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.

Education and research Gabriella Campadelli-Fiume completed her doctorate of science (Sc.D.) at the University of Bologna, Italy. Her specialization in virology was also completed at the University of Bologna. Campadelli-Fiume primarily researches Herpes simplex virus (HSV), particularly how it enters, assembles, and exits the cell during an infection. In addition, she is interested in how HSV is induced to enter the exocytic pathway.

Primary focus

HSV entry into the cell Viral assembly in cell HSV exit out of the cell Viral induced alteration of exocytic pathway

Herpes simplex virus research Campadelli-Fiume's research primarily focuses on the entry mechanisms of both Herpes simplex virus 1 (HSV-1) and Herpes simplex virus 2 (HSV-2). Her work on these Group I double-stranded DNA viruses has centered on how they interact with host cell receptors to initiate infection.

Specifically, her laboratory investigated the roles of specific viral glycoproteins, such as gD, gB, and the gH/gL complex—which are highly conserved across the Alphaherpesvirinae subfamily and serve as the core machinery for viral entry and cell-to-cell fusion.

Major discoveries Campadelli-Fiume's discovered that nectin is the host cell receptor for HSV. She also discovered the triggering activity of receptor- bound gD. In addition to these major discoveries, she identified the gF profusion domain, which provided the first evidence that retargeted HSVs exert anti-tumor activity.

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. Campadelli’s profound research, leadership principles, scientific achievements, and passion for virology, continue to convey a powerful impression to those within the scientific community. Her influence as a female scientist plays an important role to increasing the status of women in research.

Leadership Gabriella Campadelli-Fiume is an active member and leader in the scientific community.

Awards

Accademia Nazionale dei Lincei, 2002 Pasteur Institute, Athens 1997 Fellowship in the American Academy of Microbiology

Editorial activity

(2005–Present) Serves as an editorial board member for the Journal of Virology (2013–Present) Serves as an editorial board member for the Federation of European Microbiological Societies (FEMS) of Pathogens and Disease Serves on the International Advisory Board for The Lancet Journal

Scientific society and academy founder

European Society for Virology Founding Member & Executive Board Member European Academy of Microbiology Founding Member Italian Society of Virology Founding Member

Committee service

European Research Council DGXII Health Commissions Italian Ministry of Health Member of Health Research Committee from 2000-2006'

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

AlphaV-beta3-Integrin Relocalizes nectin1 and Routes Herpes Simplex Virus to Lipid Rafts

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

The Herpes Simplex Virus JMP Mutant Enters Receptor-Negative J Cells through a Novel Pathway Independent of the Known Receptors nectin1, HveA, and nectin2

References