scholarly journals THE NATURE OF THE VIRUS RECEPTORS OF RED CELLS

1948 ◽  
Vol 87 (4) ◽  
pp. 315-328 ◽  
Author(s):  
George K. Hirst
Keyword(s):  
Influenza Virus ◽  
Type A ◽  
Red Cells ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Virus Inhibitor ◽  
Virus Receptors

Evidence has been offered that influenza virus which has been heated at 56°C. for 30 or more minutes loses some of its capacity to agglutinate red cells and may completely lose its power to elute from cells on which it has been adsorbed. Such heat-inactivated virus does not possess the capacity to destroy the virus inhibitor in normal rabbit serum and this appears to be the explanation of the higher agglutinin inhibitory levels obtained with serum and heated virus as compared with serum and untreated virus. The heat-inactivated virus can be used to measure the inhibitor substance in normal rabbit serum. By two different methods it has been demonstrated that the inhibitor is destroyed in the presence of unheated influenza virus, as measured by inhibition titrations with virus inactivated at 56°C. The destruction of inhibitor by virus of either type A or B can be measured by virus of either type with similar results.

scholarly journals THE NATURE OF THE VIRUS RECEPTORS OF RED CELLS

1948 ◽  
Vol 87 (4) ◽  
pp. 301-314 ◽  
Author(s):  
George K. Hirst
Keyword(s):  
Influenza Virus ◽  
Sodium Periodate ◽  
Cell Receptor ◽  
Normal Serum ◽  
Red Cells ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Red Cell ◽  
Virus Receptors ◽  
Serum Inhibitor

The influenza virus receptors of fowl red cells and the influenza virus inhibitor of normal rabbit serum have the following attributes in common: They are stable at high temperatures and in solutions of pH as high as 10.0. They both resist destruction by a number of oxidizing agents but are readily destroyed by sodium periodate, trypsin, and influenza virus. These facts suggest that the red cell receptor and the normal serum inhibitor are either the same or analogous substances and that they may belong to the mucoprotein class of compounds.

scholarly journals THE NATURE OF THE VIRUS RECEPTORS OF RED CELLS

1949 ◽  
Vol 89 (2) ◽  
pp. 233-243 ◽  
Author(s):  
George K. Hirst
Keyword(s):  
Influenza Virus ◽  
Sodium Chloride ◽  
Sodium Periodate ◽  
Small Extent ◽  
Red Cells ◽  
Cholera Vibrio ◽  
Virus Receptors

Influenza virus, treated with sodium periodate, was adsorbed well on red cells but lacked the capacity for spontaneous elution. Heated virus was eluted from red cells by the action of cholera vibrio filtrate, unheated influenza virus, and to a small extent by heating at 56°C. Periodate-treated virus was not elutable by these methods but was liberated by exposure of the adsorbing cells to concentrations of sodium chloride of 5 to 10 per cent. This treatment had no effect on elution of heated virus.

scholarly journals IMMUNE RESPONSE OF RABBITS TO INJECTION OF PLASMODIUM KNOWLESI

1939 ◽  
Vol 70 (2) ◽  
pp. 131-139 ◽  
Author(s):  
Monroe D. Eaton ◽  
L. T. Coggeshall
Keyword(s):  
Immune Response ◽  
Plasmodium Knowlesi ◽  
Conclusive Evidence ◽  
Red Cells ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Passive Protection ◽  
Normal Monkey ◽  
Protective Antibodies

Specific complement-fixing antibodies are produced in the serum of rabbits in response to injections of living or dead Plasmodium knowlesi. Sera from rabbits receiving injections of either parasitized or normal monkey erythrocytes are parasiticidal in vitro for P. knowlesi. Because absorption of parasiticidal rabbit sera with normal monkey erythrocytes abolishes the parasiticidal effect, it is concluded that the effect is largely due to an antibody to the red cells. Normal rabbit serum is not parasiticidal. Experiments on passive protection in monkey malaria with serum from rabbits which have received intraperitoneal injections of living or dead P. knowlesi yield no conclusive evidence that protective antibodies are formed.

scholarly journals THE NATURE OF THE VIRUS RECEPTORS OF RED CELLS

1949 ◽  
Vol 89 (2) ◽  
pp. 223-232 ◽  
Author(s):  
George K. Hirst
Keyword(s):  
Influenza Virus ◽  
Human Plasma ◽  
Red Cells ◽  
Globulin Fraction ◽  
Virus Receptors

