Unusual association of beta 2-microglobulin with certain class I heavy chains of the murine major histocompatibility complex.

Bushkin, Yuri; Tung, Jwu-Sheng; Pinter, Abraham; Michaelson, James; Boyse, Edward A.

doi:10.1073/pnas.83.2.432

Cited by 12 publications

(5 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Interestingly, in the noninducer strains of mice this residue is replaced by a Cys. This Cys residue has been suggested as being involved in a disulfide bond between the heavy chain of H-2 class I molecules and &M, which results in a novel 70-kDa protein complex [31]. The complex is reduced to its constituent polypeptide chains in the presence of 2-mercaptoethanol.…”

Section: Discussionmentioning

confidence: 98%

“…Conventional wisdom suggests it is needed for assembly and expression of class I MHC antigens [l]. One class I MHC antigens are expressed on the cell surface, MHC-associated P2M can exchange freely with soluble P2M from the same or different species [2,31. The association of human P2M with HLA-A, B or C molecules results in the generation of a conformational determinant recognized by the mouse monoclonal antibody (mAb) W6l32 [4].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Expression of the W6/32 HLA epitope by cells of rat, mouse, human and other species: critical dependence on the interaction of specific MHC heavy chains with human or bovine β₂‐microglobulin

Jefferies

MacPherson

1987

Eur J Immunol

View full text Add to dashboard Cite

The HLA class I epitope W6/32 is conformationally dependent on both heavy chain and beta 2-microglobulin (beta 2M). Previously, the W6/32 epitope has been detected in humans and other primates as well as from bovine sources. Two controversial reports suggest the W6/32 epitope is constitutively expressed by either normal or transformed murine cells expressing the Db allele. Here we show that the appearance of the W6/32 epitope in murine cells results from the association of either the Db or Kd gene products with either bovine or human beta 2M. We use congenic mouse strains and hybrid H-2 class I genes between Db and Kb to map the W6/32 epitope to particular amino acid residues in the alpha 2 domain. Subsequently, we show that beta 2M exchange is not confined to murine or human cells in vitro but can be detected after beta 2M injection into a mouse. The data presented suggests that beta 2M exchange takes place at the cell surface under physiological conditions and indicates that MHC class I heavy chains are in an equilibrium between the bound and unbound form of beta 2M.

show abstract

Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Expression of the W6/32 HLA epitope by cells of rat, mouse, human and other species: critical dependence on the interaction of specific MHC heavy chains with human or bovine β₂‐microglobulin

Jefferies

MacPherson

1987

Eur J Immunol

View full text Add to dashboard Cite

show abstract

“…Unpaired cysteines can lead to unwanted cross‐linking between the HC and other proteins. Cross‐linking between HC and β 2 m has been observed for several mouse class I alleles (50). And in humans, the cross‐linking between HLA‐B27 HCs to form homodimers has been documented (51).…”

Section: Discussionmentioning

confidence: 99%

ER60/ERp57 forms disulfide‐bonded intermediates with MHC class I heavy chain

Lindquist¹,

Hämmerling

Trowsdale³

2001

FASEB j.

View full text Add to dashboard Cite

We demonstrated previously that ER60/ERp57 is recruited into early folding intermediates in the MHC class I assembly pathway (1). ER60 binding preceded the binding of β‐2‐microglobulin and was dependent on the presence of properly trimmed oligosaccharide moieties on the class I heavy chain (HC). Hence, this interaction could not be temporally differentiated from that of calnexin. Here, we show that calnexin is required for the recruitment of ER60 into early folding complexes with the HC and that in the absence of calnexin, ER60 is replaced by another member of the thiol‐reductase family, ERp72. We demonstrate that once recruited, ER60 associates covalently with HC via a disulfide bond. The ER60/HC complexes were also found in late assembly complexes, noncovalently bound to the transporter associated with antigen processing and accounted for approximately one‐third of the ER60 associated with the transporter associated with antigen processing. These results demonstrate that ER60 assists in the creation of conserved disulfide bonds within the class I HC through the formation of a mixed disulfide intermediate.

show abstract

“…One report claimed that all W6/32-reactive molecules displayed a basic amino acid at this position [9], whereas unreactive molecules had a neutral amino acid. In a second paper the presence of cysteine at position 121 was correlated with a lack of W6/32 reactivity [3]. In dolphin, position 121 is alanine, but W6/32 reacts strongly with the same dolphin PBLs.…”

Section: Discussionmentioning

confidence: 99%

Molecular Cloning of Bottle-Nosed Dolphin (Tursiops truncatus) MHC Class I cDNA.

1998

View full text Add to dashboard Cite

ABSTRACT. Using polymerase chain reaction, bottle-nosed dolphin (Tursiops truncatus) major histocompatibility complex (DoLA) class Iα chain cDNA was cloned and sequenced. Predicted amino acid sequences of DoLA class Iα chain have cystein residues for intradomain disulfide bond formation and N-linked glycosylation sites, suggesting that DoLA class Iα chain molecules construct α1, α2, and α3 domain structures. Similarity of DoLA class Iα chain cDNA to land mammal MHC class Iα chain cDNA was 90.4% in cattle, 90.2% in horse, 89.4% in sheep, and 87.8% in human. This investigation suggests that DoLA is closely related to land mammals. -KEY WORDS: bottle-nosed dolphin, MHC class I cDNA.

show abstract

Unusual association of beta 2-microglobulin with certain class I heavy chains of the murine major histocompatibility complex.

Abstract: Class I products of the major histocompatibility complex (MHC) comprise a heavy chain of about 45 kDa noncovalently linked to a 12-kDa P2-microglobulin (132m) light chain encoded on a different chromosome. We find that class

Cited by 12 publications

References 32 publications

Expression of the W6/32 HLA epitope by cells of rat, mouse, human and other species: critical dependence on the interaction of specific MHC heavy chains with human or bovine β₂‐microglobulin

Expression of the W6/32 HLA epitope by cells of rat, mouse, human and other species: critical dependence on the interaction of specific MHC heavy chains with human or bovine β₂‐microglobulin

ER60/ERp57 forms disulfide‐bonded intermediates with MHC class I heavy chain

Molecular Cloning of Bottle-Nosed Dolphin (Tursiops truncatus) MHC Class I cDNA.

Contact Info

Product

Resources

About

Unusual association of beta 2-microglobulin with certain class I heavy chains of the murine major histocompatibility complex.

Abstract: Class I products of the major histocompatibility complex (MHC) comprise a heavy chain of about 45 kDa noncovalently linked to a 12-kDa P2-microglobulin (132m) light chain encoded on a different chromosome. We find that class

Cited by 12 publications

References 32 publications

Expression of the W6/32 HLA epitope by cells of rat, mouse, human and other species: critical dependence on the interaction of specific MHC heavy chains with human or bovine β2‐microglobulin

Expression of the W6/32 HLA epitope by cells of rat, mouse, human and other species: critical dependence on the interaction of specific MHC heavy chains with human or bovine β2‐microglobulin

ER60/ERp57 forms disulfide‐bonded intermediates with MHC class I heavy chain

Molecular Cloning of Bottle-Nosed Dolphin (Tursiops truncatus) MHC Class I cDNA.

Contact Info

Product

Resources

About

Expression of the W6/32 HLA epitope by cells of rat, mouse, human and other species: critical dependence on the interaction of specific MHC heavy chains with human or bovine β₂‐microglobulin

Expression of the W6/32 HLA epitope by cells of rat, mouse, human and other species: critical dependence on the interaction of specific MHC heavy chains with human or bovine β₂‐microglobulin