[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/nucleeprotent-np-du-virus-of-the-grippe-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/nucleeprotent-np-du-virus-of-the-grippe-wikipedia\/","headline":"Nucleeprotent (NP) Du virus of the grippe \u2014 Wikipedia","name":"Nucleeprotent (NP) Du virus of the grippe \u2014 Wikipedia","description":"Nucleoprotein (NP) of the influenza virus is the major structural protein that interacts with the virus RNA segments to form,","datePublished":"2020-04-02","dateModified":"2020-04-02","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/44a4cee54c4c053e967fe3e7d054edd4?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/44a4cee54c4c053e967fe3e7d054edd4?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":100,"height":100},"url":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/nucleeprotent-np-du-virus-of-the-grippe-wikipedia\/","wordCount":2424,"articleBody":"Nucleoprotein (NP) of the influenza virus is the major structural protein that interacts with the virus RNA segments to form, with the Trimeric Polym\u00e9rase Arn, ribonucleoprotein (RNP). In addition, this protein is an important adapter that participates in the various interventions between the host cell and the virus.   Nucleoprotein is a protein of 56 KDA coded by segment 5 of the genome of the influenza virus. This segment is rich in arginine, glycine and serine. Despite the fact that nucleoprotein is mainly made up of basic amino acids, a region of the C-terminal portion includes around 30 acidic amino acids. The number of amino acids varies slightly from one type of influenza to another. As for type A influenza, nucleoprotein includes 498 amino acids, that of type B contains 560 and that of type C, 565. Also, these three proteins share homologous sequences but the latter are more pronounced between Type A and B viruses. From a three -dimensional angle, the structure of nucleoprotein is mainly composed of alpha propeller establishing an oligomer, each of which takes on a curved form having the appearance of a crescent. This structure is divided into two areas, one superior and the other lower. Polypeptides contributing to the composition of each of these areas are not structurally close to each other unlike the polypeptides in the fields of other RNA viruses which are rather colinar. This characteristic of influenza virus nucleoprotein gives it its uniqueness. As for the upper domain, two polypeptides, one encompassing amino acids 150 to 272 and the other amino acids 438 to 452, are involved in its organization. In a different way, the lower domain is assembled from three segments including residues 21 to 149, 273 to 396 and 453 to 489. In addition, nucleoprotein endorses a third domain, characterized in an exchange domain, which consists of a Flexible or flexible tod covering amino acids 402 to 428. This area with extensive conformation is made up of three beta sheets, two of which interact in order to create an intramolecular hair pin. Another characteristic of this structure is the presence of a furrow along the outside of the oligomer and located between the upper and lower domains of nucleoprotein. This cavity seems to accommodate RNA by interaction of its multiple basic amino acids with the latter’s phosphate skeleton. A considerable fraction of residues interacting with RNA is kept in the three types of influenza. (A, B and C) In terms of nucleoprotein amino acid sequence, different regions have been identified for which multiple macromolecules bind to it. A region located at the NH2 end approximately covers a third of the complete sequence of nucleoprotein and has the ability to link RNA. Two other areas (NP-1 and NP-2), which are included in about two-thirds of the protein, independent of each other, have the task of establishing interactions between nucleoprotein monomers. In addition, three fragments of the sequence of this protein (PB2-1, PB2-2 and PB2-3) come into an interaction individually with one of the monomers of the polymerase, PB2. The last 33 amino acids of the C-terminal end form the only region which does not have the function of linking a molecule but it rather consists in a repressor of the interaction between PB2 and NP and, of the interaction between NP monomers. Nucleoprotein sequence also includes important regions to link other molecules such as Actine, BAT1\/UAP56 and NLS 1 and 2. Influenza nucleoprotein interacts with many macromolecules as much viral and cellular origin. It is through these multiple interactions that this protein will be able to invest in the virus infection process. Viral [ modifier | Modifier