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

Sarah Connolly

Classes Taught

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

Research Interests

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

Select Publications

  • Fan Q, Hippler DH, Yang Y, Longnecker R, Connolly SA. 2023. Multiple sites on glycoprotein H (gH) functionally interact with the gB fusion protein to promote fusion during herpes simplex virus (HSV) entry. mBio. 14:e0336822. doi: 10.1128/mbio.03368-22
  • Fan Q, Longnecker R, Connolly SA. 2021. Herpes simplex virus glycoprotein B (gB) mutations define structural sites in domain I, the membrane proximal region, and the cytodomain that regulate entry. J Virol. 95:e0105021. doi: 10.1128/JVI.01050-21
  • Connolly SA, Jardetzky T, Longnecker R. 2021. The structural basis of herpesvirus entry. Nat Rev Microbiol. 19:110-121. doi: 10.1038/s41579-020-00448-w
  • Cairns TM and Connolly SA. 2021. Entry of Alphaherpesviruses. Curr Issues Mol Biol. 41:63-124. doi: 10.21775/cimb.041.063
  • Fan Q, Kopp SJ, Byskosh NC, Connolly SA, Longnecker R. 2018. Natural selection of glycoprotein B mutations that rescue the small-plaque phenotype of a fusion-impaired herpes simplex virus mutant. mBio. 9:5. doi: 10.1128/mBio.01948-18
  • Fan Q, Kopp SJ, Connolly SA, Longnecker R. 2017. Structure-based mutations in the herpes simplex virus type 1 (HSV-1) glycoprotein B ectodomain impart a slow phenotype. mBio. 8:3. doi: 10.1128/mbio.00614-17
  • Fan Q, Kopp SJ, Connolly SA, Muller WJ, Longnecker R. 2017. Mapping sites of herpes simplex virus type 1 glycoprotein D that permit insertions and impact gD and gB receptors usage. Sci Rep. 7:43712. doi: 10.1038/srep43712
  • Lajko M, Haddad AF, Robinson CA, Connolly SA. 2015. Using proximity biotinylation to detect herpesvirus entry glycoprotein interactions: limitations for integral membrane glycoproteins. J Virol Methods. 221:81-89. doi10.1016/j.jviromet.2015.04.031
  • Fan Q, Longnecker R, Connolly SA. 2015. A functional interaction between herpes simplex virus 1 glycoproteins gH/gL domains I-II and gD is defined using α-herpesvirus gH and gL chimeras. J Virol. 89:7159-69. doi10.1128/JVI.00740-15