scholarly journals Dianthins, ribosome-damaging proteins with anti-viral properties from Dianthus caryophyllus L. (carnation)

1981 ◽  
Vol 195 (2) ◽  
pp. 399-405 ◽  
Author(s):  
F Stirpe ◽  
D G Williams ◽  
L J Onyon ◽  
R F Legg ◽  
W A Stevens

1. Dianthin 30 and dianthin 32, two proteins isolated from the leaves of Diathus caryophyllus (carnation), were purified to homogeneity by chromatography on CM-cellulose. 2. The mol.wt. of dianthin 30 is 29 500 and that of dianthin 32 is 31 700. Both dianthins are glycoproteins containing mannose. 3. Dianthins inhibit protein synthesis in a lysate of rabbit reticulocytes, with an ID50 (concentration giving 50% inhibition) of 9.15 ng/ml (dianthin 30) and 3.6 ng/ml (dianthin 32). They act by damaging ribosomes in a less-than-equimolar ratio. Protein synthesis by intact cells is partially inhibited by dianthins at a concentration of 100 microgram/ml. 4. Dianthins mixed with tobacco-mosaic virus strongly decrease the number of local lesions on leaves of Nicotiana glutinosa.

1974 ◽  
Vol 52 (1) ◽  
pp. 23-25 ◽  
Author(s):  
Mary Boxall ◽  
B. H. MacNeill

The integrity of the local-lesion technique in producing genetically homogeneous isolates of tobacco mosaic virus from Nicotiana glutinosa has been verified using strains doubly labeled with genetic markers governing symptomatology and host range.


1983 ◽  
Vol 216 (3) ◽  
pp. 617-625 ◽  
Author(s):  
F Stirpe ◽  
A Gasperi-Campani ◽  
L Barbieri ◽  
A Falasca ◽  
A Abbondanza ◽  
...  

Ribosome-inactivating proteins, similar to those already known [Barbieri & Stirpe (1982) Cancer Surveys 1, 489-520] were purified from the seeds of Saponaria officinalis (two proteins), of Agrostemma githago (three proteins), and of Asparagus officinalis (three proteins), and from the latex of Hura crepitans (one protein). The yield ranged from 8 to 400 mg/100 g of starting material. All proteins have an Mr of approx. 30000 and an alkaline isoelectric point. Their sugar content varies from 0 (proteins from S. officinalis) to 40% (protein from H. crepitans). The ribosome-inactivating proteins inhibit protein synthesis by rabbit reticulocyte lysate, the ID50 (concentration giving 50% inhibition) ranging from 1 ng/ml (a protein from S. officinalis) to 18 ng/ml (a protein from A. githago). Those which were tested (the proteins from S. officinalis and from A. githago) also inhibit polymerization of phenylalanine by isolated ribosomes, acting in an apparently catalytic manner. The protein from H. crepitans inhibited protein synthesis by HeLa cells, with an ID50 of 4 micrograms/ml, whereas the proteins from S. officinalis and from A. githago had an ID50 of more than 50-100 micrograms/ml. The ribosome-inactivating proteins from S. officinalis and from A. githago reduced the number of local lesions by tobacco-mosaic virus in the leaves of Nicotiana glutinosa.


1967 ◽  
Vol 35 (1) ◽  
pp. 183-192 ◽  
Author(s):  
M. Weintraub ◽  
H. W. Ragetli ◽  
V. T. John

Tobacco mosaic virus particles were found in small packets and in small numbers, with the electron microscope, in necrotic leaf cells of Nicotiana glutinosa when the samples were fixed in glutaraldehyde and postfixed in OsO4, and the sections were stained with heavy metals. The numbers and size of the virus packets were increased greatly when the leaves were detached from the plant after inoculation Assay of concentration showed that detachment resulted in a 30-fold increase of virus. A similar increase in the number of virus particles detected by electron microscopy was produced by keeping inoculated plants at an air temperature of 26°C. A still greater increase in concentration was effected by incubating detached inoculated leaves at 26°C. Moreover the arrangement of virus particles in these cells resembled that of a systemic virus infection. Cells in local lesions of Chenopodium amaranticolor contained large numbers of virus particles both as packets and in the loose arrangement characteristic of systemic infection. Neither the number of particles nor their arrangement was affected in this host by detaching the leaf or by changing the air temperature. It is suggested that there may be two types of localized virus infections, one of which produces virus in low concentration and is amenable to changes in virus concentration and arrangement as a result of environmental manipulation.


