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.

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. 2015. 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. 89(14):7159-69. 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. Connolly SA and Longnecker R. 2012. Residues within the C-terminal arm of herpes simplex virus glycoprotein B contribute to its refolding during the fusion step of virus entry. J Virol. 86:6386-93.