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L Claesson-Welsh

Publications and source records attributed to L Claesson-Welsh.

131 records · Page 8Linked to original sources
PubMed1986

Oligomerization of herpes simplex virus glycoprotein B.

Glycoprotein B (gB) specified by herpes simplex virus can be extracted from virions or infected cells in the form of detergent-stable, heat-dissociable oligomers. The composition of the oligomers and requirements for their formation were investigated. Evidence is presented that the faster-migrating forms of the oligomers are homodimers of gB. Dimerization was shown to occur within minutes of polypeptide synthesis and did not depend on glycosylation, the expression of other viral proteins, or virion morphogenesis. The multiple, electrophoretically distinct forms of gB dimers differ in extent or rate of N-linked oligosaccharide processing and also have other differences that influence electrophoretic mobility.

Cell Line↗
PubMed1986

Cell surface expression of invariant gamma-chain of class II histocompatibility antigens in human skin.

A rat monoclonal antibody (McAb 21:9) reactive with the human invariant gamma-chain of class II major histocompatibility complex (MHC)-encoded antigens was isolated and was shown to react with the carbohydrate-carrying, COOH-terminal part of the gamma-chain. The McAb 21:9 binds to a molecule that is identified as the gamma-chain for the following reasons: it has an apparent m.w. of 33,000, similar to that of the gamma-chain; it has a two-dimensional gel migration pattern identical to that of the gamma-chain; and it associates with immature, but not processed class II antigens. When used for immunohistochemical staining on sections of normal human skin, only dendritic, class II MHC antigen, and anti-Leu-6 reactive Langerhans cells are labeled in the epidermis. HLA-DR-expressing keratinocytes present in the tuberculin reaction, cutaneous T cell lymphoma, and lichen planus, however, did not react with the anti-gamma-chain antibody, nor with a HLA-DQ-reactive antibody. Cell surface expression of the gamma-chain was observed on 1 to 3% of normal viable epidermal cells in suspension. By using double indirect immunofluorescence, it was possible to demonstrate the simultaneous binding of anti-gamma-chain, anti-HLA-DR, anti-Leu-10, and anti-Leu-6 antibodies, respectively, on the same cells, thus confirming their identity as Langerhans cells. The presence of the gamma-chain on the surface of the immunocompetent Langerhans cells may indicate that the cell surface, not the cytoplasm as has been suggested, is the site of the primary function of the gamma-chain.

Adult↗
PubMed1986

Class II MHC antigen expression in the atherosclerotic plaque: smooth muscle cells express HLA-DR, HLA-DQ and the invariant gamma chain.

Class II antigens of the major histocompatibility complex (MHC) are normally expressed only by cells of the immune system. They may, however, also appear on other cells, both in vivo and in vitro. We have studied class II MHC antigen expression on human arterial smooth muscle cells using immunocytochemical analysis of surgical biopsies. The class II antigens, HLA-DQ and HLA-DR are virtually absent from cells of normal arteries, but appear in atherosclerotically transformed tissue, where the majority of cells express HLA-DR, and one-third of the cells express HLA-DQ. These atherosclerotic plaques are composed of a heterogeneous population of cells, which includes smooth muscle cells, macrophages, and T cells. Among smooth muscle cells containing the muscle-specific intermediate filament protein desmin, one-third of the cells express HLA-DR and almost as many express HLA-DQ. These cells also contain the invariant gamma chain, which is associated with class II antigens during intracellular transport. Plaque macrophages, in contrast, are usually of the DQ-DR+ phenotype. The patterns of class II antigen expression are discussed in relation to cell differentiation and pathogenesis of disease.

Antigens, Differentiation, B-Lymphocyte↗
PubMed1985

Implications of the invariant gamma-chain on the intracellular transport of class II histocompatibility antigens.

We have examined the role of the invariant gamma-chain on the intracellular transport of human class II histocompatibility antigens. mRNA was selected by hybridization to cDNA corresponding to class II alpha-, beta-, and gamma-chains, and the obtained mRNA fractions were injected individually and in various combinations into X. laevis oocytes. Translation products were isolated after various periods of chase, and their carbohydrate moieties were analyzed to monitor the subcellular localization of polypeptide chains. A mixture of alpha-, beta-, and gamma-chains, or gamma-chains alone, were transported and glycosylated to the same extent as in a B lymphoblastoid cell line. However, although alpha- and beta-chains formed a complex in the absence of the gamma-chain, the transport of this complex was slowed down. Furthermore, the glycosylation of alpha- and beta-chains appeared incomplete. Thus, the invariant gamma-chain seems to play a crucial role for the rate of transport and glycosylation of class II alpha- and beta-chains.

Animals↗