Mutation of Single Hydrophobic Residue I27, L35, F39, L58, L65, L67, or L71 in the N Terminus of VP5 Abolishes Interaction with the Scaffold Protein and Prevents Closure of Herpes Simplex Virus Type 1 Capsid Shells

Mutation of Single Hydrophobic Residue I27, L35, F39, L58, L65, L67, or L71 in the N Terminus of VP5 Abolishes Interaction with the Scaffold Protein and Prevents Closure of Herpes Simplex Virus Type 1 Capsid Shells

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Veröffentlicht in:Journal of Virology 2003-04, Vol.77 (7), p.4043-4059
Hauptverfasser: Walters, Jewell N, Sexton, Gerry L, McCaffery, J Michael, Desai, Prashant
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Amino Acid Substitution
Animals
Binding Sites - genetics
Capsid - chemistry
Capsid - metabolism
Capsid - ultrastructure
Capsid Proteins - genetics
Capsid Proteins - metabolism
Capsid Proteins - ultrastructure
Cercopithecus aethiops
Genome, Viral
Herpesvirus 1, Human - genetics
Herpesvirus 1, Human - growth & development
Herpesvirus 1, Human - metabolism
Microscopy, Electron
Molecular Sequence Data
Mutagenesis, Site-Directed
Point Mutation
Protein Binding
Protein Structure, Tertiary
Structure and Assembly
Two-Hybrid System Techniques
Vero Cells
Viral Structural Proteins - chemistry
Viral Structural Proteins - metabolism
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Zusammenfassung:Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
ISSN:0022-538X
1098-5514
DOI:10.1128/JVI.77.7.4043-4059.2003