HGNC Approved Gene Symbol: B2M
Cytogenetic location: 15q21.1 Genomic coordinates (GRCh38) : 15:44,711,517-44,718,145 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 15q21.1 | Amyloidosis, hereditary systemic 6 | 620659 | 3 | |
| Immunodeficiency 43 | 241600 | Autosomal recessive | 3 |
Beta-2-microglobulin is a serum protein found in association with the major histocompatibility complex (MHC) class I heavy chain on the surface of nearly all nucleated cells (Gussow et al., 1987).
Cunningham et al. (1973) reported the complete amino acid sequence of the beta-2-microglobulin protein. It is a single polypeptide chain with a molecular mass of 11.6 kD that shows homology to immunoglobulins and HLA, suggesting a common evolutionary origin.
Suggs et al. (1981) isolated a partial cDNA clone corresponding to the B2M gene. The mature protein is predicted to contain 99 amino acids.
Gussow et al. (1987) isolated a full-length clone corresponding to the human B2M gene from a human lymphoblastoid cell cDNA library. The deduced 99-residue protein shows 70% amino acid sequence similarity to the mouse protein.
Gussow et al. (1987) determined that the B2M gene contains 4 exons and spans approximately 8 kb.
Goodfellow et al. (1975) and Smith et al. (1975) mapped the B2M gene to chromosome 15 by somatic cell hybridization.
Manolov et al. (1979) reported that the Daudi lymphoblastoid cell line, which is derived from Burkitt lymphoma (113970) and lacks both HLA antigens and beta-2-microglobulin, has 1 normal chromosome 15 and 1 with a deletion of 15q12-q21. Using high resolution banding techniques, Zhang and Zech (1981) concluded that the abnormal chromosome 15 in the Daudi cell line is del(15)(q13q15).
Cox et al. (1982) assigned the mouse B2m gene to mouse chromosome 2, which is syntenic to human chromosome 15, and suggested that B2M is not linked to major histocompatibility or immunoglobulin loci.
Arce-Gomez et al. (1978) made somatic cell hybrids between the Daudi lymphoblastoid cell line and a human cell line derived from HeLa and also showing no HLA antigens. The hybrid cells did express HLA antigens. Since Daudi cells do not express B2M despite the presence of a chromosome 15, reexpression in the hybrid cells was thought to be due to provision of beta-2-microglobulin by the other parental cell line. The experiment showed that beta-2-microglobulin is essential to expression of HLA.
On the basis of molecular cloning studies, Margulies et al. (1983) suggested that the Ly-m11 antigenic determinant demonstrated on lymphocytes by a monoclonal antibody is on the B2M molecule.
The neonatal Fc receptor (FcRn) is a heterodimer of a nonclassical MHC class I alpha chain (FCGRT; 601437) and B2M that binds the 2 most abundant serum proteins, IgG and albumin (ALB; 103600), after their constitutive cellular uptake. FcRn binds both proteins, thus acting as a salvage pathway, protecting them from lysosomal degradation and extending the catabolic half-lives of both proteins (Wani et al., 2006).
Disease Associations
Like immunoglobulins, prealbumin, and the beta protein (APP; 104760) found in the amyloid of Alzheimer disease (104300), beta-2-microglobulin has a predominantly beta-pleated sheet structure that may adopt the fibrillar configuration of amyloid in certain pathologic states (Cunningham et al., 1973).
Beta-2-microglobulin had been found in the serum of normal individuals and in the urine in elevated amounts in patients with Wilson disease (277900), cadmium poisoning, and other conditions leading to renal tubular dysfunction (Berggard and Bearn, 1968).
Hemodialysis-related amyloidosis (HRA) is a form of systemic amyloidosis with a predilection for the synovium and bone that occurs with a disturbingly high frequency among patients on long-term hemodialysis. The clinical features include carpal tunnel syndrome, erosive arthropathy, spondyloarthropathy, lytic bone lesions, and pathologic fractures. Gejyo et al. (1985) found that protein that accumulates in amyloid-laden tissue obtained from a chronic hemodialysis patient with carpal tunnel syndrome was identical to B2M in several characteristics. Connors et al. (1985) demonstrated the in vitro creation of amyloid fibers from B2M. Gorevic et al. (1985, 1986) reported the amino acid sequence of the HRA subunit protein and identified it as beta-2-microglobulin. The occurrence of amyloidosis in these patients can be prevented by periodic use of high-permeability membranes or intermittent hemofiltration.
Charra et al. (1984) reported that 38 of 52 patients receiving hemodialysis for more than 8 years for chronic renal failure not due to amyloid nephropathy developed carpal tunnel syndrome. Tissues excised at surgical decompression contained amyloid. In 95% of these patients, shoulder pain, which was presumed to be due to amyloid deposits, was present. McClure et al. (1986) demonstrated the beta-2-microglobulin nature of the amyloid in 3 patients with carpal tunnel syndrome requiring decompression surgery after long-term hemodialysis treatment for chronic renal failure not due to amyloid nephropathy. Zingraff et al. (1990) described a patient with severe renal insufficiency who had beta-2-microglobulin amyloidosis despite the fact that dialysis had never been performed. The authors suggested that some B2M variants are more amyloidogenic than others.