1984 ◽  
Vol 62 (10) ◽  
pp. 1984-1988 ◽  
Author(s):  
C. M. Kearney ◽  
J. H. Wu

The β-1,3-glucan callose is thought to form a seal which surrounds viral local lesions and prevents viral spread in many plant hosts. Therefore, we investigated the role of host β-1,3-glucanase in facilitating viral spread. The following were compared for lesion size (indicating viral spread rate) and β-1,3-glucanase activity: (i) inoculated excised leaves of Phaseolus vulgaris L. cv. Pinto supplied with sugar (small lesions) or deprived of sugar (large lesions); (ii) Nicotiana glutinosa L. infected with the VM strain (small lesions) or the U1 strain (large lesions) of tobacco mosaic virus; and (iii) Nicotiana sylvestris Spegaz. infected with the VM strain (small lesions) or the U2 strain (large lesions) of tobacco mosaic virus. In all cases, the larger, more rapidly spreading viral lesions did not have significantly higher levels of β-1,3-glucanase activity than the corresponding smaller lesions. Nicotiana sylvestris leaves with a systemic viral infection had a β-1,3-glucanase activity lower than that of leaves with local lesions. Finally, β-1,3-glucanase activity was stimulated to the same extent by a slowly developing abiotic necrosis as by local lesions of tobacco mosaic virus, β-1,3-Glucanase activity may therefore increase during localized viral infection as a result of the wounding associated with necrotic viral lesions.


1986 ◽  
Vol 240 (3) ◽  
pp. 659-665 ◽  
Author(s):  
F Stirpe ◽  
L Barbieri ◽  
M G Battelli ◽  
A I Falasca ◽  
A Abbondanza ◽  
...  

Bryodin is a strongly basic (pI greater than or equal to 9.5) glycoprotein (neutral sugar content 6.3%) with Mr 30,000, purified from the roots of Bryonia dioica (white bryony). This protein inhibits protein synthesis by a rabbit reticulocyte lysate with and ID50 (concentration causing 50% inhibition) of 0.12 nM (3.6 ng/ml) and has much less effect on protein synthesis by whole cells, with ID50 values ranging from 46 nM to 2.27 microM (1.4-67 micrograms/ml). Bryodin acts by inactivating ribosomes, with a less-than-equimolar ratio, which suggests a catalytic action. Bryodin decreases the number of local lesions induced by tobacco mosaic virus in the leaves of Nicotiana glutinosa. From all its properties, bryodin can be considered to be a ribosome-inactivating protein, similar to those already known [reviews: Barbieri & Stirpe (1982) Cancer Surveys 1, 489-520; Stirpe & Barbieri (1986) FEBS Lett. 195, 1-8].


Blood ◽  
1976 ◽  
Vol 47 (1) ◽  
pp. 145-154 ◽  
Author(s):  
FJ Forte ◽  
HS Cohen ◽  
J Rosman ◽  
ML Freedman

Abstract Benzene (0.056–0.113 M) rapidly and reversibly inhibited protein synthesis in anucleate human sickle cell and rabbit reticulocytes. Hemin (50 muM) both prevented and reversed this effect of benzene. The inhibition in rabbit reticulocytes was accompanied by a conversion of polyribosomal disaggregation required ribosomal movement along mRNA and was also prevented and reversed by 50 muM hemin. Benzene was also shown to inhibit heme synthesis in rabbit reticulocytes while neither ATP nor GSH levels were altered. A translational repressor (HCR) of reticulocyte cell-free protein synthesis was isolated from intact cells incubated with benzene, while no significant amount of HCR was found in cells incubated with both benzene and hemin. These results indicated that benzene inhibits translation at the heme-dependent site of initiation. The clinical implications of these experiments remain to be elucidated.


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