Chemical characteristics of Ia antigens

Schwartz, Benjamin D.; Cullen, Susan E.

doi:10.1007/bf00198647

Cited by 29 publications

(4 citation statements)

References 61 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Under reducing conditions, the apparent molecular weights of the a and 18 subunits for all threeof these products are 34,000 and 26,000, respectively. Under nonreducing conditions, the a and ,3 chains are disulfide-bonded; however, lysis of the cells in the presence of an alkylating agent results in the disappearance of the a-,8 dimer and the appearance of only a and f3 chains, indicating that the disulfide bonding occurs during lysis with detergent (22,28). In contrast, two alleles (d andp) of the EIC subregion encode a and ,8 subunits that have apparent molecular weights of 31,000 and 29,000, respectively; two other EIC alleles (k and r) have a and /8 subunits of 34,000 and 28,000, respectively.…”

Section: A Antigens Are Structually Different From E/c Antigensmentioning

confidence: 99%

Organization of the Immune Response Genes

Uhr

Capra

Vitetta

et al. 1979

Science

122

View full text Add to dashboard Cite

The I region of the major histocompatibility complex contains immune response genes that display considerable polymorphism; that is, there are many alleles at each locus. These genes regulate the immune response to antigen by mediating intercellular communication among lymphoreticular cells. An analysis of the primary structure of the products of two subregions of (I-A, I-E/C) was undertaken in order to understand the genetic organization of the region, the evolution of the genes and, eventually, their function.

show abstract

Section: A Antigens Are Structually Different From E/c Antigensmentioning

confidence: 99%

Organization of the Immune Response Genes

Uhr

Capra

Vitetta

et al. 1979

Science

122

View full text Add to dashboard Cite

show abstract

“…The I-A molecule consists of two non-covalently associated polypeptide suhunits of 35,000 daltons (a chain) and 26,000 daltons (fi chain). The I-E molecule is structurally similar, with a 32,000dalton a chain and a 29,000-dalton P chain [14,16]. The human la or class II antigens are encoded within the MHC (chromosome six) and are borne on molecules composed of two non-covalently associated glyeoprotein chains of 33,000-34,000 daltons (a chain) and 28,000-30,000 daltons (fi chain) [4,6].…”

mentioning

confidence: 99%

The MT4 Allodeterminant Is Borne on an HLA‐DS Molecule on DR5 Cells

et al. 1984

View full text Add to dashboard Cite

Human HLA-DR molecules have been shown to be structurally homologous to the murine I-E subregion molecules by amino acid sequence analysis. Recent studies have demonstrated the isolation of an I-A subregion-homologous molecule (HLA-DS) from human B-cell lines with the rabbit antiserum RbO3, made against a marmoset I-A-like Ia molecule. Previous work from our laboratory has demonstrated that the DR5 homozygous lymphoblastoid cell line Swei expresses at least two different Ia alpha chains and four different Ia beta chains, which associate to form four distinct human Ia molecules, alpha 1 beta 2, alpha 1 beta 3, alpha 2 beta 1, and alpha 2 beta 4, and that the alpha 2 beta 1 molecule bears the allodeterminants MB3 and MT4. To determine whether the MT4-bearing alpha 2 beta 1 molecule was an HLA-DS molecule, the alpha 2 beta 1 molecule reactive with an anti-MT4 alloserum was compared with the Ia molecule reactive with the rabbit xenoantiserum RbO3 by two-dimensional gel electrophoresis and sequential immunoprecipitation. The alpha 2 chain and the RbO3-reactive alpha chain yielded essentially similar spot patterns. The beta 1-chain spot pattern was a subset of the RbO3-reactive beta-chain spot pattern. Sequential immunoprecipitation indicated that RbO3 removed all molecules reactive with MGH88B. These results indicate that on DR5 cells the allosera-reactive alpha 2 beta 1 molecule, which bears MT4, is an HLA-DS molecule.

show abstract

mentioning

confidence: 99%

“…Studies in a number of laboratories indicate that the La antigens are glycoprotein molecules with a molecular weight of 58,000, which can be dissociated into two nonidentical polypeptides with a molecular weight of 33,000 and 25,000 (4,21). Furthermore, the antigenic determinants of these molecules appear to reside in their protein portion (4,21). Recently, data have been reported which suggest that the I-region controls a second family of antigens, both in mice (11,17,20) and humans (20a), which have carbohydratedefined antigenic determinants.…”

mentioning

confidence: 99%

Ia antigens in serum during different murine infections

Parish¹,

Freeman²,

Cheers³

et al. 1979

Infect Immun

View full text Add to dashboard Cite

There exists in the mouse a family of I-region-controlled (Ia) antigens which carry carbohydrate-defined determinants. These antigens appear in serum as glycolipids and seem to be actively secreted by antigen-activated T-cells. This paper describes the ability of selected viral, bacterial, and protozoal infections of mice to markedly alter the serum levels of these Ia antigens. All the infectious agents examined induced substantial augmentation or suppression of serum Ia concentrations or both. Lymphocytic choriomeningitis (LCM) virus first enhanced and then suppressed serum Ia levels during the course of acute infection. Enhancement occurred during the time of ongoing virus replication and splenic lymphoproliferation while suppression coincided with the peak of the cytotoxic T-cell response and virus clearance. Listeria monocytogenes infection induced a substantial reduction in Ia levels at a time just after marked depletion of T-cells in the spleen. In contrast, Brucella abortus caused a significant increase in Ia levels 7 days postinfection, which correlates with the appearance of peak numbers of bacteria in tissues. Finally, Plasmodium yoelii, a nonlethal malarial parasite which stimulates prolonged T-cell proliferation, augmented serum Ia levels, whereas P. berghei, a lethal parasite which tends to inhibit T-cell division, suppressed Ia secretion. Possible interpretations of these different results are presented.

show abstract

Chemical characteristics of Ia antigens

Cited by 29 publications

References 61 publications

Organization of the Immune Response Genes

Organization of the Immune Response Genes

The MT4 Allodeterminant Is Borne on an HLA‐DS Molecule on DR5 Cells

Ia antigens in serum during different murine infections

Contact Info

Product

Resources

About