and code ] NP-ARN [ modifier | Modifier and code ] The interaction of nucleoprotein with the single strand RNA of the virus contributes to the implementation of the ribonucleoproteic complex which gives the virus the ability to replicate. Several sequences of the protein are involved in this link but a particular region has confined to this purpose, the n-terminal portion. The latter includes amino acids 1 to 180 which can be subdivided into two parts which retain the link activity at RNA; A first containing residues 1 to 77 and a second containing amino acids 79 to 180. The second is the most important because its entire sequence links directly to RNA. Cooperation between RNA and nucleoprotein is the basis of electrostatic interactions of basic NP residues with the negatively charged phosphate skeleton. Also, contacts between amino acids from nucleoprotein and RNA nucleotides, especially pyrimidines, are present. Each nucleoprotein monomers interact with 24 viral RNA nucleotides (RNA). These reports are established on the external surface of nucleoprotein which means that the RNA is not protected from the digestion of ribonucleases. In addition, a particular characteristic of this protein is that it does not contain any of the canonical consensus reasons for fixing the RNA found in other RNA binding proteins. Np-np [ modifier | Modifier and code ] Homo-oligomerization of nucleoprotein is a necessity for the formation of ribonucleoproteic particles. This interaction between nucleoprotein monomers is mediated by the field of exchange. This area manages to establish various types of interactions such as intermoleculars establishing between hydrophobic \u03b2 sheets, hydrophobic interactions and salt bridges between protein monomers. The last nucleotides of the C-Terminal portion of nucleoprotein have inhibitory properties towards the oligomerization of this protein. NP-Polymerase [ modifier | Modifier and code ] This interaction with the Trimeric Polymerase is essential for the transition of transcription to the replication of viral RNA. Nucleoprotein is a anti -food factor linking to complementary RNA (ARNC) and RNA during the synthesis of RNPC and RNPV. The presence of a headdress on mRNA transcripts during their initiation will ensure that nucleoprotein will be unable to bond on them and thus they cannot be anti -sterminated. This highlights the need for coordination between cleavage of the cap at the 5 ‘end (produced by PB2) and the anti -centering of the end 3’ (produced by the NP) which are likely to occur According to the same mechanism. To get used to it, nucleoprotein can interact with PB2 through three regions independent of its sequence and also with PB1 which will modify the conformation of the P3 complex so that it goes from the transcription mode to the mode of replication. A single sub-unit of this complex has no contact with nucleoprotein, the PA. The split of the headdress made by the PB2 converts this sequence to start for the elongation of the channels, which is supervised by the PB1. The NP-PB2 interaction contains the instability which is caused by the 23 amino acids of the COOH end of nucleoprotein. NP-M1 [ modifier | Modifier and code ] The M1 viral matrix protein has two distinct areas connected through a flexible bond. A first amino-terminal area which includes the NLS (nuclear location signal) and which includes amino acids 1 to 164. The other area incorporates residues 165 to 252 and is located at the C-terminal end of the protein. Nucleoprotein fixed at the RNPV links to this last domain while the N-Terminal domain is reserved for NEP (nuclear export protein). The interaction between NP and matrix protein is essential for the progression of RNPV nuclear export. By clinging to the latter, she attributes the power to get out of the nucleus. On the other hand, the M1 is not linked to the RNPC replicative intermediaries, also present in the nucleus, which makes these ribonucleoproteic particles remain there. In addition, this protein maintains the RNPV in the cytoplasm for their incorporation into the viral assembly complex at the level of the plasma membrane thus avoiding their return to the nucleus. Cellular [ modifier | Modifier and code ] NP-IMPORTINE A [ modifier | Modifier and code ] Nucleoprotein interacts with the \u03b1 Import of the host cell through its nuclear location sequences (NLS). The NLS 1 is included in the n-terminal end including residues 3 to 13 and is the main sequence of \u03b1 import bond. Basic amino acids 7 and 8 of NLS 1 are preserved and are of great importance for importing into the nucleus of nucleoprotein