- 著者
-
Kuroda Makoto
Fujikura Daisuke
Nanbo Asuka
Marzi Andrea
Noyori Osamu
Kajihara Masahiro
Maruyama Junki
Matsuno Keita
Miyamoto Hiroko
Yoshida Reiko
Feldmann Heinz
Takada Ayato
- 出版者
- American Society for Microbiology
- 雑誌
- Journal of virology (ISSN:0022538X)
- 巻号頁・発行日
- vol.89, no.12, pp.6481-6493, 2015-06
- 被引用文献数
-
64
Multiple host molecules are known to be involved in the cellular entry of filoviruses, including Ebola virus (EBOV); T-cell immunoglobulin and mucin domain 1 (TIM-1) and Niemann-Pick C1 (NPC1) have been identified as attachment and fusion receptors, respectively. However, the molecular mechanisms underlying the entry process have not been fully understood. We found that TIM-1 and NPC1 colocalized and interacted in the intracellular vesicles where EBOV glycoprotein (GP)-mediated membrane fusion occurred. Interestingly, a TIM-1-specific monoclonal antibody (MAb), M224/1, prevented GP-mediated membrane fusion and also interfered with the binding of TIM-1 to NPC1, suggesting that the interaction between TIM-1 and NPC1 is important for filovirus membrane fusion. Moreover, MAb M224/1 efficiently inhibited the cellular entry of viruses from all known filovirus species. These data suggest a novel mechanism underlying filovirus membrane fusion and provide a potential cellular target for antiviral compounds that can be universally used against filovirus infections.