OmniVira

Little Brown Bats (Myotis lucifugus) 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.
PMID37243189 DOI10.3390/v15051103 Year2023 Journal Viruses Languageeng Statusepublish

Abstract

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.

Supporting text Virus Host Location
ACE2 54 coronaviruses 32 little brown bat 1 SARS-CoV-2 550 Chiroptera 371 COVID-19 425 Angiotensin-Converting Enzyme 2 177 Animals 1948 Humans 1440 SARS-CoV-2 453 Spike Glycoprotein, Coronavirus 274 spike protein, SARS-CoV-2 157

Evidence records

2 total
Zoonotic Surveillance
1 records · 1 evidence types
Evidence type Reservoir Ecology
1 records
OVE7013 Reservoir Ecology
Key finding

Little brown bats (Myotis lucifugus) could be at risk of SARS-CoV-2 infection and may serve as a natural reservoir in North America.

Virus
Severe acute respiratory syndrome coronavirus 2
Host
little brown bat Myotis lucifugus Natural host
Location
North America
Supporting text

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.

Method
in vitro binding assays | in silico molecular dynamics simulations
Geographic raw
North America
Functional Mechanism
1 records · 1 evidence types
Evidence type Receptor Usage
1 records
OVE7011 Receptor Usage
Key finding

Little brown bat ACE2 and TMPRSS2 mediate SARS-CoV-2 spike binding, indicating receptor compatibility.

Virus
Severe acute respiratory syndrome coronavirus 2
Host
little brown bat Myotis lucifugus Experimental system
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.

Method
in vitro binding assay | molecular dynamics simulation
Receptors
angiotensin-converting enzyme 2
Host factors
transmembrane serine protease 2