H‐2 antigens on murine leukemia cells and viruses

Dorfman, N. A.; Степина, В Н; Ievleva, E. S.

doi:10.1002/ijc.2910090328

Cited by 6 publications

(2 citation statements)

References 8 publications

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“…This separation of HLA and measles virus antigens was consistently observed in over 100 cells studied in two different lymphoblastoid cell lines. These findings were further confirmed when the infectious titer of measles virus grown in HLA-A2 cells was not significantly reduced after incubation with antibody directed against HLA-A2 and C. In concert with our findings, HLA antigens are not detected by electron microscopy on the envelope of Epstein-Barr virus (25), nor are H-2 antigens frequently (4-5%) observed on the surface of murine leukemia virus particles (26). Although murine leukemia virus particles seem to be independent of the histocompatibility complex during the maturation of virus through the plasma membrane, the co-capping of Friend leukemia virus gp69 and antibodies directed towards the major H-2 complex has recently been reported (11).…”

Section: Discussionsupporting

confidence: 89%

Human histocompatibility determinants and virus antigens: effect of measles virus infection on HLA expression.

Haspel¹,

Pellegrino²,

Lampert³

et al. 1977

The Journal of Experimental Medicine

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Histocompatibility antigens on the surface of human lymphoblastoid cells were quantified by a microadsorption technique. During the course of measles virus infection, no quantitative or qualitations in surface HLA antigens were observed. In contrast, infection with poliovirus type 1 or vesicular stomatitis virus, or treatment with puromycin (50 microgram/ml) resulted in a significant decrease in surface HLA. These experiments suggest that an inhibition of host protein synthesis rather than the insertion of virus-specificied antigens into the membrane results in a net decrease in amounts of this cell surface antigen. The HLA antigens also appear to be both functionally and structurally distinct from measles virus surface antigens. Pretreatment of cells with HLA-directed antibody did not prevent the infection of these cells by measles virus, thus HLA antigens appear unrelated to the measles virus receptor site on the plasma membrane. Electron microscopic studies revealed that measles virus maturation occurs at membrane sites devoid of demonstrable HLA. Furthermore, HLA antigens could not be detected on the surfaces of mature infectious virions.

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Section: Discussionsupporting

confidence: 89%

Human histocompatibility determinants and virus antigens: effect of measles virus infection on HLA expression.

Haspel¹,

Pellegrino²,

Lampert³

et al. 1977

The Journal of Experimental Medicine

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“…Studies of Aoki et al (1), Aoki and Takahashi (2), Dorfman et al (12), and Witte and Weissmann (52) indicate that the site of virion budding is unique and that incorporation of cell membrane proteins is extremely selective and specific for virus-encoded proteins. Therefore, the 50-to 100-fold concentration of gp55 by retroviruses suggests a nonrandom association of this particular membrane protein with the virion.…”

Section: Resultsmentioning

confidence: 99%

55,000-dalton, retrovirus-associated, cell membrane glycoprotein: purification and quantitative measurements of expression in viruses, cells, and tissues.

Scheinberg¹,

Strand²

1981

Mol. Cell. Biol.

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We have purified to homogeneity and characterized a 55,000-dalton rat cell membrane glycoprotein, gp55. This protein was originally identified in preparations of a defective pseudotype of the Kirsten sarcoma virus and shown to be present in several rodent retrovirus particles. The gp55 was purified from this defective virus by concanavalin A and heparin affinity chromatography, as well as by preparative sodium dodecyl sulfate-gel electrophoresis. Both preparations displayed similar purity and antigenic characteristics. The '25I-labeled gp55 was precipitated by antisera against rodent retroviruses, but not by monospecific antisera against purified type C virus structural proteins, thus indicating that gp55 was retrovirus associated, but unrelated to known retrovirus structural proteins. Competition radioimmunoassay with an anti-rat virus serum which recognized rodent group-specific antigens on gp55 indicated: (i) the presence of gp55 antigens in 15 rodent cell lines, but not 10 nonrodent cell lines; (ii) no effect of viral infection or cell transformation on the amount of gp55 expressed; (iii) up to 100-fold increases in the concentration of the gp55 antigens in nine rodent retroviruses, but not in five nonrodent viruses, as compared to cells; (iv) the presence of gp55 in rodent sera, especially of the NZB mouse, where anti-gp55 antibody was also detected; (v) a lymphoid and epithelial tissue distribution of gp55 in rats and mice. Additional competition radioimmunoassays with a broadreacting antivirus serum also detected the presence of gp55 in nonrodent, mink, and human cells and thus distinguished rat type, rodent group, and interspecies antigenic determinants on gp55. In conclusion, gp55 is a cell membrane glycoprotein associated in high concentration with retroviruses.The type C oncoviruses are enveloped ribonucleic acid (RNA) retroviruses which form particles by budding through the plasma membranes of infected cells (25). The virus encodes six structural proteins, of which two form the envelope of the virion and four form the nucleoprotein core (14). During the process of virion budding, the particles also incorporate many cellular components, including nucleic acids (8), lipids (35), histocompatibility antigens (6), adenosine triphosphatases (11), kinases (36, 43), and actin. Whereas the cellular lipids and nucleic acids are both specific and required for virion structure, the role of the other cell components in virions is unknown.We have reported the isolation and characterization of a defective mammalian oncovirus (KW virus), which is comprised of only one virionencoded structural protein (33). Instead, these particles contain several novel proteins incorporated from the rat host cell membranes. The cellular and viral expression of three of these proteins (gpllO, gp55, p20) has been partially characterized (38). gpllO and p20 are transformation related. In contrast, gp55, a 55,000-dalton glycoprotein, appeared common to several rodent retrovirus preparations, but was unrelated to virus transformation. W...

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Viruses as immunological adjuvants in cancer

Lindenmann

1974

Biochimica et Biophysica Acta (BBA) - Reviews on Cancer

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H‐2 antigens on murine leukemia cells and viruses

Cited by 6 publications

References 8 publications

Human histocompatibility determinants and virus antigens: effect of measles virus infection on HLA expression.

Human histocompatibility determinants and virus antigens: effect of measles virus infection on HLA expression.

55,000-dalton, retrovirus-associated, cell membrane glycoprotein: purification and quantitative measurements of expression in viruses, cells, and tissues.

Viruses as immunological adjuvants in cancer

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