Virus nucleoprotein

Baltimore D (1988) Gene therapy. Intracellular immunization. Nature 335 395-396 Basta S, Stoessel R, Easier M, van den Broek M, Groettrup M (2005) Cross-presentation of the long-lived lymphocytic choriomeningitis virus nucleoprotein does not require neosynthesis and is enhanced via heat shock proteins. J Immunol 175 796-805 Baum C (2007) Insertional mutagenesis in gene therapy and stem cell biology. Curr Opin Hematol 14 337-342... 

In the past, dissociation of the nucleoprotein complex has been brought about by salt solutions or by heat denaturation,129 but, more recently, decomposition has been effected by hydrolysis with trypsin,126 or by the use of dodecyl sodium sulfate130 or strontium nitrate.131 Some virus nucleoproteins are decomposed by ethyl alcohol.132 This effect may be similar to that of alcohol on the ribonucleoproteins of mammalian tissues. If minced liver is denatured with alcohol, and the dried tissue powder is extracted with 10% sodium chloride, the ribonucleoproteins are decomposed to give a soluble sodium ribonucleate while the deoxyribonucleoproteins are unaffected.133 On the other hand, extraction with 10 % sodium chloride is not satisfactory unless the proteins have first been denatured with alcohol. Denaturation also serves to inactivate enzymes of the tissues which might otherwise bring about degradation of the nucleic acid during extraction. 

The spectrophotometric evidence reviewed above for the binding of a proportion of the phenolic hydroxyl groups of the tyrosine residues of native proteins is supported by work on the action of tyrosinase on proteins. Sizer (1946) found that this enzyme oxidizes the tyrosine residues in native trypsin, pepsin, chymotrypsin, casein, peptone, insulin, and hemoglobin. Native ovalbumin, human and bovine serum albumin, tobacco mosaic virus (nucleoprotein), human y- and bovine /3-globulins, and bovine fibrinogen are not susceptible to tyrosinase, but become so after tryptic digestion. It was shown (Sizer, 1947) that for the proteins which are oxidized by tyrosinase in the native state, the observed reaction does indeed occur with the intact proteins and does not require preliminary degradation to tyrosine peptides or free tyrosine. The kinetics of the oxidation of tyrosine by tyrosinase have been studied spectropho-tometrically (Mason, 1948 etc.). 

Anthony L S, Wu H, Sweet H, et al. (1999). Priming of CD8-H CTL effector ceils in mice by immunization with a stress protein-influenza virus nucleoprotein fusion molecule. Vaccine. 17 373-383. 

Several IDPs have already been subjected to SDSL EPR investigations. So EPR data showed decreased flexibility in a region of residual helical structure in the disordered C-terminal domain of the measles virus nucleoprotein, and demonstrated the further ordering of this region upon interaction with a binding partner [119, 120]. 

The ability of clay minerals to adsorb viruses (nucleoproteins) in a similar way to proteins (Theng, 1979) can be put to various beneficial uses as well. 

Structure determination of a Galectin-3-carbohydrate complex. Conformational analysis of partially folded proteins illustrated by application to the molecular recognition element of Sendai virus nucleoprotein. ... 

M. R. Jensen, P. Bernado, R. W. H. Ruigrok and M. Blackledge, Structural Disorder within Sendai Virus Nucleoprotein and Phosphoprotein, in Flexible Viruses Structural Disorder in Viral Proteins, ed. V. N. Uversky and S. Longhi, John Wiley Sons, Inc., Hoboken, N.J., 2012, p. 95. 

Nucleoproieins. The prosthetic group of the nucleoproteins is nucleic acid, often linked through salt linkages with protamines or histones. The nucleoproteins are present in the nuclei of all cells. Chromasomes are largely nucleoproteins and some plant viruses and bacteriophages have been shown to be pure nucleoproteins. See also histones. 

NUCLEOPROTEINS. Nucleoprotein conjugates have many roles in the storage and transmission of genetic information. Ribosomes are the sites of protein synthesis. Virus particles and even chromosomes are protein-nucleic acid complexes. 

In addition to small organic molecules or metal ions, proteins may have other components tightly associated with them. Nucleoproteins, for instance, contain noncovalently bound DNA or RNA, as in some of the structural proteins of viruses. Lipoproteins contain associated lipids or fatty acids and may also carry cholesterol, as in the high-density and low-density lipoproteins in serum. 

Yusibov et al. [71] delivered to 14 human volunteers spinach expressing epitopes from the rabies virus glycoprotein and nucleoprotein fused to the coat protein of alfalfa mosaic virus (AlMV). Five of the fourteen subjects had previously received a... 

