Effect of ambient temperature on respiratory tract cells exposed to SARS-CoV-2 viral mimicking nanospheres—An experimental study
Artikel i vetenskaplig tidskrift, 2021

The novel coronavirus caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has reached more than 160 countries and has been declared a pandemic. SARS-CoV-2 infects host cells by binding to the angiotensin-converting enzyme 2 (ACE-2) surface receptor via the spike (S) receptor-binding protein (RBD) on the virus envelope. Global data on a similar infectious disease spread by SARS-CoV-1 in 2002 indicated improved stability of the virus at lower temperatures facilitating its high transmission in the community during colder months (December–February). Seasonal viral transmissions are strongly modulated by temperatures, which can impact viral trafficking into host cells; however, an experimental study of temperature-dependent activity of SARS-CoV-2 is still lacking. We mimicked SARS-CoV-2 with polymer beads coated with the SARS-CoV-2 S protein to study the effect of seasonal temperatures on the binding of virus-mimicking nanospheres to lung epithelia. The presence of the S protein RBD on nanosphere surfaces led to binding by Calu-3 airway epithelial cells via the ACE-2 receptor. Calu-3 and control fibroblast cells with S-RBD-coated nanospheres were incubated at 33 and 37 °C to mimic temperature fluctuations in the host respiratory tract, and we found no temperature dependence in contrast to nonspecific binding of bovine serum ablumin-coated nanospheres. Moreover, the ambient temperature changes from 4 to 40 °C had no effect on S-RBD-ACE-2 ligand-receptor binding and minimal effect on the S-RBD protein structure (up to 40 °C), though protein denaturing occurred at 51 °C. Our results suggest that ambient temperatures from 4 to 40 °C have little effect on the SARS-CoV-2-ACE-2 interaction in agreement with the infection data currently reported.

enzymes

viruses

epithelium

epithelial cells

binding protein

diseases and conditions

materials properties

protein structure

nanomaterials

Författare

Alexandra Paul

The University of Texas at Austin

Chalmers, Biologi och bioteknik, Kemisk biologi

Sachin Kumar

The University of Texas at Austin

Sayantani Chatterjee

Max Planck Institute for Polymer Research

Sabine Pütz

Max Planck Institute for Polymer Research

Natasha Nehra

The University of Texas at Austin

Daniel S. Wang

The University of Texas at Austin

Arsalan Nisar

The University of Texas at Austin

Christian M. Jennings

The University of Texas at Austin

Sapun H. Parekh

Max Planck Institute for Polymer Research

The University of Texas at Austin

Biointerphases

1559-4106 (ISSN) 1934-8630 (eISSN)

Vol. 16 011006

Ämneskategorier

Infektionsmedicin

Annan medicinsk grundvetenskap

Mikrobiologi inom det medicinska området

DOI

10.1116/6.0000743

Mer information

Skapat

2021-01-29