Study finds human surfactant protein A can inhibit SARS-CoV-2 infectivity Coronavirus Disease COVID Protein SARSCoV2 biorxivpreprint SUNY JohnsHopkins
By Bhavana KunkalikarApr 10 2023Reviewed by Benedette Cuffari, M.Sc. In a recent study posted to the bioRxiv* preprint server, researchers in the United States assess the efficacy of the human surfactant protein A against severe acute respiratory syndrome coronavirus 2 infectivity.
What is human SP-A? Human SP-A is a hydrophilic protein found on mucosal epithelial surfaces of the upper airway and lungs. This protein can bind to pathogen-associated molecular patterns of invading microbes. Herein, the competitive inhibition of SP-A recognition of RBD and S protein by sugars was examined by incubating SP-A with immobilized RBD and S protein with sugars. The team assessed whether there was a direct interaction between SP-A and ACE2. Furthermore, the impact of SP-A on RBD-human ACE2 interaction was examined by incubating them simultaneously on RBD-immobilized enzyme-linked immunosorbent assay plates.
Results SP-A showed dose-dependent binding to the SARS-CoV-2 S protein in the presence of calcium. However, the presence of ethylenediaminetetraacetic acid reduced the interaction between SP-A and S protein by 46%. This suggests that while SP-A and S protein binding was somewhat calcium-dependent, other non-calcium-dependent regions may also be involved in their interaction since EDTA was not able to completely eliminate SP-A and S protein binding.
Higher levels of maltose did not eliminate the interaction between SP-A and S protein and RBD. SP-A was also found to bind glycoconjugates on SARS-CoV-2 S protein and RBD. The observed interaction between proteins may occur irrespective of the presence or dosage of sugars, thus suggesting the possibility of other types of protein-protein interaction.
SP-A was also found to decrease hACE2 binding to RBD, whereas bovine serum albumin did not affect the interaction between RBD and hACE2. Thus, SP-A could disrupt the binding of RBD and hACE2.
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