Functional analysis of late-budding domain activity associated with the PSAP motif within the vesicular stomatitis virus M protein

被引:34
作者
Irie, T
Licata, JM
Jayakar, HR
Whitt, MA
Bell, P
Harty, RN
机构
[1] Univ Penn, Sch Vet Med, Dept Pathobiol, Philadelphia, PA 19104 USA
[2] Univ Penn, Sch Med, Div Med Genet, Gene Therapy Program, Philadelphia, PA 19104 USA
[3] GTx Inc, Memphis, TN 38163 USA
[4] Univ Tennessee, Ctr Hlth Sci, Dept Mol Sci, Memphis, TN 38163 USA
关键词
D O I
10.1128/JVI.78.14.7823-7827.2004
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A PPPY motif within the M protein of vesicular stomatitis virus (VSV) functions as a late-budding domain (L-domain); however, L-domain activity has yet to be associated with a downstream PSAP motif. VSV recombinants with mutations in the PPPY and/or PSAP motif were recovered by reverse genetics and examined for growth kinetics, plaque size, and budding efficiency by electron microscopy. Results indicate that unlike the PPPY motif, the PSAP motif alone does not possess L-domain activity. Finally, the insertion of the human immunodeficiency virus type 1 p6 L-domain and flanking sequences into the PSAP region of M protein rescued budding of a PPPY mutant of VSV to wild-type levels.
引用
收藏
页码:7823 / 7827
页数:5
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