PhD Scientific Days 2025

Poster Session II. - J: Theoretical and Translational Medicine

Interactions between the SARS-CoV-2 E protein and the SERCA regulatory system

Előadó neve

Ms. Berta Blanka

Neptun code

IWI1BX

Előadó munkahelye

Department of Biophysics and Radiation Biology

Előadó telefonszáma

06203489292

Előadó e-mail címe

blanka9707@gmail.com

Az előadás címe

Interactions between the SARS-CoV-2 E protein and the SERCA regulatory system

Szerző(k) neve és munkahelye

Blanka Berta¹, Rita Padányi¹, Hedvig Tordai¹, Gergely L. Lukács², Béla Papp³, Ágnes Enyedi^4,5, Tamás Hegedűs^1,5

1: Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary
2: Department of Physiology, McGill University, Montréal, Quebec, Canada
3: Inserm U976, Institut de Recherche Saint-Louis, Université de Paris, Department of Hemato- Immunology Research, DRF-Institut Francois Jacob, CEA, Hôpital Saint-Louis, Paris, France
4: Department of Transfusiology, Semmelweis University, Budapest, Hungary
5: ELKH-SE Biophysical Virology Research Group, Eötvös Loránd Research Network, Budapest, Hungary

Bemutatás módja

Poszter

Szekció

Poster Session II. - J: Theoretical and Translational Medicine

Language of the presentation

Hungarian

Preferred session

Theoretical and Translational Medicine

Összefoglaló szövege

Introduction
The SARS-CoV-2 coronavirus (COVID-19)-caused acute respiratory syndrome has emerged
as a major global threat. The smallest structural protein of the SARS-CoV-2 virus, the
envelope protein (E protein), regulates viral replication, but its exact role is not well
understood. E protein contains a single transmembrane (TM) helix and a disordered cytosolic
segment and it can function as monomer or can form homo-pentamer. Both the pentameric
and monomeric structures of E protein are similar to the regulator proteins of
sarco/endoplasmic reticulum calcium ATPase (SERCA).
Aims
This study aimed to investigate the interactions between the E protein and SERCA2b and its
regulator proteins (regulins: PLN, ALN, ELN), and to determine the functional consequences
of E protein expression on Ca²⁺ signaling in mammalian cells.
Method
Close interaction between E protein and SERCA2b and its regulins was investigated by
Acceptor Photobleaching-Förster Resonance Energy Transfer (AP-FRET) technique and co-
immunoprecipitation. Genetically encoded Ca²⁺ sensors were used to monitor Ca²⁺ levels in
the endoplasmic reticulum (ER) and cytosol.
Results
We detected the homo-oligomerization of the E protein and hetero-oligomerization between E
protein and all the regulins (PLN, ALN and ELN). FRET and co-immunoprecipitation results
showed the interaction of E protein and SERCA. E protein expression decreased the rate of
ER Ca²⁺ reload after depletion of the ER store, suggesting inhibition of SERCA activity.
Modified SERCA function also influenced cytosolic Ca²⁺ signaling, extending the duration
of the decay phase of the signal.
Conclusion
Our results reveal novel regulatory mechanisms in the virus-host interaction network,
indicating that E protein disrupts host Ca²⁺ homeostasis through its interaction with SERCA
and its regulators, which may play a critical role in viral pathogenesis.
Funding
NKFIH 127961 and 137610 ;TKP2021-EGA-23;NKFI-1-K137610
2024-1.2.3-HU-RIZONT-2024-00003

University

Semmelweis University

Supervisor

Dr. Padányi Rita

Publication of my abstract

I give consent to the publication of my abstract on the website of the congress.

phd.section.field

in doctoral studies after complex exam (PhD)

Kind

Szabad

Status

elfogadva

Accepted presentation method

poszter

Előadás fájl jóváhagyás

nem rendelkezett róla

Előadó

7436

Start

19:12

End

19:18