Crucial role of PA in virus life cycle and host adaptation of influenza A virus

2014 ◽  
Vol 204 (2) ◽  
pp. 137-149 ◽  
Author(s):  
Jiao Hu ◽  
Xiufan Liu
Keyword(s):  
Life Cycle ◽  
Influenza A Virus ◽  
Crucial Role ◽  
Influenza A ◽  
Host Adaptation ◽  
Virus Life Cycle

scholarly journals The role of Ran-binding protein 3 during influenza A virus replication

2013 ◽  
Vol 94 (5) ◽  
pp. 977-984 ◽  
Author(s):  
Rey Predicala ◽  
Yan Zhou
Keyword(s):  
Life Cycle ◽  
Influenza A Virus ◽  
Nuclear Export ◽  
Influenza A ◽  
Binding Protein ◽  
Late Phase ◽  
Nuclear Retention ◽  
Interacting Protein ◽  
Virus Life Cycle

Influenza A virus vRNP nuclear export is CRM1-dependent. Ran-binding protein 3 (RanBP3) is a Ran-interacting protein that is best known for its role as a cofactor of CRM1-mediated cargo nuclear export. In this study, we investigated the role of RanBP3 during the influenza A virus life cycle. We found that RanBP3 was phosphorylated at Ser58 in the early and late phases of infection. Knockdown of RanBP3 expression led to vRNP nuclear retention, suggesting that RanBP3 is involved in vRNP nuclear export. Moreover, we demonstrated that the function of RanBP3 during vRNP nuclear export is regulated by phosphorylation at Ser58, and that RanBP3 phosphorylation is modulated by both PI3K/Akt and Ras/ERK/RSK pathways in the late phase of viral infection.

scholarly journals Phosphorylation Controls the Nuclear-Cytoplasmic Shuttling of Influenza A Virus Nucleoprotein

2015 ◽  
Vol 89 (11) ◽  
pp. 5822-5834 ◽  
Author(s):  
Weinan Zheng ◽  
Jing Li ◽  
Shanshan Wang ◽  
Shuaishuai Cao ◽  
Jingwen Jiang ◽  
...  
Keyword(s):  
Life Cycle ◽  
Influenza A Virus ◽  
Influenza A ◽  
Early Stage ◽  
Phosphorylation Sites ◽  
Nuclear Retention ◽  
Virus Growth ◽  
Virus Life Cycle ◽  
Importin Α ◽  
Infected Cells

ABSTRACTThe nucleoprotein (NP) is a major component of the viral ribonucleoprotein (vRNP) complex. During the replication of influenza virus, the vRNP complex undergoes nuclear-cytoplasmic shuttling, during which NP serves as one of the determinants. To date, many phosphorylation sites on NP have been identified, but the biological functions of many of these phosphorylation sites remain unknown. In the present study, the functions of the phosphorylation sites S9, Y10, and Y296 were characterized. These residues are highly conserved, and their phosphorylation was essential for virus growth in cell culture and in a mouse model by regulating the activity of the viral polymerase and the nuclear-cytoplasmic shuttling of NP. The phosphorylation and dephosphorylation of S9 and Y10 controlled nuclear import of NP by affecting the binding affinity between NP and different isoforms of importin-α. In addition, the phosphorylation of Y296 caused nuclear retention of NP by reducing the interaction between NP and CRM1. Furthermore, tyrosine phosphorylation of NP during the early stage of virus infection was ablated when Y296 was mutated to F. However, at later stages of infection, it was weakened by the Y10F mutation. Taken together, the present data indicate that the phosphorylation and dephosphorylation of NP control the shuttling of NP between the nucleus and the cytoplasm during virus replication.IMPORTANCEIt is well known that phosphorylation regulates the functions of viral proteins and the life cycle of influenza A virus. As NP is the most abundant protein in the vRNP complex of influenza A virus, several phosphorylation sites on this protein have been identified. However, the functions of these phosphorylation sites were unknown. The present study demonstrates that the phosphorylation status of these sites on NP can mediate its nuclear-cytoplasmic shuttling, which drives the trafficking of vRNP complexes in infected cells. The present data suggest that the phosphorylated residues of NP are multistep controllers of the virus life cycle and new targets for the design of anti-influenza drugs.

