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poliomyelitis/protease
Линкът е запазен в клипборда
Страница 1 от 27 резултата
[Insertional mutagenesis of protease 2A of the poliomyelitis virus and its substrate, simultaneously expressed in Escherichia coli cells].
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In order to clarify the structural features of protein substrates which determine their sensitivity towards poliovirus 2A protease, a high-efficiency bacterial expression system for cDNA of the poliovirus genome fragment has been developed. The expressed protein encompasses the C-end half of the VP1
Activator of plasminogen and protease from various cell cultures and present in poliomyelitis vaccine.
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beta-Galactosidase containing a human immunodeficiency virus protease cleavage site is cleaved and inactivated by human immunodeficiency virus protease.
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A "cleavage cassette" specifying a decapeptide human immunodeficiency virus (HIV) protease cleavage site was introduced into six different locations of beta-galactosidase (beta-D-galactoside galactohydrolase, EC 3.2.1.23) in Escherichia coli. Four of these constructs retained beta-galactosidase
Structure-Function Mutational Analysis and Prediction of the Potential Impact of High Risk Non-Synonymous Single-Nucleotide Polymorphism on Poliovirus 2A Protease Stability Using Comprehensive Informatics Approaches.
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Polio viral proteinase 2A performs several essential functions in genome replication. Its inhibition prevents viral replication, thus making it an excellent substrate for drug development. In this study, the three-dimensional structure of 2A protease was determined and optimized by homology
Newcastle Disease Virus-Based Vectored Vaccine against Poliomyelitis.
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The poliovirus eradication initiative has spawned global immunization infrastructure and dramatically decreased the prevalence of the disease, yet the original virus eradication goal has not been met. The suboptimal properties of the existing vaccines are among the major reasons why the program has
Interference with vaccinia virus growth caused by insertion of the coding sequence for poliovirus protease 2A.
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Attempts were made to express noninfectious derivatives of full-length type 1 (Mahoney) and type 2 (Lansing) poliovirus cDNAs in live recombinant vaccinia viruses for vaccine purposes. Vaccinia virus (VV) would not tolerate insertions of polio cDNA containing the coding sequence for the polio
Viral proteases: an emerging therapeutic target.
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Only a few viral diseases are presently treatable because of our limited knowledge of specific viral target molecules. An attractive class of viral molecules toward which chemotherapeutic agents could be aimed are proteases coded by some virus groups such as retro- or picornaviruses (poliomyelitis,
Anti-poliovirus activity of protease inhibitor AG-7404, and assessment of in vitro activity in combination with antiviral capsid inhibitor compounds.
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The National Research Council has recommended that at least one, preferably two, polio antiviral drugs be developed as a supplement to the tools currently available for control of polio outbreaks post-eradication. The primary application of such drugs is expected to be the resolution of chronic
Enteroviral proteases: structure, host interactions and pathogenicity.
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Enteroviruses are common human pathogens, and infections are particularly frequent in children. Severe infections can lead to a variety of diseases, including poliomyelitis, aseptic meningitis, myocarditis and neonatal sepsis. Enterovirus infections have also been implicated in asthmatic
[Cloning and expression of the 3C-proteinase gene from the poliomyelitis virus in E. coli cells].
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Expression of the 3C protease gene of poliovirus type 1 (Mahoney) in E. coli cells using various vectors was studied. The 3C gene was shown to be expressed effectively upon its cloning in HindII/HindII (bases 5240 to 6770) and in HindII/HindIII (bases 5240 to 6056) fragments of poliovirus cDNA in
Formation of poliomyelitis subviral particles in the yeast Saccharomyces cerevisiae.
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The sequence of the poliovirus genome encoding 3CD (a protease) was transferred to the yeast Saccharomyces cerevisiae on expression vectors with either a constitutive or an inducible promoter. Transformants could only be obtained with vectors carrying the inducible transcription unit. Extracts of
Immunogenic, non-infectious polio subviral particles synthesized in Saccharomyces cerevisiae.
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Polioviral genes coding for P1, the precursor for the structural proteins, and 3CD, the viral protease, were cloned in a Saccharomyces cerevisiae inducible expression system. N-antigenic empty capsids could be isolated from the yeast cell extract provided that pirodavir, a capsid-binding compound
[Isolation and purification of 3C-proteinase from the poliomyelitis virus. Identification of an active form of the enzyme].
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All the forms of 3C protease previously found were isolated and purified. A 3D polymerase's fragment covalently bound with 3C protein does not affect the specific proteolytic activity of the enzyme, whereas the elimination of 26 N-terminal amino acid residues of 3C protease leads to its
Picornavirus non-structural proteins as targets for new anti-virals with broad activity.
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Picornaviridae is one of the largest viral families and is composed of 14 genera, six of which include human pathogens. The best known picornaviruses are enteroviruses (including polio, PV, and rhinoviruses), foot-and-mouth disease virus (FMDV), and hepatitis A virus (HAV). Although infections often
Potent inhibition of enterovirus D68 and human rhinoviruses by dipeptidyl aldehydes and α-ketoamides.
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Enterovirus D68 (EV-D68) is an emerging pathogen responsible for mild to severe respiratory infections that occur mostly in infants, children and teenagers. EV-D68, one of more than 100 non-polio enteroviruses, is acid-labile and biologically similar to human rhinoviruses (HRV) (originally
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