JVI Accepts, published online ahead of print on 20 September 2006

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J. Virol. doi:10.1128/JVI.01471-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

CryoEM of Protein IX-Modified Adenoviruses Suggests a New Position for the C-terminus of Protein IX

Michael P. Marsh, Samuel K. Campos, Matthew L. Baker, Christopher Y. Chen, Wah Chiu, and Michael A. Barry^*

Program in Structural and Computational Biology and Molecular Biophysics, National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Department of Molecular and Human Genetics, The Department of Immunology, and Center for Cell and Gene Therapy, Baylor College of Medicine, Houston, TX 77030; Departments of Bioengineering and Biochemistry & Cell Biology, Rice University, Houston, TX; Department of Internal Medicine, Division of Infectious Diseases, Translational Immunovirology Program, Mayo Clinic, Rochester, MN

^* To whom correspondence should be addressed. Email: barry.michael{at}mayo.edu.

Recombinant human adenovirus is a useful gene delivery vector for clinical gene therapy. Minor capsid protein IX of adenovirus has been of recent interest since multiple studies have shown that modifications can be made to its C-terminus to alter viral tropism or add molecular tags and/or reporter proteins. We examined the structure of an engineered adenovirus displaying the green fluorescent protein (EGFP) fused to the C-terminus of protein IX. Cryo-electron microscopy and reconstruction localized the C-terminal EGFP fusion between the H2 hexon and the H4 hexon, positioned between adjacent facets, directly above the density previously assigned as protein IIIa. The original assignment of IIIa was based largely on indirect evidence and the data presented herein support the reassignment of the IIIa density as protein IX.

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