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Transcellular transport of West Nile virus-like particles across human endothelial cells depends on residues 156 and 159 of envelope protein

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Title: Transcellular transport of West Nile virus-like particles across human endothelial cells depends on residues 156 and 159 of envelope protein
Authors: Hasebe, Rie Browse this author →KAKEN DB
Suzuki, Tadaki Browse this author →KAKEN DB
Makino, Yoshinori Browse this author →KAKEN DB
Igarashi, Manabu Browse this author →KAKEN DB
Yamanouchi, Satoko Browse this author
Maeda, Akihiko Browse this author →KAKEN DB
Horiuchi, Motohiro Browse this author →KAKEN DB
Sawa, Hirofumi Browse this author →KAKEN DB
Kimura, Takashi Browse this author →KAKEN DB
Issue Date: 8-Jun-2010
Publisher: BioMed Central
Journal Title: BMC Microbiology
Volume: 10
Start Page: 165
Publisher DOI: 10.1186/1471-2180-10-165
Abstract: Background: West Nile virus (WNV) causes viremia after invasion to the hosts by mosquito bite. Endothelial cells could play an important role in WNV spread from the blood stream into the central nervous system and peripheral tissues. Here, we analyzed the capacity of virus-like particles (VLPs) of the highly virulent NY99 6-LP strain (6-LP VLPs) and the low virulence Eg101 strain (Eg VLPs) to cross cultured human endothelial cells. Results: 6-LP VLPs were transported from the apical to basolateral side of endothelial cells, whereas Eg VLPs were hardly transported. The localization of tight junction marker ZO-1 and the integrity of tight junctions were not impaired during the transport of 6-LP VLPs. The transport of 6-LP VLPs was inhibited by treatment with filipin, which prevents the formation of cholesterol-dependent membrane rafts, suggesting the involvement of raft-associated membrane transport. To determine the amino acid residues responsible for the transport of VLPs, we produced mutant VLPs, in which residues of E protein were exchanged between the 6-LP and Eg strains. Double amino acid substitution of the residues 156 and 159 greatly impaired the transport of VLPs. Conclusion: Our results suggest that a transcellular pathway is associated with 6-LP VLPs transport. We also showed that the combination of the residues 156 and 159 plays an important role in the transport of VLPs across endothelial cells.
Rights: http://creativecommons.org/licenses/by/2.0
Type: article
URI: http://hdl.handle.net/2115/43321
Appears in Collections:獣医学院・獣医学研究院 (Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 長谷部 理絵

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