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2 results on '"Tetsuya Sekimoto"'

1. Apical transport of influenza A virus ribonucleoprotein requires Rab11-positive recycling endosome.

Author

Fumitaka Momose, Tetsuya Sekimoto, Takashi Ohkura, Shuichi Jo, Atsushi Kawaguchi, Kyosuke Nagata, and Yuko Morikawa

Subjects
Medicine, Science
Abstract

Influenza A virus RNA genome exists as eight-segmented ribonucleoprotein complexes containing viral RNA polymerase and nucleoprotein (vRNPs). Packaging of vRNPs and virus budding take place at the apical plasma membrane (APM). However, little is known about the molecular mechanisms of apical transport of newly synthesized vRNP. Transfection of fluorescent-labeled antibody and subsequent live cell imaging revealed that punctate vRNP signals moved along microtubules rapidly but intermittently in both directions, suggestive of vesicle trafficking. Using a series of Rab family protein, we demonstrated that progeny vRNP localized to recycling endosome (RE) in an active/GTP-bound Rab11-dependent manner. The vRNP interacted with Rab11 through viral RNA polymerase. The localization of vRNP to RE and subsequent accumulation to the APM were impaired by overexpression of Rab binding domains (RBD) of Rab11 family interacting proteins (Rab11-FIPs). Similarly, no APM accumulation was observed by overexpression of class II Rab11-FIP mutants lacking RBD. These results suggest that the progeny vRNP makes use of Rab11-dependent RE machinery for APM trafficking.

Published
2011
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2. Apical transport of influenza A virus ribonucleoprotein requires Rab11-positive recycling endosome

Author

Tetsuya Sekimoto, Fumitaka Momose, Yuko Morikawa, Kyosuke Nagata, Atsushi Kawaguchi, Shuichi Jo, and Takashi Ohkura

Subjects
RNA viruses, Viral Diseases, lcsh:Medicine, Microtubules, Biochemistry, chemistry.chemical_compound, Molecular cell biology, Viral classification, RNA polymerase, lcsh:Science, Polymerase, Ribonucleoprotein, Multidisciplinary, Cell Polarity, DNA-Directed RNA Polymerases, Endocytosis, Cell biology, Transport protein, Nucleic acids, Host-Pathogen Interaction, Protein Transport, Infectious Diseases, Ribonucleoproteins, Influenza A virus, Medicine, Membranes and Sorting, Guanosine Triphosphate, Protein Binding, Signal Transduction, Research Article, Endosome, Cell Survival, Endosomes, Biology, Models, Biological, Microbiology, Cell Line, Dogs, Orthomyxoviridae Infections, Virology, Animals, Immunoprecipitation, Protein Interactions, lcsh:R, RNA, Proteins, Molecular biology, Influenza, Nucleoprotein, Cell Compartmentation, Protein Structure, Tertiary, chemistry, rab GTP-Binding Proteins, biology.protein, lcsh:Q, Rab, Gene expression, Protein Multimerization, RNA transport
Abstract

Influenza A virus RNA genome exists as eight-segmented ribonucleoprotein complexes containing viral RNA polymerase and nucleoprotein (vRNPs). Packaging of vRNPs and virus budding take place at the apical plasma membrane (APM). However, little is known about the molecular mechanisms of apical transport of newly synthesized vRNP. Transfection of fluorescent-labeled antibody and subsequent live cell imaging revealed that punctate vRNP signals moved along microtubules rapidly but intermittently in both directions, suggestive of vesicle trafficking. Using a series of Rab family protein, we demonstrated that progeny vRNP localized to recycling endosome (RE) in an active/GTP-bound Rab11-dependent manner. The vRNP interacted with Rab11 through viral RNA polymerase. The localization of vRNP to RE and subsequent accumulation to the APM were impaired by overexpression of Rab binding domains (RBD) of Rab11 family interacting proteins (Rab11-FIPs). Similarly, no APM accumulation was observed by overexpression of class II Rab11-FIP mutants lacking RBD. These results suggest that the progeny vRNP makes use of Rab11-dependent RE machinery for APM trafficking.

Published
2011

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