Characteristics of Nucleocytoplasmic Transport of H1N1 Influenza A Virus Nuclear Export Protein

Gao, Shengyan; Wang, Shanshan; Cao, Shuai; Sun, Lei; Li, Jing; Bi, Yuhai; Gao, George F.; Liu, Wenjun

doi:10.1128/jvi.00257-14

Cited by 17 publications

(18 citation statements)

References 38 publications

(38 reference statements)

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“…In addition, we have also found that the CA04 strain displays different vRNP distribution patterns, forming unique nuclear aggregates, with respect to WSN by comparing different strains of H1N1 NEP for vRNP nuclear translocation. In the further study, we confirmed that CA04 NEP interacts less efficiently with CRM1 and site T48 is responsible for the nuclear aggregation [ 44 ]. In view of NEP playing an important role in viral polymerase activity and vRNP nuclear transport efficiency, these differences may be one reason for divergence of the pathogenicity and host adaptation range between these virus strains.…”

Section: Discussionmentioning

confidence: 73%

“…It may not need a NLS as it is only 14 kDa in size, and at present, no NLS has been found in NEP. Through the use of an inhibitor of NLS-dependent active nuclear transport and an energy depletion assay, it was demonstrated that NEP enters the nucleus by passive diffusion [ 44 ].…”

Section: Nucleocytoplasmic Shuttling Mechanism Of Iav Proteinsmentioning

confidence: 99%

“…Further, it has been demonstrated that the NES1 and NES2 of NEP [ 43 ] are CRM1 dependent and jointly participate in the nuclear export of NEP and vRNP. Interestingly, the NEPs of different strains result in distinct cellular distribution patterns, forming unique nuclear aggregates, with the weaker binding capacity to CRM1 due to one amino acid change in the NES, perhaps facilitating the export of the vRNP complex [ 44 ].…”

Section: Nucleocytoplasmic Shuttling Mechanism Of Iav Proteinsmentioning

confidence: 99%

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Nucleocytoplasmic Shuttling of Influenza A Virus Proteins

Zheng

et al. 2015

Viruses

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Influenza viruses transcribe and replicate their genomes in the nuclei of infected host cells. The viral ribonucleoprotein (vRNP) complex of influenza virus is the essential genetic unit of the virus. The viral proteins play important roles in multiple processes, including virus structural maintenance, mediating nucleocytoplasmic shuttling of the vRNP complex, virus particle assembly, and budding. Nucleocytoplasmic shuttling of viral proteins occurs throughout the entire virus life cycle. This review mainly focuses on matrix protein (M1), nucleoprotein (NP), nonstructural protein (NS1), and nuclear export protein (NEP), summarizing the mechanisms of their nucleocytoplasmic shuttling and the regulation of virus replication through their phosphorylation to further understand the regulation of nucleocytoplasmic shuttling in host adaptation of the viruses.

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Section: Discussionmentioning

confidence: 73%

Section: Nucleocytoplasmic Shuttling Mechanism Of Iav Proteinsmentioning

confidence: 99%

Section: Nucleocytoplasmic Shuttling Mechanism Of Iav Proteinsmentioning

confidence: 99%

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Nucleocytoplasmic Shuttling of Influenza A Virus Proteins

Zheng

et al. 2015

Viruses

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“…Another interesting RNP export modality was discovered while investigating mRNA export in Influenza A viruses (IAV) [ 138 ]. Electron microscopy studies show that IAV enlarges the nuclear pores in infected cells by around 20 nm (a final size of around 50 nm) [ 139 , 140 ] ( Figure 4 ). The increase in pore diameter facilitates the translocation of large protein complexes.…”

Section: Other Exits For Mrnamentioning

confidence: 99%

Multiple Export Mechanisms for mRNAs

Delaleau

Borden

2015

Cells

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Nuclear mRNA export plays an important role in gene expression. We describe the mechanisms of mRNA export including the importance of mRNP assembly, docking with the nuclear basket of the nuclear pore complex (NPC), transit through the central channel of the NPC and cytoplasmic release. We describe multiple mechanisms of mRNA export including NXF1 and CRM1 mediated pathways. Selective groups of mRNAs can be preferentially transported in order to respond to cellular stimuli. RNAs can be selected based on the presence of specific cis-acting RNA elements and binding of specific adaptor proteins. The role that dysregulation of this process plays in human disease is also discussed.

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“…, , Gao et al . , ). The NP of the WSN strain contains a CRM1‐dependent NES and two CRM1‐independent NESs, which are crucial for nuclear export (Yu et al .…”

Section: Introductionmentioning

confidence: 97%

Differential nucleocytoplasmic shuttling of the nucleoprotein of influenza a viruses and association with host tropism

Zheng

Hou

et al. 2016

Cellular Microbiology

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The nucleoprotein (NP) of influenza A virus plays a crucial role in virus replication, infectivity, and host adaptation. As a major component of the viral ribonucleoprotein complexes (vRNP), NP initiates vRNP shuttling between the nucleus and cytoplasm in the host cell. However, the characteristics of the nucleocytoplasmic shuttling of NP from H1N1 influenza A virus still remain unclear. In the present study, the subcellular localization and the related key residues of the H1N1 influenza virus NP were identified and evaluated. The NP of influenza virus A/WSN/33 (H1N1; WSN) displayed a more obvious nuclear accumulation than A/Anhui/1/2013 (H7N9; AH) and A/chicken/Shandong/lx1023/2007 (H9N2; SD). NP residue K4, located in NLS1, and residue F253, located in NES3, from WSN NP are not conserved in H7N9 and H9N2, which instead encode Q4 and I253, respectively. Crucially, these residues are involved in the regulation of NP nucleocytoplasmic shuttling through interactions with CRM1 and importin-α. Moreover, residues at position 253 also play important roles in the replication of the virus, resulting in an increase in vRNP polymerase activity and an alteration of the cell tropism and pathogenicity in mice. The present data revealed a pivotal role of the Q4 and I253 residues of NP from H7N9 in enhancing the cytoplasmic accumulation of NP and vRNP activity compared to the K4 and F253 residues in WSN-NP. In addition, an F253I substitution in the NP of WSN altered the survival ratio of infected mice and the growth curve in infected avian-origin cells (DF-1). The current data indicate that the F253I mutation results in attenuated pathogenicity of the virus in mice and altered cell tropism. The present study demonstrated the dissimilarity in subcellular NP transport processes between H1N1 virus WSN and other influenza A virus strains, as well as uncovered the mechanism responsible for this difference.

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Characteristics of Nucleocytoplasmic Transport of H1N1 Influenza A Virus Nuclear Export Protein

Cited by 17 publications

References 38 publications

Nucleocytoplasmic Shuttling of Influenza A Virus Proteins

Nucleocytoplasmic Shuttling of Influenza A Virus Proteins

Multiple Export Mechanisms for mRNAs

Differential nucleocytoplasmic shuttling of the nucleoprotein of influenza a viruses and association with host tropism

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