompatibility complex (MHC). The association is initiated in the endoplasmic reticulum of infected cells and abrogates the intracellular transport of the class I molecules. To examine which parts of the E19 molecule are responsible for the association with the class I antigens and which parts confine the protein to the endoplasmic reticulum we have constructed a series of mutated E19 genes, which have been expressed in an improved mammalian expression vector. By various manipulations the membrane anchoring and the cytoplasmic domains were removed from the protein. The biosynthesis of the mutant protein was exanined. All mutant proteins were secreted from the cells suggesting that the transmembrane and/or cytoplasmic portions of the E19 molecule are responsible for its confinement to the endoplasmic reticulum. The ability to associate with class I antigens was retained by the lumenal domain of the E19 protein.

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Section: Discussionmentioning

confidence: 99%

Structural and functional dissection of an MHC class I antigen-binding adenovirus glycoprotein.

Pääbo¹,

Weber²,

Nilsson³

et al. 1986

The EMBO Journal

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“…IgG VL: human V, Newm (LIHUNM; Chen & Poljak 1974); IgG VK: human V. Roy (K1HURY; Appella 1971); H-2E''. mouse a chain (HLMSED; Larhammar et al 1983); Pig R: poly Ig receptor, rabbit (QRRBG; Mostov et al 1984); OX-2: rat ; Thy-1: rat (TDRT; Campbell et al 1981); Po: (Lemke & Axel 1985); IgG CL: human Coj (L2HU; Titani et at. 1970).…”

Section: B236jmag Defines a Subgroup Of The Ig Familymentioning

confidence: 99%

Neural Protein 1B236/Myelin‐Associated Glycoprotein (MAG) Defines a Subgroup of the Immunoglobulin Superfamily

Lai

Watson

Bloom

et al. 1987

Immunological Reviews

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We have reviewed the structure and properties of the neural protein 1B236/MAG. This molecule consists largely of five Ig-like domains separated from its carboxyl terminal tail by a single membrane-spanning region. Two forms of the protein differ in the length and sequence of the carboxyl terminus: these are encoded by alternatively spliced mRNAs that are differentially expressed during postnatal neural development. The Ig-like domains of 1B236/MAG are unusual in having structural similarities to Ig V domains but with short Cys-Cys distances characteristic of C domains. Several other Ig-like molecules exhibit this structural feature, including the cell adhesion molecule N-CAM, which is most closely related in sequence to 1B236/MAG. We have proposed 1B236/MAG as the prototype for this subgroup of the Ig family and offer a model for this type of Ig domain structure. 1B236/MAG probably acts as a cell adhesion molecule to mediate interactions between cells in a fashion similar to that proposed for N-CAM. In particular, 1B236/MAG may be involved in interactions between myelinating oligodendrocytes or Schwann cells and axons or between adjacent layers of myelin membrane during the process of myelin compaction. It is most likely that the homophilic or heterophilic interactions of 1B236/MAG occur through binding to the Ig-like domains. The structure of 1B236/MAG is therefore quite consistent with its proposed function and may serve as the model for this class of cell-cell interaction molecules. One would predict, for example, that the neuron-glia cell adhesion molecule Ng-CAM, also known as NILE or L1 (Bock et al. 1985, Friedlander et al. 1985), which mediates interactions between neurons and glial cells, would have a very similar structure to those of N-CAM and 1B236/MAG. In addition, the carboxyl terminal tails of the 1B236/MAG proteins may also be involved in interactions with cytoskeletal components, during membrane vesicle transport through the glial cytoplasm during myelination or through neuronal axoplasm or cytoplasm. The availability of full-length cDNA clones of 1B236/MAG mRNAs with the ability to express these products in vitro will enable the structure and interactions of 1B236/MAG to be tested in detail.

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“…Since gene conversion is believed to be important for the development , r , of variability of class II genes (Larhammar et al 1983, Mengele-Gaw et al 1984, Weiss et al 1983, one possible explanation for the dilemma is that the DRw8 0 chain also carries the DRw52 determinant, but that cells with the 3,5 or w6 specificities have the same or a cross-reacting determinant encoded by a distinct DR fi gene. Since gene conversion is believed to be important for the development , r , of variability of class II genes (Larhammar et al 1983, Mengele-Gaw et al 1984, Weiss et al 1983, one possible explanation for the dilemma is that the DRw8 0 chain also carries the DRw52 determinant, but that cells with the 3,5 or w6 specificities have the same or a cross-reacting determinant encoded by a distinct DR fi gene.…”

Section: I Ti'mentioning

confidence: 99%

Implication of Structural Class II Gene Polymorphism for the Concept of Serologic Specificities

Möller

Carlsson

Wallin

1985

Immunological Reviews

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We have used DNA-DNA hybridization methods to study the relationship of genetic polymorphisms to the established HLA-D region determinants as detected with serological reagents. The supertypic determinants DRw52 and 53 are closely associated with a particular RFLP detected with the DR beta probe, but are seemingly encoded by a distinct beta gene compared to the "conventional" DR antigens. DQw1 is closely associated with a DQ alpha chain polymorphism, whereas the DQw2 and 3 specificities have correlations to RFLP using the DQ beta probe. Additional DQ polymorphism, in linkage disequilibrium with DR but yet without a serological counterpart is also described. Considering the finding that there exist a varying number of DR beta genes in different DR haplotypes (Böhme et al. 1985), from 1 in DRw8 to 3 (or 4) in DR4- and DR7-positive cells, we have made a tentative re-evaluation of the genetic basis for the conventional DR specificities. The combination of cell surface antigens encoded by DR and DQ loci are believed to form the basis for MLC stimulating determinants. We have speculated that a combination of determinants encoded by distinct DR beta genes and in certain instances additional DQ polymorphism is responsible for the DR types. Thus, only a limited variability is observed after DNA-DNA hybridization using DR beta probes. Only DR1-, 2- and 4-positive cells have distinct bands not detected in any other haplotypes, whereas DR3, 5, w6, and w8 can be characterized by a combination of bands, which is the result of hybridization with several DR beta genes. Furthermore, we have suggested that the difference between the DR3 and DRw6 specificities is due to variability with regard to 1 DQ beta gene, and have also made the assumption that DRw6 cells may express a lower concentration of DR locus encoded products compared to DR3-positive cells (Haziot et al. 1985). In addition, we have discussed the genetic basis for so-called DR blanks, implying that an unorthodox combination of DR and DQ determinants forms the basis for difficulties in assigning DR types to such cells in some cases and that "blanks" can be associated with low expression at the cell surface of well-known DR determinants. The use of cDNA and genomic probes for distinct class II genes to elucidate the mechanisms of HLA and disease association has been documented and discussed.

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Molecular analysis of human class II transplantation antigens and their genes

Cited by 40 publications

References 9 publications

Structural and functional dissection of an MHC class I antigen-binding adenovirus glycoprotein.

Structural and functional dissection of an MHC class I antigen-binding adenovirus glycoprotein.

Neural Protein 1B236/Myelin‐Associated Glycoprotein (MAG) Defines a Subgroup of the Immunoglobulin Superfamily

Implication of Structural Class II Gene Polymorphism for the Concept of Serologic Specificities

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