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Matrix associated RNP pre-assembly complex
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Glycosylated, palmitylated and folded HA trimer
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In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
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pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus
The influenza A virus M2 cytoplasmic tail is required for infectious virus production and efficient genome packaging
Functional analysis of PA binding by influenza a virus PB1: effects on polymerase activity and viral infectivity
SUBUNIT Influenza RNA polymerase is composed of three subunits: PB1, PB2 and PA.SIMILARITY Belongs to the influenza viruses PB2 family.
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HA folded, glycosylated, and palmitylated
Involvement of hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits
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Escaping from the cell: assembly and budding of negative-strand RNA viruses
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Nuclear location of all three influenza polymerase proteins and a nuclear signal in polymerase PB2
Total chemical synthesis of the integral membrane protein influenza A virus M2: role of its C-terminal domain in tetramer assembly
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Dissecting the role of the golgi complex and lipid rafts in biosynthetic transport of cholesterol to the cell surface
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The PA subunit is required for efficient nuclear accumulation of the PB1 subunit of the influenza A virus RNA polymerase complex
FUNCTION Implicated in endonuclease cleavage of capped RNA primers. Displays an elongation factor activity in viral RNA synthesis. Dispensable for viral transcription, but not replication.SUBUNIT Influenza RNA polymerase is composed of three subunits: PB1, PB2 and PA.SIMILARITY Belongs to the influenza viruses PA family.
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FUNCTION RNA-dependent RNA polymerase which is responsible for replication and transcription of virus segments. Binds the promoter sequence of the encapsidated viral RNA. Displays an endonuclease activity involved in cap-stealing. Cleaves cellular pre-mRNA to generate primers for viral transcription.CATALYTIC ACTIVITY Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).SUBUNIT Influenza RNA polymerase is composed of three subunits: PB1, PB2 and PA.SIMILARITY Belongs to the influenza viruses polymerase PB1 family.SIMILARITY Contains 1 RdRp catalytic domain.
Glycosylated, palmitylated and folded HA trimer:Lipid Raft Complex
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FUNCTION Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.CATALYTIC ACTIVITY Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.ENZYME REGULATION Inhibited by the neuraminidase inhibitors zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs interfere with the release of progeny virus from infected cells and are effective against all influenza strains. Resistance to neuraminidase inhibitors is quite rare.MISCELLANEOUS The influenza A genome consist of 8 RNA segments. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains. The mechanism of variation can be the result of point mutations or the result of genetic reassortment between segments of two different strains.SIMILARITY Belongs to the glycosyl hydrolase 34 family.
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FUNCTION Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals and is responsible of the active RNP import into the nucleus through the cellular importin alpha/beta pathway. Later in the infection, nucleus export of RNP are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that the nucleoprotein binds directly exportin-1 (XPO1) and plays an active role in RNP nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmask nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.SIMILARITY Belongs to the influenza viruses nucleoprotein family.
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ENZYME REGULATION The M2 protein from most influenza A strains is inhibited by amantadine and rimantadine, resulting in viral uncoating incapacity. Emergence of amantadine-resistant variants is usually rapid.MISCELLANEOUS When the channel is activated, one or more imidazole moities of His-37 probably become bi-protonated.SIMILARITY Belongs to the influenza viruses matrix protein M2 family.
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FUNCTION Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.SUBUNIT Homotrimer of disulfide-linked HA1-HA2.MISCELLANEOUS Major glycoprotein, comprises over 80% of the envelope proteins present in virus particle.MISCELLANEOUS The extent of infection into host organism is determined by HA. Influenza viruses bud from the apical surface of polarized epithelial cells (e.g. bronchial epithelial cells) into lumen of lungs and are therefore usually pneumotropic. The reason is that HA is cleaved by tryptase clara which is restricted to lungs. However, HAs of H5 and H7 pantropic avian viruses subtypes can be cleaved by furin and subtilisin-type enzymes, allowing the virus to grow in other organs than lungs.MISCELLANEOUS The influenza A genome consist of 8 RNA segments. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains. The mechanism of variation can be the result of point mutations or the result of genetic reassortment between segments of two different strains.SIMILARITY Belongs to the influenza viruses hemagglutinin family.
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MISCELLANEOUS Most abundant protein in virion. When expressed alone can form virus-like particles in transfected cells.SIMILARITY Belongs to the influenza viruses Matrix protein M1 family.
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Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins
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Heat shock protein 70 is related to thermal inhibition of nuclear export of the influenza virus ribonucleoprotein complex
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Identification of two separate domains in the influenza virus PB1 protein involved in the interaction with the PB2 and PA subunits: a model for the viral RNA polymerase structure
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The three influenza virus polymerase (P) proteins not associated with viral nucleocapsids in the infected cell are in the form of a complex
Association of influenza virus matrix protein with ribonucleoproteins
SIMILARITY Belongs to the importin beta family.SIMILARITY Contains 6 HEAT repeats.SIMILARITY Contains 1 importin N-terminal domain.
FUNCTION Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes.SUBUNIT Homodimer. Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C STIP1. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8.DOMAIN The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.PTM ISGylated.PTM S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.SIMILARITY Belongs to the heat shock protein 90 family.
Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex
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'HSP70' negatively regulates 'Binding of M1 to vRNP'
'Importin beta-3 [nucleoplasm]' positively regulates 'Viral Polymerase Assembly'
'HSP90 [nucleoplasm]' positively regulates 'Viral Polymerase Assembly'
TISSUE SPECIFICITY HSPA1B is testis-specific.INDUCTION By heat shock.SIMILARITY Belongs to the heat shock protein 70 family.
