scholarly journals SOME EFFECTS OF IODINE AND OTHER REAGENTS ON THE STRUCTURE AND ACTIVITY OF TOBACCO MOSAIC VIRUS

1941 ◽  
Vol 24 (6) ◽  
pp. 679-690 ◽  
Author(s):  
M. L. Anson ◽  
W. M. Stanley
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Guanidine Hydrochloride ◽  
Urea Solution ◽  
Nicotiana Glutinosa ◽  
Native Form ◽  
Tobacco Plants ◽  
Sh Groups ◽  
Normal Number ◽  
Acid Reagent

1. Denatured tobacco mosaic virus has a number of SH groups corresponding to its total sulfur content of 0.2 per cent. The SH groups were estimated by titration with ferricyanide, tetrathionate, and p-chloromercuribenzoate in guanidine hydrochloride solution and by reduction of the uric acid reagent in urea solution. 2. The SH groups of tobacco mosaic virus or their precursors can be abolished by reaction of the native form of the virus with iodine. 3. Tobacco mosaic virus whose SH groups have been oxidized beyond the S-S stage by iodine but whose tyrosine groups have not been converted into di-iodotyrosine groups still retains its normal biological activity as shown by the number of lesions it causes on Nicotiana glutinosa plants and by the characteristic disease produced in Turkish tobacco plants. 4. The inoculation of Turkish tobacco plants with active virus whose SH groups have been abolished by iodine results in the production of virus with the normal number of SH groups. 5. If enough iodine is added to tobacco mosaic virus or if the iodine reaction is carried out at a sufficiently high temperature, then the tyrosine groups are converted into di-iodotyrosine groups and the virus is inactivated. 6. Tobacco mosaic virus can be almost completely inactivated by iodoacetamide under conditions under which iodoacetamide reacts with few if any of the protein's SH groups. 7. Tobacco mosaic virus is not inactivated by dilute p-chloromercuribenzoate.

scholarly journals THE SULFHYDRYL GROUPS OF EGG ALBUMIN

1941 ◽  
Vol 24 (4) ◽  
pp. 399-421 ◽  
Author(s):  
M. L. Anson
Keyword(s):  
Guanidine Hydrochloride ◽  
Sulfhydryl Groups ◽  
Urea Solution ◽  
Ferricyanide Reduction ◽  
Native Form ◽  
Egg Albumin ◽  
Sh Groups ◽  
Reduction Test ◽  
Hydrochloride Solution

1. 1 cc. of 0.001 M ferricyanide, tetrathionate, or p-chloromercuribenzoate is required to abolish the SH groups of 10 mg. of denatured egg albumin in guanidine hydrochloride or Duponol PC solution. Both the nitroprusside test and the ferricyanide reduction test are used to show that the SH groups have been abolished. 2. 1 cc. of 0.001 M ferrocyanide is formed when ferricyanide is added to 10 mg. of denatured egg albumin in neutral guanidine hydrochloride or urea solution. The amount of ferricyanide reduced to ferrocyanide by the SH groups of the denatured egg albumin is, within wide limits, independent of the ferricyanide concentration. 3. Ferricyanide and p-chloromercuribenzoate react more rapidly than tetrathionate with the SH groups of denatured egg albumin in both guanidine hydrochloride solution and in Duponol PC solution. 4. Cyanide inhibits the oxidation of the SH groups of denatured egg albumin by ferricyanide. 5. Some samples of guanidine hydrochloride contain impurities which bring about the abolition of SH groups of denatured egg albumin and so interfere with the SH titration and the nitroprusside test. This interference can be diminished by using especially purified guanidine hydrochloride, adding the titrating agent before the protein has been allowed to stand in guanidine hydrochloride solution, and carrying out the nitroprusside test in the presence of a small amount of cyanide. 6. The SH groups of egg albumin can be abolished by reaction of the native form of the protein with iodine. It is possible to oxidize all the SH groups with iodine without oxidizing many of the SH groups beyond the S-S stage and without converting many tyrosine groups into di-iodotyrosine groups. 7. p-chloromercuribenzoate combines with native egg albumin either not at all or much more loosely than it combines with the SH groups of denatured egg albumin or of cysteine. 8. The compound of mercuribenzoate and SH, like the compound of aldehyde and SH and like the SH in native egg albumin, does not give a nitroprusside test or reduce ferricyanide but does reduce iodine.

scholarly journals THE REACTIONS OF IODINE AND IODOACETAMIDE WITH NATIVE EGG ALBUMIN

1940 ◽  
Vol 23 (3) ◽  
pp. 321-331 ◽  
Author(s):  
M. L. Anson
Keyword(s):  
Amino Acids ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Reducing Power ◽  
Experimental Results ◽  
Ferricyanide Reduction ◽  
Native Form ◽  
Egg Albumin ◽  
Sh Groups ◽  
Sh Group

