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Genomic Surveillance Detection of SARS-CoV-1–Like Viruses in Rhinolophidae Bats, Bandarban Region, Bangladesh
Christopher Bradburne
1
, Ausraful Islam
1, Ian Bird, Elliott Abbott, Sarah Harrison, Morgan Chunn, Diana Radune, Md Rakib Hasan, Brian Janes, Sean Lovett, John Lagergren, Timothy O’Hanlon, Konad Debnath, Clifton McKee, Mohammad Enayet Hossain, Molly Gallagher, Daniel Jacobson, Mohammed Ziaur Rahman, Katie Caviness, Raina K. Plowright, and Emily S. Gurley
Author affiliation: Johns Hopkins Applied Physics Laboratory, Laurel, Maryland, USA (C. Bradburne, I. Bird, S. Harrison, M. Chunn, T. O’Hanlon, M. Gallagher); icddr,b, Dhaka, Bangladesh (A. Islam, M.R. Hasan, K. Debnath, M.E. Hossain, M.Z. Rahman); National Bioforensic Analysis Center, National Biodefense Analysis and Countermeasures Center, Fort Detrick, Maryland, USA (E. Abbott, D. Radune, B. Janes, S. Lovett, K. Caviness); Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA (J. Lagergren, D. Jacobson); Johns Hopkins University Bloomberg School of Public Health, Baltimore, Maryland, USA (C. McKee, E.S. Gurley); College of Veterinary Medicine, Cornell University, Ithaca, New York, USA (R.K. Plowright)
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Figure 2

Figure 2. Binding efficiency and fold change of SARS-CoV-1–like virus viruses in Rhinolophidae bats, Bandarban Region, Bangladesh. A) Heatmap depicting binding efficiency of receptor binding domain (RBD) sequences from B4 and regional bridging hosts. The map shows that derived B4 RBD has low-to-moderate binding efficiency to angiotensin converting enzyme 2 (ACE2) sequences from regional bridging hosts. B) Fold change of coronavirus RBDs including derived B4 to human ACE2, relative to wild-type virus (horizontal dotted line). B4, samples from bat 4; CoV, coronavirus.
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