Gabriella Campadelli-Fiume

Gabriella Campadelli-Fiume is a virologist with a primary research focus on herpes simplex virus, fusion and viral entry. She is a retired professor of virology from the University of Bologna, Italy. Her specialization in virology was also completed at the University of Bologna.

Additional contributions to virology Gabriella Campadelli-Fiume took part in a study showing that glycoproteins gD, gB, and gH/gL permit herpes virus to enter cells and were involved in fusion. Their research indicated that gD is not required for the interactions between the glycoproteins gB and gH/gL. Rather, their interactions are made possible due to the multiple sites carried by gB. The multiple sites of gB can be found in the pleckstrin-domain that carries the bipartite fusion loop, and interaction with gH/gL can take place successfully without gD.

Influence Women have made significant progress towards equality within scientific fields of work. However, as efforts to increase women's participation in science fields, inequality exists. Furthermore, an underrepresented group of women remain in these fields. Campadelli-Fiume is an influential woman who continues to bridge the gender gap within the scientific community. Her achievements throughout her career have earned substantial amounts of attention and credible recognition globally. As the author of an overall encyclopedic of basic virology and clinical manifestations, Human Herpesviruses, her work has been included in the University of Pennsylvania’s 2007 Celebration of Women Writers. She has gained recent attention for laudable women in science by the International Society of Antiviral Research (ISAR) that has featured her as a prominent woman scientist. The American Academy of Microbiology awarded recognition of her scientific achievement and her contributions to advanced microbiology.

Editorial activity

(2005–Present) Serves as an editorial board member for the Journal of Virology ''

Major publications

Preclinical therapy of disseminated HER-2+ ovarian and breast carcinomas with a HER-2-retargeted oncolytic herpesvirus

Herpes Simplex Virus Glycoproteins gH/gL and gB Bind Toll-Like Receptor 2, and Soluble gH/gL Is Sufficient To Activate NF-κB

Herpes Simplex Virus gD Forms Distinct Complexes with Fusion Executors gB and gH/gL in Part through the C-terminal Profusion Domain

Construction of a Fully Retargeted Herpes Simplex Virus 1 Recombinant Capable of Entering Cells Solely via Human Epidermal Growth Factor Receptor 2

Herpes Simplex Virus gD Forms Distinct Complexes with Fusion Executors gB and gH/gL in Part through the C-terminal Profusion Domain

Intracellular Trafficking and Maturation of Herpes Simplex Virus Type 1 gB and Virus Egress Require Functional Biogenesis of Multivesicular Bodies

A Herpes Simplex Virus Recombinant That Exhibits a Single-Chain Antibody to HER2/neu Enters Cells through the Mammary Tumor Receptor, Independently of the gD Receptors

Heptad Repeat 2 in Herpes Simplex Virus 1 gH Interacts with Heptad Repeat 1 and Is Critical for Virus Entry and Fusion

Hydrophobic α-Helices 1 and 2 of Herpes Simplex Virus gH Interact with Lipids, and Their Mimetic Peptides Enhance Virus Infection and Fusion

The Egress of Herpesviruses from Cells: the Unanswered Questions

The Ectodomain of Herpes Simplex Virus Glycoprotein H Contains a Membrane α-Helix with Attributes of an Internal Fusion Peptide, Positionally Conserved in the Herpesviridae Family

Coexpression of UL20p and gK Inhibits Cell-Cell Fusion Mediated by Herpes Simplex Virus Glycoproteins gD, gH-gL, and Wild-Type gB or an Endocytosis-Defective gB Mutant and Downmodulates Their Cell Surface Expression

Entry of Herpes Simplex Virus Mediated by Chimeric Forms of Nectin1 Retargeted to Endosomes or to Lipid Rafts Occurs through Acidic Endosomes