A hydrophilic protein called human SP-A is present on the mucosal epithelial surfaces of the lungs and upper airways. The pathogen-associated molecular patterns (PAMPs) of encroaching microorganisms can bind to this protein.
According to an in silico investigation, SP-A may have a comparable affinity to the SARS-CoV-2 spike protein as the angiotensin-converting enzyme 2 (ACE2)-spike interaction, which may have an effect on how the SARS-CoV-2 infection progresses. Global efforts are being made to create and improve immunomodulatory and antiviral medications as a result of the ongoing evolution of SARS-CoV-2 variations, which endanger the efficacy of emerging coronavirus vaccines and therapies (COVID-19).
Concerning the study
In the current work, scientists examine whether SP-A can interact with the receptor-binding domain (RBD), ACE2, and SARS-CoV-2 spike in human cells.
The competitive suppression of by incubating SP-A with immobilized RBD and S protein along with sugars, the SP-A recognition of RBD and S protein by sugars was investigated. The group evaluated whether SP-A and ACE2 had a direct relationship. By simultaneously incubating RBD and human ACE2 (hACE2) on ELISA plates with RBD immobilized, the effect of SP-A on this interaction was also investigated.
Pseudotyped particles and the contagious SARS-CoV-2 Delta variant were used to evaluate SP-potential A’s to reduce SARS-infectiousness. CoV-2’s Furthermore tested was SP-capacity A’s to bind RBD and S protein and thereby prevent viral entrance.
Tests were done to establish SP-contribution A’s to the SARS-CoV-2 Delta variant’s infectivity, binding, and entrance. Moreover, salivary SP-A levels are samples of COVID-19 patients who were hospitalized with different levels of disease severity were also determined.
