THE BIOCHEMICAL AND PHYSIOLOGICAL CHARACTERIZATION OF POLIOVIRUS MUTANTS (TEMPERATURE-SENSITIVE, IN SITU LYSIS, GUANIDINE RESISTANT, MUTATIONS).

Persistent Link:
http://hdl.handle.net/10150/187872
Title:
THE BIOCHEMICAL AND PHYSIOLOGICAL CHARACTERIZATION OF POLIOVIRUS MUTANTS (TEMPERATURE-SENSITIVE, IN SITU LYSIS, GUANIDINE RESISTANT, MUTATIONS).
Author:
ANTINORO, NORLA MARIE WALSER.
Issue Date:
1984
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
Poliovirus is a small, structurally simple virus that can serve as a powerful model system for the elucidation of the basic processes involved in the genetic control of macromolecular synthesis. The physical and biochemical characterization of temperature-sensitive and drug-resistant mutants of this virus can provide insight into the normal sequence of events during the replication and assembly of the wild-type (wt) virus. The specific interference of the infecting virus with the major pathways of macromolecular synthesis in the host cell offers a possible inroad to the exploration of the relevant control systems. This research is divided into two major segments: (1) a temperature-sensitive mutant of poliovirus type 1, tsB9, and a guanidine-resistant mutant, gʳH, were characterized physiologically; (2) a physiological screening procedure that quickly and efficiently reveals the phenotype of a large number of poliovirus mutants in a short period of time was developed and validated. Two guanidine-resistant and twelve temperature-sensitive mutants of poliovirus type 1, Mahoney, were generated and compared with wt, defective-interfering particles, gʳH, and tsB9 using the screening procedure herein developed. The temperature-sensitive mutant, tsB9, appears to be a structural protein mutant bearing a related defect in ribonucleic acid synthesis at the restrictive temperature. The mutant gʳH was found to differ from the wt virus only in the guanidine resistance of its growth and ribonucleic acid synthesis, although a detailed electrophoretic analysis of its proteins was not done. Among the newly isolated mutants, strains were found with defects in each of the major viral functions except one. No mutant was found to be defective in the ability to inhibit host-cell protein synthesis. The screening procedure developed met all of the criteria set for it mentioned above. It has the potential of being adapted to many virus-cell systems for the rapid determination of mutant phenotype.
Type:
text; Dissertation-Reproduction (electronic)
Keywords:
Poliovirus -- Genetics.; Viral genetics.
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Molecular and Cellular Biology; Graduate College
Degree Grantor:
University of Arizona

Full metadata record

DC FieldValue Language
dc.language.isoenen_US
dc.titleTHE BIOCHEMICAL AND PHYSIOLOGICAL CHARACTERIZATION OF POLIOVIRUS MUTANTS (TEMPERATURE-SENSITIVE, IN SITU LYSIS, GUANIDINE RESISTANT, MUTATIONS).en_US
dc.creatorANTINORO, NORLA MARIE WALSER.en_US
dc.contributor.authorANTINORO, NORLA MARIE WALSER.en_US
dc.date.issued1984en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractPoliovirus is a small, structurally simple virus that can serve as a powerful model system for the elucidation of the basic processes involved in the genetic control of macromolecular synthesis. The physical and biochemical characterization of temperature-sensitive and drug-resistant mutants of this virus can provide insight into the normal sequence of events during the replication and assembly of the wild-type (wt) virus. The specific interference of the infecting virus with the major pathways of macromolecular synthesis in the host cell offers a possible inroad to the exploration of the relevant control systems. This research is divided into two major segments: (1) a temperature-sensitive mutant of poliovirus type 1, tsB9, and a guanidine-resistant mutant, gʳH, were characterized physiologically; (2) a physiological screening procedure that quickly and efficiently reveals the phenotype of a large number of poliovirus mutants in a short period of time was developed and validated. Two guanidine-resistant and twelve temperature-sensitive mutants of poliovirus type 1, Mahoney, were generated and compared with wt, defective-interfering particles, gʳH, and tsB9 using the screening procedure herein developed. The temperature-sensitive mutant, tsB9, appears to be a structural protein mutant bearing a related defect in ribonucleic acid synthesis at the restrictive temperature. The mutant gʳH was found to differ from the wt virus only in the guanidine resistance of its growth and ribonucleic acid synthesis, although a detailed electrophoretic analysis of its proteins was not done. Among the newly isolated mutants, strains were found with defects in each of the major viral functions except one. No mutant was found to be defective in the ability to inhibit host-cell protein synthesis. The screening procedure developed met all of the criteria set for it mentioned above. It has the potential of being adapted to many virus-cell systems for the rapid determination of mutant phenotype.en_US
dc.typetexten_US
dc.typeDissertation-Reproduction (electronic)en_US
dc.subjectPoliovirus -- Genetics.en_US
dc.subjectViral genetics.en_US
thesis.degree.namePh.D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.disciplineMolecular and Cellular Biologyen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.identifier.proquest8505220en_US
dc.identifier.oclc693584918en_US
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