Publications at DePaul University
- 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
- 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
- Connolly SA, Jardetzky T, Longnecker R. 2021. The structural basis of herpesvirus entry. Nat Rev Microbiol. 19:110-121.
- Cairns TM and Connolly SA. 2021. Entry of Alphaherpesviruses. Curr Issues Mol Biol. 41:63-124. [Also published as Chapter 2 in 'Alphaherpesviruses: Molecular Biology, Host Interactions and Control', Heldwein EE and Smith GA, ed. (Caister Academic Press), pp. 41-102 (2020)].
- 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.
- 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.
- 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.
- 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.
- 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.
- 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. 88:6470-82.
- Zago A, Connolly SA, Spear PG, Longnecker R. 2013. The fusion loops and membrane proximal region of Epstein-Barr virus glycoprotein B (gB) can function in the context of herpes simplex virus 1 gB when substituted individually but not in combination. Virus Res. 171:227-30.
- Rowe CL, Connolly SA, Chen J, Jardetzky TS, Longnecker R. 2013. A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion. Virology. 436(1):118-26