A substance (VHI) exists in human plasma which inhibits the agglutination of red cells by influenza virus and is distinct from influenza antibody. When plasma is fractionated by alcohol in the cold the VHI comes out mainly with a mixture of lipid-free alpha and beta globulins (fraction IV-4). On further fractionation the activity comes out with a fraction consisting mainly of beta1 globulin (fraction IV-7). Boiling fraction IV-4 or IV-7 after considerable dilution brings about a large increase in the amount of VHI, much more than can be detected in the original plasma. A similar VHI has been extracted from the ghosts of fowl red cells.

scholarly journals PURIFICATION OF AN INFLUENZA VIRUS SUBSTRATE, AND DEMONSTRATION OF ITS COMPETITIVE ANTAGONISM TO APPLE PECTIN

1949 ◽  
Vol 89 (1) ◽  
pp. 11-22 ◽  
Author(s):  
D. W. Woolley
Keyword(s):  
Influenza Virus ◽  
Calcium Ions ◽  
Water Soluble ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Apple Pectin ◽  
Alkaline Extract ◽  
Competitive Antagonism ◽  
Soluble Material

A substance was demonstrated in erythrocytes which antagonized the inhibiting effect of apple pectin on influenza virus hemagglutination. This substance was purified and found to be a water-soluble material, rather labile, and with some properties which suggested that it contained a polysaccharide. It was destroyed in vitro by highly purified preparations of the virus. It occurred in greatest amount in human erythrocytes and to a lesser extent in the red cells of species not susceptible to the virus. It was also found in normal rabbit serum. Calcium ions were found to be essential to the action of apple pectin in causing inhibition of virus hemagglutination. A second substance was purified from an alkaline extract of erythrocytes, and shown likewise to have an effect antagonistic to that of pectin. However, this latter material was not destroyed by the virus, and seemed to owe its effect to the binding of calcium ions.

scholarly journals ELECTROKINETIC PHENOMENA. III

1930 ◽  
Vol 14 (2) ◽  
pp. 163-177 ◽  
Author(s):  
Harold A. Abramson
Keyword(s):  
Red Cells ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Red Cell ◽  
Protein Film ◽  
Electrokinetic Phenomena ◽  
Cell Destruction ◽  
Electrophoretic Mobilities ◽  
Isoelectric Points ◽  
Complete Protein

A survey of the published electrophoretic mobilities of certain mammalian red cells reveals that the isoelectric points accorded to these cells are the result of equilibria incidental to red cell destruction. The electrophoretic mobilities of normal washed sheep and human cells have now been studied in 0.85 per cent NaCl solutions from about pH 3.6 to 7.4. All measurements were made within 2 minutes of the preparation of the suspension of red cells. In no case was reversal of sign of charge observed under these conditions. Reversal of sign of charge occurred only after sufficient time had elapsed to permit sufficient adsorption of the products of red cell destruction. There is little change in mobility as the pH of the medium is decreased. Reversal of sign of charge does occur in the presence of normal and immune (anti-sheep) rabbit sera. The isoelectric point determined under these conditions does not appear to be connected specifically with the immune body but is perhaps associated with phenomena incidental to red cell destruction and the presence of serum. The characteristic lowering of mobility by amboceptor occurs, however, from pH 4.0 to pH 7.4. The curves of mobility plotted against pH for normal and for immune sera support the viewpoint that the identity of the isoelectric points for normal and sensitized sheep cells is not primarily concerned with the immune reaction. It is most unlikely that an "albumin" or a "globulin" surface covers red cells with a complete protein film. Although serum protein reacts with red cells in acid solutions, this is not demonstrable for gelatin. The lowering of mobility usually ascribed to anti-sheep rabbit serum may also occur, but to a lesser degree, in normal rabbit serum. This diminution of mobility is not, in the first place, associated with sensitization to hemolysis induced by complement. This supports the view that only a very small part of the red cell surface need be changed in order to obtain complete hemolysis in the presence of complement.

scholarly journals A HEMOLYTIC SYSTEM ASSOCIATED WITH ENTERITIS IN RABBITS

1963 ◽  
Vol 117 (4) ◽  
pp. 647-661 ◽  
Author(s):  
Robert S. Evans ◽  
Margaret Bingham ◽  
Russell S. Weiser
Keyword(s):  
Red Cells ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Red Cell ◽  
Heat Stable ◽  
Heat Labile