alone as much as that of the whole viral ribonucleoproteic particle. The NLS 2, on the other hand, is a sequence shared in two parts between the amino acids 198 and 216. The latter is not as effective for the circulation of the NP to the nucleus. Np-actine [ modifier | Modifier and code ] At a later time during the infection, large quantities of nucleoprotein accumulate in the cytoplasm of the host cell due to an overload of the import route to the nucleus. A certain fraction of this imposing quantity of cytoplasmic nucleoprotein forms bonds with actin filaments. This interaction plays a considerable role in regulating the location of RNPs by keeping them in the cell cytoplasm. By going against the importation of RNPs, the NP-Actine complex collaborates in nuclear export in order to prevent the return of these ribonucleoproteic particles in the nucleus. NP-CRM 1 [ modifier | Modifier and code ] CRM 1, an exportine, is a cell receiver that links nuclear export (NES). By interacting with the nucleoprotein nes, CRM 1 is involved in the nuclear export route in order to expel the rnps from the nucleus. Without the help of this exportine, an accumulation of NP is remarkable at the nucleus. NP-BAT 1 \/ INPAP56 [ modifier | Modifier and code ] BAT 1\/UAP56 is a cellular splicing factor that belongs to the Dead-Box family of [ATPASE] SRN-dependent. It is a 48 KDA polypeptide included in the RAF-2, an activation factor of the Polym\u00e9rase RNA, as an active component of the latter. BAT 1\/UAP56 or RAF-2P48 binds to nucleoprotein via a set of 20 amino acids appearing on the n-terminal part of the protein. This complicity facilitates the generation of RNA-NP complexes but RAF-2P48 does not interact in any way with the complex. This factor acts only as a riding hood vis-\u00e0-vis nucleoprotein so that it comes into contact with RNA. The impossibility for Bat 1\/UAP56 to get in touch with the RNA-NP complex would be due to the proximity of everyone’s liaison sites on nucleoprotein. Fields N., Bernard; Knipe M., David; Howley M., Peter (1996), Fundamental Virology , 3 It is edition, Lippincott-Raven, \u00e9-U Ozama, Makoto et al.(2007, jan.), \u00abContributions of two nuclear localization signals of Influenza A virus nucleoprotein to viral replication\u00bb. Journal of Virology, Vol.81, No.1, p.30-41 Neumann, Gabriele; Castrucci R., Mary; Kawaoka, Yoshihiro (1997, D\u00e9c.), \u00abNUCLEAR IMPORT and Export of Influenza virus nucleoprotein\u00bb. Journal of Virology, Vol.71, No.12, p.9690-9 Digard, Paul; Elton, Debra; Bishop, Konrad (1999, mars), \u00abModulation of nuclear localization of the Influenza virus nucleoprotein through interaction with actin filaments\u00bb. Journal of Virology, Vol.73, No.3, p.2222-2231 Portela, Agustin; Digard, Paul (2002), \u00abThe Influenza virus nucleoprotein: a multifonctional RNA-binding protein pivotal to virus replication\u00bb. Journal of General Virology, p.723-734 Albo, Carmen; Valencia, Alfonso; Portela, Agustin (1995, Juin), \u00abidtification of an rning region within the N-Terminal Third of the Influenza virus nucleoprotein\u00bb. Journal of Virology, Vol.69, No.6, p.3799-3 Li, Zejun et al. (2009, mai), \u00abMutational Analysis of conserved amino acids in the Influenza A virus nucleoprotein\u00bb. Journal of Virology, Vol.83, No.9, p.4153-4162 Ye, Qiaozhen; Krug M., Robert; Tao, Yizhi Jane (2006, d\u00e9c.), \u00abThe mechanism by which Influenza A virus nucleoprotein forms oligomers and binds RNA\u00bb. Nature, p.1078-1082 Boulo, S\u00e9bastien (2008, Dec.), “Structural and functional studies of nucleoprotein and polymerase of the flu virus in association with their human nuclear carrier” Akarsu, H. et al. (2006), “Nucleocytoplasmic trafficking in proteins and ribonucleoproteins of the influenza virus”. 2006 virology, p.301-309 Biswas K., Siddhartha; Boutz L., Paul; Nayak P., Debi (1998, juil.), \u00abInfluenza virus nucleoprotein interact with Influenza virus polymerase proteins\u00bb. Journal of Virology, Vol.72, No.7, p.5493-5501 Elton, Debra et al. (2001, jan.), \u00abInteraction of the Influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway\u00bb. Journal of Virology, Vol.75, No.1, p.408-419 MOMOSE, Fumita et al. (2001, F\u00e9v.), \u00abCellular splicing factor RAF-2P48\/NPI-5\/BAT1\/BAT1\/UP56 Interacts with the Influenza Virus Nucleoprotein and Enhances Viral RNA Synthesis\u00bb. Journal of Virology, Vol.75, No.4, p.1899-1 "},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/nucleeprotent-np-du-virus-of-the-grippe-wikipedia\/#breadcrumbitem","name":"Nucleeprotent (NP) Du virus of the grippe \u2014 Wikipedia"}}]}]