Phone: (205) 348-0310
Carol Duffy received a Ph.D. in Microbiology from the University of Iowa in 2000 and completed her postdoctoral research at Cornell University. She was appointed Assistant Professor at the University of Alabama in 2007.
My research interests lie in elucidating the mechanisms used by herpes simplex virus type 1 (HSV-1) to replicate within its host. The herpesviruses have been co-evolving with their hosts for millions of years, and have consequently developed elaborate mechanisms for replication and evasion of their hosts’ defense systems. HSV-1 is a neurotropic herpesvirus that infects ~80% of young adults worldwide. Infection of its human host is initiated with a lytic infection of the mucosal epithelium and continues through invasion of the peripheral nervous system that usually leads to establishment of a reactivatable latent infection. On occasion, HSV-1 spreads to the central nervous system, causing the most common type of sporadic viral encephalitis seen in western countries. In addition, HSV-1 can infect the corneal epithelium, causing a disease known as herpes simplex keratitis that often results in vision damage.
HSV-1 contains a structure unique to all herpesviruses called the tegument, which is composed of 20+ viral and cellular proteins packaged into virions between the capsid and envelope. Tegument proteins play a variety of roles in infection including the regulation of viral and host gene expression and the promotion of virus assembly and egress. Many tegument proteins are synthesized late in infection at the time of virus assembly. Upon infection, both the genome-containing capsid and the tegument proteins are released into the host cell. Thus tegument proteins can potentially exert their activities at both very early times prior to viral gene expression, and late times when they are produced in high amounts.
Studies in my lab focus on determining the roles of the various tegument proteins during HSV-1 replication and the mechanisms by which those roles are carried out. To this end, we utilize techniques in genetics, molecular biology, cell biology, biochemistry, microscopy, genomics, and proteomics. HSV-1 provides an excellent research system due to its short replication cycle and ease of culture. In addition there are a large number of available mutant HSV-1 strains, and with the development of the HSV-1 Bacterial Artificial Chromosome system, new mutants are easily designed and generated.
Duffy, C., E.F. Mbong, and J.D. Baines. VP22 of Herpes Simplex Virus 1 Promotes Protein Synthesis at Late Times in Infection and Accumulation of a Subset of Viral mRNAs at Early Times in Infection. Journal of Virology. 83:1009-1017, 2009.
Duffy, C., J.H. LaVail, A.N. Tauscher, E.G. Wills, J.A. Blaho, and J.D. Baines. Characterization of a UL49-null Mutant: VP22 of Herpes Simplex Virus 1 Facilitates Viral Spread in Cultured Cells and the Mouse Corneal Epithelium. Journal of Virology. 80:8664-75, 2006.
J.D. Baines and C. Duffy. Nucleocapsid Assembly and Envelopement of Herpes Simplex Virus. In: Alpha Herpesviruses: Molecular and Cellular Biology. (Ed. R.M. Sandri-Goldin). Pp. 175-204. Caister Academic Press: Norfolk, UK.
Beard, P.M., C. Duffy, and J.D. Baines. Quantification of the DNA Cleavage and Packaging Proteins UL15 and UL28 in A and B Capsids of Herpes Simplex Virus Type 1. Journal of Virology. 78:1367-1374, 2003.
Duffy, C., S. Phillips, and A. Klingelhutz. Microarray Analysis Identifies Differentiation-Associated Genes Regulated by Human Papillomavirus Type 16 E6. Virology. 314:196-205, 2003.
de Beer T., J. Meyer, M. Ortega, Q. Yang, L. Maes, C. Duffy, N. Berton, J. Sippy, M. Overduin, M. Feiss, and C. Catalano. Insights into Specific DNA Recognition During Assembly of a Viral Genome Packaging Machine; Structure and Genetics of the DNA Binding Domain of gpNu1. Molecular Cell. 9:981-991, 2002.
Duffy, C. and M. Feiss. The Large Subunit of Bacteriophage ?’s Terminase Plays a Role in DNA Translocation and Packaging Termination. Journal of Molecular Biology. 316:547-561, 2002.
Hwang Y., J.Q. Hang, J. Neagle, C. Duffy, and M. Feiss. Endonuclease and Helicase Activities of Bacteriophage ? Terminase: Changing Nearby Residue 515 Restores Activity to the gpA K497D Mutant Enzyme. Virology. 277:204-214, 2000.