Association of influenza virus matrix protein with ribonucleoproteins may control viral growth and morphology
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Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes
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FUNCTION Mediates the nuclear export of encapsidated genomic RNAs (ribonucleoproteins, RNPs). Acts as an adapter between viral RNPs complexes and the nuclear export machinery of the cell. Possesses no intrinsic RNA-binding activity, but includes a C-terminal M1-binding domain. This domain is believed to allow recognition of RNPs to which the M1 protein is bound. Because the M1 protein is not available in large quantities until the later stages of infection, such an indirect recognition mechanism probably ensures that genomic RNPs are not exported from the nucleus before sufficient quantities of viral mRNA and progeny genomic RNA have been synthesized. Furthermore, the RNPs enters the cytoplasm only when they have associated with the M1 protein that is necessary to guide them to the plasma membrane. May down-regulate viral RNA synthesis when overproduced.SUBUNIT Binds M1 protein. May interact with human nucleoporin RAB/HRB and exportin XPO1/CRM1.MISCELLANEOUS Average number present in a viral particle is estimated to be 130-200 molecules.SIMILARITY Belongs to the influenza viruses NEP family.
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EMBL:AF389121 H1N1 Genomic RNA Segment 7
Influenza A virus (A/Puerto Rico/8/34/Mount Sinai(H1N1)) segment 7, complete sequence.
Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export
EMBL:AF389120 H1N1 Genomic RNA Segment 6
Influenza A virus (A/Puerto Rico/8/34/Mount Sinai(H1N1)) segment 6, complete sequence.
Transport of processed viral proteins to the cell membrane
Once processed, the viral proteins are transported from the golgi apparatus to the plasma membrane.
The mature ternary influenza viral polymerase complex consists of PB1, PB2, and PA. The N-terminus of PB1 (residues 1-48) interacts with PB2, and amino acids 506-659 in PB1 interact with the PA subunit (Gonzalez, 1996; Perez, 2001). Although monomeric PB1, PB2 and PA, as well as PB1-PB2 and PB1-PA dimers are likely to exist in infected cells, it is believed that most of the polymerase proteins are assembled into the trimeric PB1-PB2-PA complex (Detjen, 1987). Newly synthesized subunits of the polymerase are imported into the nucleus through nuclear localization signals (NLS), which interact with cellular importin family proteins (Jones, 1986; Buolo, 2006). Importin beta-3 (Ran binding protein 5) facilitates nuclear import of PB1 and a PB1-PA dimer (Deng, 2006); coexpression of PA with PB1 was shown to enhance the import of PB1 (Fodor, 2004). A PB1-PB2 dimer has been found to interact with the molecular chaperone heat shock protein 90 (HSP90) to facilitate import (Naito, 2007). The three subunits assembled in the nucleus form a mature ternary polymerase complex that binds viral vRNA or cRNA (Jones, 1986; Buolo, 2006).
Authored: Bortz, E, Garcia-Sastre, A, 2007-02-12 19:39:05
As influenza viruses bud from the plasma membrane of infected cells, complete virions are not seen inside cells. In polarized epithelial cells, assembly and budding of influenza occurs from the apical plasma membrane (Schmitt, 2004). For efficient assembly, all virion components must accumulate at the budding site, and it is believed that the viral glycoprotein accumulation determines the site of virus assembly and budding (Nayak, 2004). M1 is thought to be the bridge between the envelope glycoproteins and the RNPs for assembly (Schmitt, 2004). M2 is also required, because if it is not present RNPs are not packaged into budding virions (McCown, 2005), however it role is not known.
M1 protein binds to viral RNP through its C-terminal domain (Baudin, 2001). The influenza M1 protein accumulates in the infected cell nucleus through a nuclear localization signal (NLS) RKLKR (residues 101-105) in its N-terminus (Ye, 1999). A host cell protein, HSP70, is thought to inhibit M1 binding at nonpermissive temperatures (Hirayama et al., 2004).
EMBL:AF389122 H1N1 Genomic RNA Segment 8
Influenza A virus (A/Puerto Rico/8/34/Mount Sinai(H1N1)) segment 8, complete sequence.
The M2 from influenza A virus is a 97-residue protein with a single transmembrane helix that associates to form a tetramer in the endoplasmic reticulum (Salom et al, 2000). A 15-20-residue segment C-terminal to the membrane-spanning region has been postulated to aid in the stabilization of the tetrameric assembly (Kochendoerfer et al 1999).
EMBL:AF389118 H1N1 Genomic RNA Segment 4
Influenza A virus (A/Puerto Rico/8/34/Mount Sinai(H1N1)) segment 4, complete sequence.
EMBL:AF389115 H1N1 Genomic RNA Segment 1
Influenza A virus (A/Puerto Rico/8/34/Mount Sinai(H1N1)) segment 1, complete sequence
EMBL:AF389116 H1N1 Genomic RNA Segment 2
Influenza A virus (A/Puerto Rico/8/34/Mount Sinai(H1N1)) segment 2, complete sequence.
EMBL:AF389117 H1N1 Genomic RNA Segment 3
Influenza A virus (A/Puerto Rico/8/34/Mount Sinai(H1N1)) segment 3, complete sequence.
EMBL:AF389119 H1N1 Genomic RNA Segment 5
Influenza A virus (A/Puerto Rico/8/34/Mount Sinai(H1N1)) segment 5, complete sequence.
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