Jana, Mrinmoy and Delipan, Rathina and Sarkar, Arighna and Raran-Kurussi, Sreejith and Ringe, Rajesh P and Mandal, Kalyaneswar (2025) Chemically synthesized LRAD3-D1 interacts with N-terminal domain of SARS-CoV-2 spike protein. Chembiochem, 26 (22). e202500403.
Full text not available from this repository.Abstract
Growing evidence of post-COVID neurological complications, such as encephalopathy, neurodegeneration, and cognitive impairment, suggests severe acute respiratory syndrome-related corona virus 2 (SARS-CoV-2) viral infection into the central nervous system (CNS). Therefore, understanding the mechanisms of viral entry into the CNS, where human angiotensin-converting enzyme 2 (ACE2) is barely expressed, is critical for addressing the neurological consequences of COVID-19. Importantly, the low-density lipoprotein receptor class A domain containing 3 (LRAD3) is overexpressed in brain cells, suggesting a possible ACE2-independent alternate pathway of viral entry into brain cells. Herein, the interaction of the chemically synthesized LRAD3 domains with SARS-CoV-2 spike protein is reported. It is observed that the extracellular domains of LRAD3 depend on calcium for proper folding and maintaining their structural integrity. The results reveal that domain 1 of LRAD3, which is most accessible from the cell surface, engages with the N-terminal domain of the viral spike protein. These findings open up possibilities to develop new therapeutic strategies targeting ACE2 independent viral entry pathways.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | LRAD3 ectodomain; SARS-CoV-2 entry; neurological disorders; peptide synthesis |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 01 Feb 2026 14:20 |
| Last Modified: | 01 Feb 2026 14:20 |
| URI: | http://crdd.osdd.net/open/id/eprint/3224 |
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