Failure of Neuraminidase to unmask Histocompatibility Antigens on Trophoblast

DURING outbred pregnancy the mother is exposed to genetically foreign tissue because the offspring inherits transplantation antigens from the father. The survival of the foetus is ensured by the intervention of the trophoblast which does not express transplantation antigens between mother and foetus: mouse trophoblast is not rejected even when transplanted into immune recipients^1,3. The mechanism of this failure to express histocompatibility antigens is not understood^1–4, but Kirby et al. have suggested that the extracellular fibrinoid surrounding trophoblast cells is involved^5,6. Currie has suggested that the thick sialomucinous glycocalyx of the trophoblast cell might “mask” the histocompatibility antigens on the trophoblast^7,8 and has demonstrated that neuraminidase unmasked these antigens⁸. Our experiments, however, show that trophoblast incubated with neuraminidase cannot sensitize allogeneic mice to donor histocompatibility antigens. Furthermore, pretreatment of trophoblastic implants with neuraminidase did not interfere with their proliferation and growth in highly immune allogeneic recipients.     

Constant Production of Type C Virus Particles in a Continuous Tissue Culture derived from Pleural Effusion Cells of a Lymphoma Patient

PARTICLES resembling viruses were first observed in organs of mice with spontaneous leukaemia and in thin sections of a biopsy specimen from a lymph node of a patient with acute lymphocytic leukaemia by Dmochowski and Grey¹. They also found them in some biopsy specimens of lymph nodes and bone marrows before and after growth in tissue culture^2,3,8. Recent reports have described the presence of type C virus particles in other human tumours including liposarcoma⁴, osteosarcoma^5,6, giant cell tumour⁹, rhabdomyosarcoma (unpublished results of L. D. and E. S. P.) and breast carcinoma⁷.     

Antigenic Heterogeneity of Human IgD Immunoglobulins

SUBCLASSES of the three major classes of human immunoglobulins, IgG, IgA and IgM, are recognized: four of IgG are well defined^1,2 and at least two of IgA^3–5 and two of IgM^6,7 have been demonstrated. This communication presents evidence for the existence of an antigenic heterogeneity in the heavy chains of IgD, which may also be indicative of subclasses within this class of immunoglobulin.     

Coexistence of Intraspecies and Interspecies Specific Antigenic Determinants on the Major Structural Polypeptide of Mammalian C-type Viruses

THE report of a shared viral antigen (termed gs-3) among mammalian C-type viruses from four species¹, extending an earlier report of cross reactivity between mouse and cat viral antigens², has far reaching implications in the search for human cancer viruses or their gene products. The report is confirmed both by the data presented here and also by the data obtained by another laboratory³. Our gel diffusion assays using various selected sera against mouse, hamster and cat crude and purified C-type viral antigens indicate that the cross reactive antigenic determinants are specifically present on the major structural polypeptide of C-type viruses. The polypeptide also carries species specific determinants. These conclusions are drawn from complement fixation and gel diffusion tests using six types of antisera (either individual sera or pools) prepared as described in Table 1.     

Binding of Radioactively Labelled Concanavalin A and Wheat Germ Agglutinin to Normal and Virus-transformed Cells

VARIOUS substances isolated from plants cause animal cells to clump. Several of these lectins¹ preferentially agglutinate cells which have been transformed spontaneously or by chemicals or viruses^2–7. The best known lectins of this class are concanavalin A (Con A) isolated from jack beans⁸ and wheat germ agglutinin⁴, which seem to bind to carbohydrate groups on the cell surface. The determinants recognized by the lectins seem to be N-acetyl-D-glucosamine for WGA⁴ and probably α-methyl-D-glucopyranoside for Con A⁶.     

Reduced Polyteny of Ribosomal RNA Cistrons in Giant Chromosomes of <Emphasis Type="Italic">Drosophila hydei</Emphasis><Superscript>*</Superscript>

The polytenization of rRNA cistrons in Drosophila species is studied in an attempt to follow the course of under-representation of heterochromatic compared with euchromatic chromosome regions.     

Synthesis by Ribosomes of Viral Coat Protein containing Ester Linkages

Peptidyl transferase, the ribosomal enzyme which synthesizes peptide bonds, can catalyse the formation of ester linkages between α-hydroxyacyl-tRNA and aminoacyl-tRNA when ribosomes carry out a specific translation of phage R17 RNA in vitro.     

N-Acetylcysteine inactivates Migration Inhibitory Factor and Delayed Hypersensitivity Reactions

In vitro studies suggest that delayed hypersensitivity follows the production of migration inhibitory factor (MIF) by sensitive lymphocytes in the presence of specific antigen. This factor arrests the migration of macrophages in vitro and in vivo. After attraction, aggregation and activation in vivo, these bystander cells produce toxic substances which induce the local reaction¹. When lymphocytes from tuberculin (PPD) sensitized guinea-pigs were incubated with PPD, cell-free supernatant fluids of the cultures contained MIF². Such migration inhibitory fluids injected intradermally with PPD, into PPD-sensitive animals, enhanced the delayed hypersensitivity reaction³. Concentrated migration inhibitory supernatant fluids injected intradermally into unsensitized animals produced local reactions of induration and erythema within 6 h; reactions reached a maximum after 16 h. Histologically there was an infiltrate of mononuclear cells at the site of injection and neutrophils and eosinophils were also present¹.     

Structure of the Purple Membrane

IN the preceding article¹ it has been shown that a cell membrane fragment, the purple membrane, isolated from Halobacterium halobium² contains retinal bound in a mole ratio of 1 : 1 to a protein of molecular weight 26,000 which is the only protein present. We now describe the structure of the purple membrane and its localization in the bacterial cell envelope.