Information om | Engelska ordet NUCLEOCAPSID

Exempel på hur man kan använda NUCLEOCAPSID i en mening

• At the core is a single helical strand of genomic RNA tightly bound to N (nucleocapsid) protein and associated with the L (large) and P (phosphoprotein) proteins, which provide RNA polymerase activity during replication.
• The matrix protein (M) constitutes a layer between the virion envelope and the nucleocapsid core of the rhabdovirus.
• Adenoviruses (members of the family Adenoviridae) are medium-sized (90–100 nm), nonenveloped (without an outer lipid bilayer) viruses with an icosahedral nucleocapsid containing a double-stranded DNA genome.
• While alphavirus virions are spherical and contain an icosahedral nucleocapsid, RuV virions are pleiomorphic and do not contain icosahedral nucleocapsids.
• Viral genome codes for five polypeptides, namely, nucleocapsid protein N, phosphoprotein P, matrix protein M, glycoprotein G and large protein L in five monocistronic mRNAs.
• The nucleocapsid consists of 15 conspicuous vertical helices located along the long axis; each helix has two parallel striations, composed of 14 globular capsomers, each of which is 8 nm in diameter.
• Alphavirus particles are enveloped, have a 70 nm diameter, tend to be spherical (although slightly pleomorphic), and have a 40 nm isometric nucleocapsid.
• The influenza B virus capsid is enveloped while its virion consists of an envelope, a matrix protein, a nucleoprotein complex, a nucleocapsid, and a polymerase complex.
• The muralytic (peptidoglycan-digesting) enzyme, P5, then digests a portion of the cell wall, and the nucleocapsid enters the cell coated with the bacterial outer membrane.
• The virion is non-enveloped with a flexuous and filamentous nucleocapsid, 680 to 900 nanometers (nm) long and is 11–20 nm in diameter.
• As Type C retroviruses, replicating murine leukemia viruses produce a virion containing a spherical nucleocapsid (the viral genome in complex with viral proteins) surrounded by a lipid bilayer derived from the host cell membrane.
• The retroviral genome is coated by a viral nucleocapsid protein that may function like a single stranded binding protein and therefore enhances processivity and facilitates template exchanges.
• The structure of the virions is consistent with that of others in the poxvirus family: they are composed of a nucleocapsid, core envelope, lateral body, and an extracellular envelope.
• The virion essentially is a nucleocapsid that is visible under an electron microscope and is able to infect cultured cells from a broad range of mammals including rabbit kidney (RK13), African green monkey kidney (Vero), equine foetal kidney (EFK), and is able to infect humans.
• A viral tegument or tegument, more commonly known as a viral matrix, is a cluster of proteins that lines the space between the envelope and nucleocapsid of all herpesviruses.
• The L RNA segment encodes an RNA-dependent RNA polymerase (L protein), the M RNA segment encodes two surface glycoproteins (Gc and Gn) and a nonstructural protein (NSm), while the S RNA segment encodes a nucleocapsid protein (N) and, in an alternative overlapping reading frame, a second nonstructural protein (NSs).
• Viral entry to the CD4+ cell begins with attachment of the R5 HIV-1 glycoprotein 120 (gp120) to the CD4+ T-cell receptor, which produces a conformational change in gp120 and allows it to bind to CCR5, thereby triggering glycoprotein 41 (gp41) mediated fusion of the viral envelope with the cell membrane and the nucleocapsid enters the host cell (Figure 1).
• The L RNA segment encodes an RNA-dependent RNA polymerase (L protein), the M RNA segment encodes two surface glycoproteins (Gc and Gn) and a nonstructural protein (NSm), while the S RNA segment encodes a nucleocapsid protein (N) and, in an alternative overlapping reading frame, a second nonstructural protein (NSs).
• Gag encodes group-specific antigen (nucleocapsid proteins), Pro for protease, Pol responsible for RNA-dependent DNA polymerase (reverse-transcriptase) region & integrase, and Env encodes the envelope glycoprotein for virion peplomer proteins.
• The RNA-dependent RNA polymerase, glycoprotein precursor, nucleocapsid, and P4 proteins of WMoV exhibited limited sequence homology with the orthologous proteins of other emaraviruses, while proteins encoded by additional genomic RNA segments displayed no significant homology with proteins reported in GenBank, suggesting that the genus Emaravirus evolved further with a divergent octapartite genome.

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