Viruses are parasitic nucleoprotein complexes. They often consist of only a single nucleic acid molecule (DNA or RNA, never both) and a protein coat. Viruses have no metabolism of their own, and can therefore only replicate themselves with the help of host cells. They are therefore not regarded as independent organisms. Viruses that damage the host cell when they replicate are pathogens. Diseases caused by viruses include AIDS, rabies, poliomyelitis, measles, German measles, smallpox, influenza, and the common cold. 

Virases are much simpler organisms than bacteria, and they are made from protein substances and nucleic acid. A single nucleoprotein molecule formed from molecules of nucleic acid that are chemically bound to a bulky protein molecule can be considered a simple viral particle. The protein molecule plays the role of a protective membrane. Thus the virus can be schematically described as a nucleic acid insert that is protected by a protein covering. A virus can contain either ribonucleic acid or deoxyribonucleic acid, but it never contains both of them together. The type of nucleic acid is the basis of one of the classifications of viruses. Viruses are obligatory intracellular parasites, which, upon entering a cell (i.e. after being infected) use many biochemical systems of the host cell. 

Heaphy, S., Finch, IT., Gait, M.J., Karn, J. and Singh, M. Human Immunodefidency virus type-1 regulator of virion expression, rev, forms nucleoprotein filaments after binding to a purine-rich bubble located within the rev responsive element (1991) Proc. Natl. Acad. Sd. U.S.A. 88,... 

A schematic diagram of an influenza virus particle that illustrates its constituent components and morphology. The surface antigens hemagglutinin and neuraminidase are attached to the lipid and matrix protein shell that encapsulates the eight negative-stranded RNA genes of the virus and associated nucleoprotein and polymerase. 

II A radically different type of nucleoprotein is that provided by the smaller RNA viruses of the elongated spiral type like tobacco mosaic, or of the polyhedral type such as tomato bushy stunt, tipula virus or poliomyelitis virus. The only one of these adequately studied has been tobacco mosaic virus, Franklin [19, 20], and here it appears that the protein and not the nucleic acid determines the structure. There is only one RNA chain and this is wound helically so that one protein is in contact with three successive nucleotides. 

DNA is a polydeoxyribonucleotide that contains many monodeoxy-ribonucleotides covalently linked by 3 ->5 -phosphodiester bonds. With the exception of a few viruses that contain single-stranded DNA, DNA exists as a double-stranded molecule, in which the two strands wind around each other, forming a double helix. In eukaryotic cells, DNA is found associated with various types of proteins (known collectively as nucleoprotein) present in the nucleus, whereas in prokaryotes, the protein-DNA complex is present in the nucleoid. 

NUCLEOPROTEINS AND NUCLEIC ACIDS. Nucleic adds are compounds in which phosphoric acid is combined with carbohydrates and with bases derived from purine and pyrimidine. Nucleoproteins are conjugated proteins consisting of a protein moiety and a nucleic acid. Originally, nucleoproteins were thought to occur only in the nuclei of cells, but it was later established that they are far more widely distributed, being found in cells of all types, animal and plant. They are found in the chromosomes, in the genes, in viruses, and bacteriophages. 

Plasmid. A circular DNA duplex that replicates autonomously in bacteria. Plasmids that integrate into the host genome are called episomes. Plasmids differ from viruses in that they never form infectious nucleoprotein particles. 

Ulmer JB, Fu TM, Deck RR, Friedman A, Guan L, DeWitt C, Liu X, Wang S, Liu MA, Donnelly JJ, Caulfield MJ (1998), Protective CD4+ and CD8+ T cells against influenza virus induced by vaccination with nucleoprotein DNA, J. Virol. 72 5648-5653. 

The nucleocapsids are envelopes that contain a nucleoprotein in the center, which transports the viral DNA to the cell nucleus. After replication, new copies of the viral genome are encapsulated in the nucleus, creating new nucleocapsids. The nucleocapsids then migrate to the cytoplasm and leave the cell by a budding process. In this process, the nucleocapsids become enveloped by the acquisition of the host cell plasma membrane. The resulting virions are extracellular (budded virus, BV) and these constitute the main products of the first stage of the infection process in the caterpillar, known as primary infection. 

Similarly, significantly higher humoral responses were obtained after s.c. administration of either a lipid and/or a nonionic-based vesicle-entrapped plasmid for the nucleoprotein of H3N2 influenza virus in comparison to the naked DNA alone [226],... 

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