The following experimental results have been obtained. 1. Native egg albumin treated with iodine and then denatured no longer gives a nitroprusside test or reduces dilute ferricyanide in neutral Duponol PC solution. 2. More iodine is needed to abolish the ferricyanide reduction if the reaction between native egg albumin and iodine is carried out at pH 6.8 than if the reaction is carried out at pH 3.2. At pH 6.8 iodine reacts with tyrosine as well as with cysteine. 3. Cysteine and tryptophane are the only amino acids with reducing groups which are known to react with dilute iodine at pH 3.2 The reducing power of cysteine is abolished by the reaction with iodine, whereas the reducing power of tryptophane remains intact. Pepsin and chymotrypsinogen which contain tryptophane but not cysteine, do not react at all with dilute iodine at pH 3.2. 4. Native egg albumin treated with iodoacetamide at pH 9.0 and then denatured by Duponol PC reduces only 60 per cent as much dilute ferricyanide as egg albumin which has not been treated with iodoacetamide. 5. The SH group is the only protein reducing group which is known to react with iodoacetamide. The simplest explanation of the new observation that the SH groups of egg albumin can be modified by reactions with the native form of the protein is that the native egg albumin has free and accessible but relatively unreactive SH groups which can react with iodine and iodoacetamide despite the fact that they do not react with ferricyanide, porphyrindin, or nitroprusside. Preliminary experiments suggested by the results with egg albumin indicate that the tobacco mosaic virus is modified by iodine at pH 2.8 without being inactivated and that the tobacco mosaic and rabbit papilloma viruses are not inactivated by iodoacetamide at pH 8.0.

scholarly journals Novel N Gene-Associated, Temperature-Independent Resistance to the Movement of Tobacco Mosaic Virus Vectors Neutralized by a Cucumber Mosaic Virus RNA1 Transgene

2002 ◽  
Vol 76 (24) ◽  
pp. 12908-12916 ◽  
Author(s):  
Tomas Canto ◽  
Peter Palukaitis
Keyword(s):  
Salicylic Acid ◽  
Green Fluorescent Protein ◽  
Tobacco Mosaic Virus ◽  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Fluorescent Protein ◽  
N Gene ◽  
Nicotiana Glutinosa ◽  
Tobacco Plants ◽  
Green Fluorescent

ABSTRACT The N gene conditions for resistance to Tobacco mosaic virus (TMV) but only below 28°C. However, a TMV-based vector expressing green fluorescent protein (TMV-GFP) showed only limited movement at 33°C in tobacco plants harboring the N gene and other genes cointrogressed from Nicotiana glutinosa. TMV-GFP moved efficiently in tobacco plants that either lacked these genes or that contained the N gene but were transgenic for RNA1 of Cucumber mosaic virus. These findings identified novel temperature-independent resistance to the movement of TMV-GFP which could be neutralized by a different viral transgene. Using the N gene and nahG gene-transgenic tobacco, we show that this novel resistance is manifested specifically by the N gene itself and operates via a pathway independent of salicylic acid.

THE INHIBITING EFFECT OF SOME HETEROCYCLIC AND OTHER ORGANIC COMPOUNDS ON TOBACCO MOSAIC VIRUS

1955 ◽  
Vol 1 (7) ◽  
pp. 549-559 ◽  
Author(s):  
M. Weintraub ◽  
W. G. Kemp
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Organic Compounds ◽  
Virus Multiplication ◽  
Nicotiana Glutinosa ◽  
Inhibiting Effect ◽  
Mechanism Of Inhibition ◽  
Virus Content ◽  
Rate Of Oxygen Consumption ◽  
Main Effects

A number of heterocyclic and miscellaneous organic compounds have been tested for their effectiveness as virus inhibitors by a half-leaf technique using Nicotiana glutinosa and tobacco mosaic virus. Several of these compounds were found to be effective in varying degrees, the main effects being a reduction in the total number of lesions produced, a delay in symptom expression, and a decrease in virus multiplication as indicated by small lesions, on the treated half-leaves. Although nothing is known about the mechanism of inhibition, it can be concluded that to effect inhibition compounds act through the physiology of the host, rather than directly on the virus. The virus content of treated half-leaves has been estimated by measuring their rate of oxygen consumption. These data indicate that the inhibiting compounds affect the metabolism of the host, as reflected in a change in respiration when compared to control half-leaves, and that the symptomless areas on the treated half-leaves do not contain significant concentrations of virus.

scholarly journals Inhibitory Effect of Osthole from Cnidium monnieri on Tobacco Mosaic Virus (TMV) Infection in Nicotiana glutinosa

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 65 ◽  
Author(s):  
Ya-Han Chen ◽  
Dong-Sheng Guo ◽  
Mei-Huan Lu ◽  
Jian-Ying Yue ◽  
Yan Liu ◽  
...  
Keyword(s):  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Plant Virus ◽  
Inhibitory Effect ◽  
Nicotiana Glutinosa ◽  
1H And 13C Nmr ◽  
Virus Activity ◽  
Viral Particles ◽  
Coumarin Compound

The coumarin compound of osthole was extracted from Cnidium monnieri and identified by LC-MS and 1H- and 13C-NMR. Osthole was tested for anti-virus activity against tobacco mosaic virus (TMV) using the half-leaf method. The results showed that stronger antiviral activity on TMV infection appeared in Nicotiana glutinosa than that of eugenol and ningnanmycin, with inhibitory, protective, and curative effects of 72.57%, 70.26%, and 61.97%, respectively. Through observation of the TMV particles, we found that osthole could directly affect the viral particles. Correspondingly, the level of coat protein detected by Western blot was significantly reduced when the concentrations of osthole increased in tested plants compared to that of the control. These results suggest that osthole has anti-TMV activity and may be used as a biological reagent to control the plant virus in the half-leaf method.

scholarly journals Effect of Yeast CTA1 Gene Expression on Response of Tobacco Plants to Tobacco Mosaic Virus Infection

2002 ◽  
Vol 129 (3) ◽  
pp. 1032-1044 ◽  
Author(s):  
Andrzej Talarczyk ◽  
Magdalena Krzymowska ◽  
Wojciech Borucki ◽  
Jacek Hennig
Keyword(s):  
Gene Expression ◽  
Virus Infection ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Tobacco Plants ◽  
Tobacco Mosaic Virus Infection ◽  
Mosaic Virus Infection
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