scholarly journals Evidence for a crucial role of a host non-coding RNA in influenza A virus replication

RNA Biology ◽  
2013 ◽  
Vol 11 (1) ◽  
pp. 66-75 ◽  
Author(s):  
Carla Winterling ◽  
Manuel Koch ◽  
Max Koeppel ◽  
Fernando Garcia-Alcalde ◽  
Alexander Karlas ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Virus Replication ◽  
Crucial Role ◽  
Influenza A ◽  
Non Coding Rna

scholarly journals A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein

Virus Genes ◽  
2014 ◽  
Vol 49 (1) ◽  
pp. 157-162 ◽  
Author(s):  
Qinfang Liu ◽  
Bhupinder Bawa ◽  
Jingjiao Ma ◽  
Feng Li ◽  
Wenjun Ma ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Crucial Role ◽  
Influenza A ◽  
Terminal Domain ◽  
M1 Protein

scholarly journals The Functional Role of Loops and Flanking Sequences of G-Quadruplex Aptamer to the Hemagglutinin of Influenza a Virus

2021 ◽  
Vol 22 (5) ◽  
pp. 2409
Author(s):  
Anastasia A. Bizyaeva ◽  
Dmitry A. Bunin ◽  
Valeria L. Moiseenko ◽  
Alexandra S. Gambaryan ◽  
Sonja Balk ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Core Structure ◽  
Dna Aptamer ◽  
Tertiary Structures ◽  
Quadruplex Dna ◽  
G Quadruplex ◽  
Flanking Sequences ◽  
Related Proteins

Nucleic acid aptamers are generally accepted as promising elements for the specific and high-affinity binding of various biomolecules. It has been shown for a number of aptamers that the complexes with several related proteins may possess a similar affinity. An outstanding example is the G-quadruplex DNA aptamer RHA0385, which binds to the hemagglutinins of various influenza A virus strains. These hemagglutinins have homologous tertiary structures but moderate-to-low amino acid sequence identities. Here, the experiment was inverted, targeting the same protein using a set of related, parallel G-quadruplexes. The 5′- and 3′-flanking sequences of RHA0385 were truncated to yield parallel G-quadruplex with three propeller loops that were 7, 1, and 1 nucleotides in length. Next, a set of minimal, parallel G-quadruplexes with three single-nucleotide loops was tested. These G-quadruplexes were characterized both structurally and functionally. All parallel G-quadruplexes had affinities for both recombinant hemagglutinin and influenza virions. In summary, the parallel G-quadruplex represents a minimal core structure with functional activity that binds influenza A hemagglutinin. The flanking sequences and loops represent additional features that can be used to modulate the affinity. Thus, the RHA0385–hemagglutinin complex serves as an excellent example of the hypothesis of a core structure that is decorated with additional recognizing elements capable of improving the binding properties of the aptamer.

scholarly journals Role of Virally-Encoded Deubiquitinating Enzymes in Regulation of the Virus Life Cycle

2021 ◽  
Vol 22 (9) ◽  
pp. 4438
Author(s):  
Jessica Proulx ◽  
Kathleen Borgmann ◽  
In-Woo Park
Keyword(s):  
Immune Response ◽  
Life Cycle ◽  
Deubiquitinating Enzyme ◽  
Deubiquitinating Enzymes ◽  
Antiviral Immune Response ◽  
Cellular Processes ◽  
Virus Life Cycle ◽  
Infected Cells ◽  
Dependent Processes

The ubiquitin (Ub) proteasome system (UPS) plays a pivotal role in regulation of numerous cellular processes, including innate and adaptive immune responses that are essential for restriction of the virus life cycle in the infected cells. Deubiquitination by the deubiquitinating enzyme, deubiquitinase (DUB), is a reversible molecular process to remove Ub or Ub chains from the target proteins. Deubiquitination is an integral strategy within the UPS in regulating survival and proliferation of the infecting virus and the virus-invaded cells. Many viruses in the infected cells are reported to encode viral DUB, and these vial DUBs actively disrupt cellular Ub-dependent processes to suppress host antiviral immune response, enhancing virus replication and thus proliferation. This review surveys the types of DUBs encoded by different viruses and their molecular processes for how the infecting viruses take advantage of the DUB system to evade the host immune response and expedite their replication.

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