Some tumors lack cell surface expression of HLA class I molecules and this may be one mechanism by which tumor cells escape immune recognition by cytotoxic T cells. In some cases, there is loss of the heavy chain surface expression encoded by the HLA-A, -B, and -C genes which is responsible; in other cases, expression of the B2M gene for the light chain is responsible. The Daudi lymphoblastoid cell line, derived from a patient with Burkitt lymphoma and lacking both HLA antigens and beta-2 microglobulin, fails to express HLA class I molecules because of a specific defect in the B2M component. In the Daudi cell line, Rosa et al. (1983) demonstrated a G-to-C transversion in the initiator ATG sequence of the B2M gene, predicted to change the initiator methionine residue to isoleucine.
In the human melanoma cell line FO-1, D'Urso et al. (1991) found that the lack of expression of HLA class I antigens was the result of a defect in the B2M gene: a deletion of the first exon of the 5-prime flanking region and of a segment of the first intron.
Bicknell et al. (1994) used single-strand conformation polymorphism (SSCP) analysis to screen a series of 37 established colorectal cell lines, 22 fresh tumor samples, and 22 normal DNA samples for mutations in the B2M gene. Exon 1 (including the leader peptide sequence) and exon 2 were screened separately. Mutations were found in 6 of 7 colorectal cell lines and 1 of 22 fresh tumors, whereas no mutations were detected in the normal DNA samples. Sequencing of these mutations showed that an 8-bp CT repeat in the leader peptide sequence was particularly variable, since 3 of the cell lines and 1 fresh tumor sample had deletions in this region. In 2 related colorectal cell lines, DLD-1 and HCT-15, 2 similar mutations were identified, a C-to-A substitution in codon 10 and a G-to-T mutation in the splice sequence of intron 1. Expression of beta-2-microglobulin was examined using a series of monoclonal antibodies in an ELISA system. Reduced expression correlated with a mutation in 1 allele of the B2M gene, whereas loss of expression was seen in instances where a line was homozygous for a mutation or heterozygous for 2 mutations.
Immunodeficiency 43
In 2 sibs, born of consanguineous parents, with immunodeficiency-43 (IMD43; 241600) originally reported by Waldmann (1969), Wani et al. (2006) identified a homozygous missense mutation in the B2M gene (A11P; 109700.0001). The findings were consistent with the hypothesis that FcRn, which contains B2M, binds IgG and albumin and serves to salvage both proteins.
In 2 Turkish sibs, born of consanguineous parents, with IMD43, Ardeniz et al. (2015) identified a homozygous loss-of-function mutation in the B2M gene (109700.0003). Patient lymphocytes showed no detectable B2M surface protein expression, and serum levels of B2M were undetectable. MHC-I was undetectable on the surface of patient cells, and there was intracellular accumulation of the MHC-I heavy chain (see HLA-A, 142800). Surface expression of CD1A (188370), CD1B (188360), and CD1C (188340) was absent on monocyte-derived dendritic cells, consistent with the notion that B2M also stabilizes the surface expression of these molecules. There was also functional inactivation of NK cells and lack of invariant natural killer T cells (iNKT). Absent neonatal Fc receptor surface expression led to low serum IgG and albumin in both sibs.
Hereditary Systemic Amyloidosis 6
In 4 affected members of a family with autosomal dominant visceral amyloidosis (AMYLD6; 620659), Valleix et al. (2012) identified a heterozygous mutation in the B2M gene (D96N; 109700.0002). The authors referred to the mutation as D76N and noted that variant nomenclature did not include the 20-amino acid signal peptide. Studies on the recombinant mutant protein showed reduced stability of the fully folded mutant protein and significantly increased conversion of the mutant protein into fibrils with amyloid-like properties under physiologic conditions, whereas the wildtype protein did not aggregate at all. In mid-adult life, the patients developed slowly progressive chronic diarrhea with weight loss and sicca syndrome. One had sensorimotor axonal polyneuropathy and orthostatic hypotension and 2 had severe autonomic neuropathy. Valleix et al. (2012) noted that the amyloid deposition in this family was different from that observed in dialysis-related amyloidosis, in which B2M-amyloid accumulates around bones and joints. In addition, serum B2M was not increased in the patients with familial disease, whereas it is increased in those with dialysis-related amyloidosis.
In 3 affected members of a Portuguese family with hereditary systemic amyloidosis, Prokaeva et al. (2022) identified a heterozygous pro52-to-leu (P52L; 109700.0004) substitution in the B2M gene. Haslett et al. (2023) identified this mutation in another patient of Portuguese descent; they considered a common ancestor possible.
