THE CHARACTERIZATION OF FOOT-AND-MOUTH DISEASE VIRUS-RNA DEPENDENT RNA POLYMERASE AND ITS LOCALIZATION IN INFECTED CELL CULTURE AND ANIMAL TISSUE.
Item
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Title
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THE CHARACTERIZATION OF FOOT-AND-MOUTH DISEASE VIRUS-RNA DEPENDENT RNA POLYMERASE AND ITS LOCALIZATION IN INFECTED CELL CULTURE AND ANIMAL TISSUE.
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Identifier
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AAI8212222
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identifier
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8212222
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Creator
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WOOL, STEVEN HARRIS.
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Contributor
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Jules Golubow
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Date
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1982
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Language
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English
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Publisher
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City University of New York.
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Subject
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Chemistry, Biochemistry
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Abstract
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Foot-and-mouth disease virus is a single stranded RNA virus which is known to be replicated by a viral-induced RNA polymerase. In this thesis, the RNA polymerase is shown to be composed of one viral and four host cell polypeptides. In addition, it is shown that the sera from convalescent animals contain an antibody against the viral induced polymerase component. These sera are made specific for this viral polypeptide by adsorbing out the antibody against the viral capsid polypeptides.;The use of this antisera in an electron microscopic immunolabeling procedure shows the presence of the viral polymerase polypeptide (P-56) in the lumen of the rough endoplasmic reticulum (RER), in the Golgi and within and on the surface of smooth membranous vacuoles. The latter structures which are shown to be induced during the infectious process are also shown by EM autoradiography to be the site of polymerase activity. The results of these studies suggest a theory for the synthesis, processing and maturation of the polymerase which resembles the processing for secretory proteins which are synthesized on the RER, processed through the Golgi and sequestered into Golgi vacuoles.;Lastly, these studies were extended into animal tissue so that the process could be confirmed in infected whole animals. Mammary, liver and skin tissues were examined from infected animals. Smooth membranous vacuoles in the liver were found in numbers greater than in control tissue. Both mammary and liver tissue showed that the immunolabeling for the P-56 polymerase polypeptide was associated with smooth membranous vacuoles. In the case of the mammary, the vacuoles were of definite Golgi origin since they contained milk secretory proteins known to be Golgi products.;This thesis, therefore, demonstrates that the P-56 polymerase polypeptide is made on the rough endoplasmic reticulum, processed through the Golgi and inserted into the vacuolar membrane where it combines with host proteins and becomes the active polymerase complex.
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Type
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dissertation
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Source
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PQT Legacy CUNY.xlsx
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degree
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Ph.D.
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Program
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Biochemistry
