College of Science and Health > Faculty & Staff > Faculty A-Z > Sarah Connolly

Sarah Connolly

Classes Taught
  • Microbiology (BIO 210)
  • General Biology I (BIO 191)
  • Molecular Virology (HLTH 320)
  • Health Research Literacy (HLTH 202)
  • Human Pathogens and Defense (HLTH 194)
  • Focal Point Seminar (LSP 112)- Ebolavirus: Biology, Public Health, and Ethics
Research Interests

The goal of Connolly's research is to understand how herpesviruses achieve the first step of infection: entering a host cell. Her lab is interested specifically in how proteins on the surface of the virus interact with each other and with cellular receptors to trigger fusion of the viral membrane that surrounds the virus with the cellular membrane. Dr. Connolly's work is also aimed at defining how the viral fusion protein physically refolds to force the membranes to merge. Her lab uses molecular biology, microbiology, cell biology and protein biochemistry techniques to study the model human herpesvirus, herpes simplex virus type 1.

Select Publications

Fan Q., Kopp SJ, Byskosh NC, Connolly SA, Longnecker R. Natural Selection of Glycoprotein B Mutations That Rescue the Small-Plaque Phenotype of a Fusion-Impaired Herpes Simplex Virus Mutant. MBio. 2018 Oct 16;9(5). 

Fan Q, Kopp SJ, Connolly SA, Longnecker R. Structure-Based Mutations in the Herpes Simplex Virus 1 Glycoprotein B Ectodomain Arm Impart a Slow-Entry Phenotype. MBIO. 2017 May 16;8(3).

Fan Q, Longnecker, R, Connolly SA. A Functional Interaction between Herpes Simplex Virus 1 Glycoprotein gH/gL Domains I and II and gD is Defined by Using Alphaherpesvirus gH and gL Chimeras. J Virol. 2015 July;89(14):7159-69

Lajko M, Haddad AF, Connolly SA. 2015. Using proximity biotinylation to detect herpesvirus entry glycoproteion interactions: Limitations for integral membrane glycoproteins. J Virol Methods. 221:81-9.

Fan Q, Longnecker R, Connolly SA. 2014. Substitution of herpes simplex virus 1 entry glycoproteins with those of saimiriine herpesvirus 1 reveals a gD-gH/gL functional interaction and a region within the gD profusion domain that is critical for fusion. J Virol. 88(11):6470-82.