This project seeks to discover and describe mechanisms of virus assembly, ultimately at near-atomic resolution and including an understanding of the dynamic and energetic aspects of virus capsid maturation. Objects to be studied include the head of bacteriophage HK97, with particular interest in capsid assembly, capsid maturation, and control and mechanism of covalent crosslinking;phage lambda tails, with particular interest in length determination and the role of assembly chaperones;phage lambda long tail fibers, with particular interest in the role and mode of interaction of an assembly chaperone; and the capsids of a group of phages with unusually large capsids, with particular interest in how large capsid sizes are determined accurately. This work will enhance our understanding of virus life cycles and of molecular machines. The group of viruses under study shares many of the features of its assembly and maturation with animal viruses, especially including Herpesvirus, so these studies have the potential to enhance our understanding of human pathogens.

Public Health Relevance

This project studies the structure of viruses and the way virus particles are assembled in the infected cell from their component proteins and DNA. This will advance understanding of virus life cycles and so potentially our ability to disrupt those life cycles. The specific viruses under study, bacteriophages, do not directly cause human disease, but they share many similarities with human viruses, particularly the Herpes viruses.

National Institute of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
Research Project (R01)
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Prokaryotic Cell and Molecular Biology Study Section (PCMB)
Program Officer
Sakalian, Michael
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University of Pittsburgh
Schools of Arts and Sciences
United States
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Huet, Alexis; Duda, Robert L; Hendrix, Roger W et al. (2016) Correct Assembly of the Bacteriophage T5 Procapsid Requires Both the Maturation Protease and the Portal Complex. J Mol Biol 428:165-81
Casjens, Sherwood R; Hendrix, Roger W (2015) Bacteriophage lambda: Early pioneer and still relevant. Virology 479-480:310-30
Tso, Dan-ju; Hendrix, Roger W; Duda, Robert L (2014) Transient contacts on the exterior of the HK97 procapsid that are essential for capsid assembly. J Mol Biol 426:2112-29
Cardone, Giovanni; Duda, Robert L; Cheng, Naiqian et al. (2014) Metastable intermediates as stepping stones on the maturation pathways of viral capsids. MBio 5:e02067
Xu, Jun; Hendrix, Roger W; Duda, Robert L (2014) Chaperone-protein interactions that mediate assembly of the bacteriophage lambda tail to the correct length. J Mol Biol 426:1004-18
Oh, Bonnie; Moyer, Crystal L; Hendrix, Roger W et al. (2014) The delta domain of the HK97 major capsid protein is essential for assembly. Virology 456-457:171-8
Pope, Welkin H; Jacobs-Sera, Deborah; Russell, Daniel A et al. (2014) Genomics and proteomics of mycobacteriophage patience, an accidental tourist in the Mycobacterium neighborhood. MBio 5:e02145
Pietilä, Maija K; Laurinmäki, Pasi; Russell, Daniel A et al. (2013) Structure of the archaeal head-tailed virus HSTV-1 completes the HK97 fold story. Proc Natl Acad Sci U S A 110:10604-9
Duda, Robert L; Oh, Bonnie; Hendrix, Roger W (2013) Functional domains of the HK97 capsid maturation protease and the mechanisms of protein encapsidation. J Mol Biol 425:2765-81
Smith, Margaret C M; Hendrix, Roger W; Dedrick, Rebekah et al. (2013) Evolutionary relationships among actinophages and a putative adaptation for growth in Streptomyces spp. J Bacteriol 195:4924-35

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