期刊
JOURNAL OF VIROLOGY
卷 86, 期 6, 页码 3014-3026出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.05826-11
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资金
- NIH [R01AI051517]
- NIH from the Southeastern Regional Center of Excellence for Emerging Infections and Biodefense [U54 AI057157]
- NIH from the National Center for Research Resources [2P20 RR020171]
- [R01GM070662]
Hendra virus is a highly pathogenic paramyxovirus classified as a biosafety level four agent. The fusion (F) protein of Hendra virus is critical for promoting viral entry and cell-to-cell fusion. To be fusogenically active, Hendra virus F must undergo endocytic recycling and cleavage by the endosomal/lysosomal protease cathepsin L, but the route of Hendra virus F following internalization and the recycling signals involved are poorly understood. We examined the intracellular distribution of Hendra virus F following endocytosis and showed that it is primarily present in Rab5- and Rab4-positive endosomal compartments, suggesting that cathepsin L cleavage occurs in early endosomes. Hendra virus F transmembrane domain (TMD) residues S490 and Y498 were found to be important for correct Hendra virus F recycling, with the hydroxyl group of S490 and the aromatic ring of Y498 important for this process. In addition, changes in association of isolated Hendra virus F TMDs correlated with alterations to Hendra virus F recycling, suggesting that appropriate TMD interactions play an important role in endocytic trafficking.
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