Allelic variation in the B2m gene has been reported in the mouse (Robinson et al., 1981).
Class I MHC molecules, known to be important for immune responses to antigen, are expressed also by neurons that undergo activity-dependent, long-term structural and synaptic modifications. Huh et al. (2000) showed that in mice genetically deficient for cell surface class I MHC, due to deletion of either TAP1 (170260) or beta-2-microglobulin, or for a class I MHC receptor component, CD3-zeta (186780), refinement of connections between retina and central targets during development is incomplete. In the hippocampus of adult mutants, N-methyl-D-aspartate receptor-dependent long-term potentiation is enhanced, and long-term depression is absent. Specific class I MHC mRNAs are expressed by distinct mosaics of neurons, reflecting a potential for diverse neuronal functions. These results demonstrated an important role for these molecules in the activity-dependent remodeling and plasticity of connections in the developing and mature mammalian central nervous system.
The defect in hereditary hemochromatosis (235200) resides in the HFE gene (613609) in the class I MHC region. This fact lends significance to the findings of de Sousa et al. (1994), who reported a comparative histologic and quantitative analysis of iron distribution in the tissues of mice homozygous and heterozygous for knockout of the beta-2-microglobulin gene. Progressive hepatic iron overload, indistinguishable from that observed in human hemochromatosis, was found only in mice homozygous for the mutated B2M gene.
In 2 sibs, born of consanguineous parents, with immunodeficiency-43 (IMD43; 241600) originally reported by Waldmann (1969), Wani et al. (2006) identified a homozygous c.913G-C transversion in exon 1 of the B2M gene, resulting in an ala11-to-pro (A11P) substitution at the midpoint of the signal sequence. Both sibs had B2M serum levels that were less than 1.0% of normal as well as soluble HLA levels that were less than 0.2% of normal. Transfection studies showed that the mutant B2M gene resulted in reduced expression of the B2M, MHC class I, and FcRn proteins.
In 4 affected members of a family with autosomal dominant visceral amyloidosis (AMYLD6; 620659), Valleix et al. (2012) identified a heterozygous c.286G-A transition (c.286G-A, NM_004048) in the B2M gene, resulting in an asp96-to-asn (D96N) substitution. The authors referred to the mutation as D76N and noted that variant nomenclature did not include the 20-amino acid signal peptide. Studies on the recombinant mutant protein showed reduced stability of the fully folded mutant protein and significantly increased conversion of the mutant protein into fibrils with amyloid-like properties under physiologic conditions, whereas the wildtype protein did not aggregate at all. Although the high-resolution crystal structure of the mutant protein was similar to wildtype, the D76N substitution has 2 notable effects: establishment of new hydrogen bonds and increase of the isoelectric point. In mid-adult life, the patients developed slowly progressive chronic diarrhea with weight loss and sicca syndrome. One had sensorimotor axonal polyneuropathy and orthostatic hypotension and 2 had severe autonomic neuropathy. Postmortem examination of 1 patient, who died at age 70 years, showed extensive B2M-containing amyloid deposits in the spleen, liver, heart, salivary glands, and nerves. Colonic biopsy from another affected individual also contained B2M-containing amyloid deposits. Amyloid scintigraphy of 2 patients showed a heavy visceral amyloid burden in the spleen and adrenal glands, but not in heart. Valleix et al. (2012) noted that the amyloid deposition in this family was different from that observed in dialysis-related amyloidosis, in which B2M-amyloid accumulates around bones and joints. In addition, serum B2M was not increased in the patients with familial disease, whereas it is increased in those with dialysis-related amyloidosis.
In 2 Turkish sibs, born of consanguineous parents, with immunodeficiency-43 (IMD43; 241600), Ardeniz et al. (2015) identified a homozygous G-to-T transversion in intron 1 of the B2M gene (c.67+1G-T), predicted to result in a frameshift and premature termination in exon 2. Each unaffected parent was heterozygous for the mutation, which was not found in 200 control chromosomes. Patient cells showed absence of the mutant transcript, consistent with nonsense-mediated mRNA decay. Patient lymphocytes showed no detectable B2M surface protein expression, and undetectable serum levels of B2M.
In 3 members of a Portuguese family with hereditary systemic amyloidosis (AMYLD6; 620659), Prokaeva et al. (2022) identified a heterozygous 2-bp deletion/insertion (c.154_155delinsTT) in exon 2 of the B2M gene that resulted in a pro52-to-leu (P52L) substitution in the mature protein. The authors also referred to the mutation as P32L.
In a 63-year old man of Portuguese descent with cardiac amyloidosis, who had a family history of amyloidosis, Haslett et al. (2023) detected the same P52L substitution in B2M identified by Prokaeva et al. (2022). Haslett et al. (2023) considered a common ancestor possible.
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