Literature detail

Little Brown Bats (<i>Myotis lucifugus</i>) Support the Binding of SARS-CoV-2 Spike and Are Likely Susceptible to SARS-CoV-2 Infection.

Shubhada K Chothe1,2 Padmaja Jakka1,2 Veda Sheersh Boorla3 Santhamani Ramasamy1,2 Abhinay Gontu1,2 Ruth H Nissly1,2 Justin Brown1,4 Gregory Turner4 Brent J Sewall5 DeeAnn M Reeder6 Kenneth A Field6 Julie B Engiles7 Saranya Amirthalingam1 Abirami Ravichandran1 Lindsey LaBella1,2 Meera Surendran Nair1,2 Costas D Maranas3 Suresh V Kuchipudi1,2
Affiliations 7 institutions
  1. Animal Diagnostic Laboratory, Department of Veterinary and Biomedical Sciences, The Pennsylvania State University, University Park, PA 16802, USA.
  2. Center for Infectious Disease Dynamics, Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, PA 16802, USA.
  3. Department of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802, USA.
  4. Pennsylvania Game Commission, 2001 Elmerton Ave, Harrisburg, PA 17110, USA.
  5. Department of Biology, Temple University, Philadelphia, PA 19122, USA.
  6. Department of Biology, Bucknell University, Lewisburg, PA 17837, USA.
  7. Departments of Pathobiology and Clinical Studies, New Bolton Center, School of Veterinary Medicine, University of Pennsylvania, Kennett Square, PA 19348, USA.
PMID 37243189 2023 Viruses eng epublish
PubMed DOI Browse context

Article

Publication summary

Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), believed to have originated from a bat species, can infect a wide range of non-human hosts. Bats are known to harbor hundreds of coronaviruses capable of spillover into human populations. Recent studies have shown a significant variation in the susceptibility among bat species to SARS-CoV-2 infection. We show that little brown bats (LBB) express angiotensin-converting enzyme 2 receptor and the transmembrane serine protease 2, which are accessible to and support SARS-CoV-2 binding. All-atom molecular dynamics (MD) simulations revealed that LBB ACE2 formed strong electrostatic interactions with the RBD similar to human and cat ACE2 proteins. In summary, LBBs, a widely distributed North American bat species, could be at risk of SARS-CoV-2 infection and potentially serve as a natural reservoir. Finally, our framework, combining in vitro and in silico methods, is a useful tool to assess the SARS-CoV-2 susceptibility of bats and other animal species.

ACE2 coronaviruses little brown bat SARS-CoV-2 Chiroptera COVID-19 Angiotensin-Converting Enzyme 2 Animals Humans SARS-CoV-2 Spike Glycoprotein, Coronavirus spike protein, SARS-CoV-2

Structured evidence records

Evidence records

2 total
1 records
Extraction confidence 0.90
Key finding

Little brown bat ACE2 and TMPRSS2 support SARS-CoV-2 spike binding, suggesting that this bat species could be susceptible to SARS-CoV-2 infection.

Virus
Location
Not specified
Supporting text

We show that little brown bats (LBB) express angiotensin-converting enzyme 2 receptor and the transmembrane serine protease 2, which are accessible to and support SARS-CoV-2 binding. All-atom molecular dynamics simulations revealed that LBB ACE2 formed strong electrostatic interactions with the RBD similar to human and cat ACE2 proteins.

Method
binding assay; molecular dynamics simulation
Experimental system
in vitro cell culture
1 records
Extraction confidence 0.95
Key finding

Little brown bats express ACE2 and TMPRSS2 that support SARS-CoV-2 spike binding and exhibit ACE2-RBD interactions similar to human and cat ACE2, indicating receptor compatibility for viral entry.

Virus
Location
Not specified
Supporting text

We show that little brown bats (LBB) express angiotensin-converting enzyme 2 receptor and the transmembrane serine protease 2, which are accessible to and support SARS-CoV-2 binding. All-atom molecular dynamics simulations revealed that LBB ACE2 formed strong electrostatic interactions with the RBD similar to human and cat ACE2 proteins.

Method
molecular dynamics simulation; in vitro binding assay
Receptors
ACE2
Host factors
TMPRSS2