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ID 20596
file
creator
Shimazu, Yukie
Yoshida, Tetsuya
NDC
Medical sciences
abstract
For many enveloped viruses, cellular multivesicular body (MVB) sorting machinery has been reported to be utilized for efficient viral budding. Matrix and Gag proteins have been shown to contain one or two L-domain motifs (PPxY, PT/SAP, YPDL, and FPIV), some of which interact specifically with host cellular proteins involved in multivesicular body sorting, which are recruited to the viral budding site. However, for many enveloped viruses, L-domain motifs have not yet been identified, and the involvement of MVB sorting machinery in viral budding is still unknown. Here we show that both Sendai virus (SeV) matrix protein M and accessory protein C contribute to virus budding by physically interacting with Alix/AIP1. A YLDL sequence within the M protein showed L-domain activity, and its specific interaction with the N-terminus of Alix/AIP1 (1-211) was important for the budding of virus-like particles (VLPs) of M protein. In addition, M-VLP budding was inhibited by the overexpression of some deletion mutants of Alix/AIP1 and depletion of endogenous Alix/AIP1 using specific siRNAs. The YLDL sequence was not replaceable by other L-domain motifs, such as PPxY and PT/SAP, and even YPxL. C protein was also able to physically interact with the N-terminus of Alix/AIP1 (212-357) and enhanced M-VLP budding independently of M-Alix/AIP1 interaction, although it was not released from the transfected cells itself. Our results suggest that the interaction of multiple viral proteins with Alix/AIP1 may enhance the efficiency of the utilization of cellular MVB sorting machinery for efficient SeV budding.
journal title
Journal of Virology
volume
Volume 81
issue
Issue 5
start page
2263
end page
2273
date of issued
2007-03
publisher
American Society for Microbiology
issn
0022-538X
ncid
publisher doi
language
eng
nii type
Journal Article
HU type
Journal Articles
DCMI type
text
format
application/pdf
text version
author
rights
Copyright (c) 2007 American Society for Microbiology
relation url
department
Graduate School of Biomedical Science