By Pooja Toshniwal PahariaSep 26 2022Reviewed by Aimee Molineux In a recent study published in PLoS Pathogens, researchers investigated the receptor tropism and serological cross-reactivity for spike protein receptor-binding domains from two clade 3 sarbecoviruses found in Russian Rhinolophus bats: Khosta-1 in Rhinolophus ferrumequinum and Khosta 2 in R.
About the study In the present study, researchers investigated host cell infection by Russian Rhinolophus bat sarbecoviruses’ S and their neutralization by monoclonal antibodies and vaccinated donor sera. The 293T ‘producer cells’ were lysed, and the lysates were subjected to Western blot analysis. To explore protein interactions between Khosta 2 and hACE2 in comparison with other clade 1 S RBDs, Khosta 2 RBD structure predictions were made based on previously published data, which was then aligned by multiple sequence alignment to ACE2-bound SARS-CoV-1 and SARS-CoV-2 co-structures for phylogenetic assessments.
Results and discussion The exogenous protease mediated Khosta-1 RBD entry into Huh-7 cells; however, protease addition did not facilitate Khosta-1 RBD entry in BHK cells transfected with several CoV receptors, indicating that trypsin-dependent Khosta-1 entry in Huh-7 cells did not depend on hACE2. Contrastingly, trypsin addition enhanced receptor-dependent entry signals for SARS-CoV-2 RBDs and Khosta 2 RBD, indicating that Khosta 2 RBDs utilized hACE2 receptors for cell infection.
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