A disease characterized by frequent association of enteritis and polyagglutinable cells often develops in weanling rabbits. The red cell lesion renders the cells susceptible to agglutination and hemolysis in normal rabbit sera. The degree of red cell abnormality varies among different animals and disappears when the animals recover. The abnormality of the red cells responsible for their polyagglutinability and susceptibility to hemolysis was resistant to the action of trypsin or papain and persisted in heated stroma preparations derived from polyagglutinable cells. The factors necessary for agglutination and hemolysis of the polyagglutinable cells are present in normal rabbit sera but are lacking in the sera of affected rabbits. These factors returned to normal levels as the polyagglutinable cell lesion disappeared. The sera of rabbits with polyagglutinable cells contained normal levels of complement and properdin. Whereas the agglutinating factor in normal sera is heat-stable at 56°C for 30 minutes, the hemolytic factor is heat labile. The hemolytic factor is apparently distinct from complement and properdin since it was adsorbed from normal rabbit serum by zymosan or by polyagglutinable cells at 0°C. However, complement was fixed when normal rabbit serum was reacted with stroma from polyagglutinable cells. Hemolysis of polyagglutinable cells by normal rabbit serum at 25°C was inhibited by preliminary incubation of the mixture at 0°C prior to incubation at 25°C. Evidence was obtained which indicated that this inhibition was due to progression of a reaction involving Ca++ independent of a reaction involving Mg++.

Detection of Viral Antigens in Mouse and Rat Tumor Cells by Immunoelectron Microscopy Following Periodate-Lysine-Paraformaldehyde (PLP) Fixation

1976 ◽  
Vol 34 ◽  
pp. 252-253
Author(s):  
Y. Ohtsuki ◽  
G. Seman ◽  
J. M. Bowen ◽  
M. Scanlon ◽  
L. Dmochowski
Keyword(s):  
Immunoelectron Microscopy ◽  
Mammary Tumor ◽  
Type A ◽  
Rabbit Serum ◽  
Virus Particles ◽  
Viral Antigens ◽  
Culture Cells ◽  
Mouse Mammary Tumor ◽  
Tumor Virus ◽  
Immunoperoxidase Labeling

Recently, periodate-lysine-paraformaldehyde (PLP) fixation was reported for immunoelectron microscopy (1). In PLP fixation, carbohydrates are oxidized by periodate and cross-linked by lysine; paraformaldehyde stabilizes proteins and lipids. By using PLP fixation, intracytoplasmic type A viral antigens have been previously demonstrated by immunoperoxidase labeling (2). In the present study, PLP fixation has been applied for the detection of the same antigens in mouse mammary tumor culture cells by both immunoferritin and immunoperoxidase methods. Rabbit anti-intracytoplasmic type A virus serum (anti-A), kindly provided by Dr. M. Muller (3), rabbit anti-strain A mouse mammary tumor virus (anti-MMTV) and preimmune rabbit serum as control were used to detect viral antigens in cells of C3H/HeJ strain mouse mammary tumor culture. Attempts have been also made to demonstrate peroxidase labeling of type C virus particles in frozen sections of an SD-MSV-induced NZB rat bone tumor tissue by rabbit anti-MuLV serum.

Identification of Maize Rayado Fino Virus by Immunoelectron Microscopy

1985 ◽  
Vol 43 ◽  
pp. 636-637
Author(s):  
O. E. Bradfute
Keyword(s):  
Electron Microscopy ◽  
Zea Mays ◽  
Costa Rica ◽  
Severe Disease ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Virus Particles ◽  
Far North ◽  
Maize Rayado Fino Virus ◽  
Antibody Coating

Maize rayado fino virus (MRFV) causes a severe disease of corn (Zea mays) in many locations throughout the neotropics and as far north as southern U.S. MRFV particles detected by direct electron microscopy of negatively stained sap from infected leaves are not necessarily distinguishable from many other small isometric viruses infecting plants (Fig. 1).Immunosorbent trapping of virus particles on antibody-coated grids and the antibody coating or decoration of trapped virus particles, was used to confirm the identification of MRFV. Antiserum to MRFV was supplied by R. Gamez (Centro de Investigacion en Biologia Celular y Molecular, Universidad de Costa Rica, Ciudad Universitaria, Costa Rica).Virus particles, appearing as a continuous lawn, were trapped on grids coated with MRFV antiserum (Fig. 2-4). In contrast, virus particles were infrequently found on grids not exposed to antiserum or grids coated with normal rabbit serum (similar to Fig. 1). In Fig. 3, the appearance of the virus particles (isometric morphology, 30 nm diameter, stain penetration of some particles, and morphological subunits in other particles) is characteristic of negatively stained MRFV particles. Decoration or coating of these particles with MRFV antiserum confirms their identification as MRFV (Fig. 4).

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