Elisabetta Battocchio

Curriculum vitae

Born on 11th November 1994, she has obtained the master’s degree in Pharmacy and Industrial Pharmacy at the University of Milan. She carried out her experimental internship at the “Mario Negri” Pharmacological Research Institue of Milan, in Dr Marco Gobbi’s Laboratory of Pharmacodynamics and Pharmacokynetics in order to elaborate the thesis entitled “Direct interaction between β-amyloid and Tau protein and the effects on the amyloid fibrils formation”.

This work period has allowed her to learn both the Surface Plasmon Resonance (SPR) and its applications in various fields and basic molecular techniques including ThT kinetic assay.

In 2019 she won a research fellowship at University of Milan Bicocca for the project “Characterization of autoantibody anti-monomeric amyloid versus oligomeric amyloid with Surface Plasmon Resonance in CSF of patients affected by cerebral amyloid angiopathy inflammation” in Dr Fabrizio Piazza’s laboratory of CAA and AD Traslational Research and Biomarkers, becoming member of the Inflammatory Cerebral Amyloid Angiopathy and Alzheimer’s Disease Biomarkers (iCAB) International Network.

From november 2020 she’s a PhD student in Experimental Neuroscience at University of Milan Bicocca, in collaboration with Neuroscience Institute of Research National Centre. She is working in Dr.ssa Claudia Verderio’s laboratory of Cell-to-cell signaling in brain, under the supervision of both Dr.ssa Claudia Verderio and Prof Giulio Sancini.

PhD Project

Exploring molecular interactors mediating motion of glial extracellular vescicles (EVs) carrying pathogenic misfolded proteins at the neuron surface

  • Curriculum: Neuroscienze sperimentali
  • Tutor: Prof. Giulio Alfredo Sancini   Cotutor: Dr.ssa Claudia Verderio

Extracellular vesicles (EVs) are circular membrane fragments which function as intercellular signalling vehicles. They transfer bioactive cargoes influencing both the behaviour of the target cells and the surrounding environment.

In the brain, accumulating evidences indicates that glial cells communicate with neurons through secretion of EVs and in the diseased brain EVs become vehicle of pathogenic molecules, including misfolded proteins, such as β-amyloid and Tau protein, associated with neurodegeneration. Moreover, data from the lab I am working in show that microglial large EVs (>200 nm in diameter) carrying Aβ efficiently move extracellularly along axonal processes spreading synaptic dysfunctions in the mouse brain. In addition, EVs isolated from CSF of AD patients have been found to propagate tau pathology after injection in mouse brain.

The aim of my PhD project is to investigate the molecular mechanisms underlying large EV extracellular motion at the neuron surface.

To do this, three different aspects will be investigated: i) proteomic analysis of surface proteins in EVs released from microglia exposed to Aβ and/or Tau protein, ii) analysis of estracellular motion of these EVs on neurons lacking candidate EV receptors and iii) analysis of the impact of these EVs on dendritic spine morphology.

Primary cultures of neurons and microglia will be used and optical manipulation experiments combined with time-lapse imaging will be employed in order to study EV-neuron interaction dynamics and EV effects on dendritic spine morphology after placing single EVs in contact with the neuronal surface. Finally, neurons lacking candidate receptors for the EVs will be used in order to investigate the binding partners of EVs on neurons surface.

Hopefully this study will pave the way to novel therapeutic strategies to limit the spreading of synaptic dysfunciton and neurodegenerative processes in Alzheimers’ Disease.

Congresses and workshops

  • SINdem 2020 – Firenze, 12-14 marzo 2020
  • Alzheimer’s Association International Conference 2020 – 26-30 luglio 2020
  • Congresso Scientifico Annuale AISM 2020 – 27 novembre 2020
  • NeuroMI 2020 virtual annual meeting – 18 dicembre 2020


  • Beeg, M., Battocchio, E., et al. (2021). Nonphosphorylated tau slows down Aβ1-42 aggregation, binds to Aβ1-42 oligomers, and reduces Aβ1-42 toxicityJournal of Biological Chemistry, 296(15), 100664. https://doi.org/10.1016/j.jbc.2021.100664

Further info