PMC:7278327 / 5077-8295 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7278327","sourcedb":"PMC","sourceid":"7278327","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7278327","text":"The Case for a Functional Association of SARS-CoV-2-and nAChR in the Pathophysiology of COVID-19\nSeveral empirical studies have demonstrated that the nAChR represents a major receptor for the RABV that mechanistically drives CNS transport of infective viral particles, leading to classic neurological sequelae associated with disease progression [15–17]. Due to the efficient neuroinvasive properties of RABV [18,19], including the ability to bypass the blood-brain barrier, studies have used RABV-based vectors for the delivery of drugs to the CNS, with some success [20]. Furthermore, genetic engineering of the RABV has been employed to generate novel vaccines consisting of non-replicating RABV particles expressing chimeric capsid proteins containing human immunodeficiency virus 1 (HIV-1) [21,22], MERS-CoV, Ebolavirus, and hepatitis C virus (HCV) sequences [23–25].\nIn light of the above, a similar mechanism may underlie the multiple neurological effects of SARS-CoV-2 infection within the CNS. Patients with COVID-19 commonly present with sensory neurological symptoms that include anosmia and/or loss of taste. It has been proposed that the olfactory epithelium within the nasal cavity represents an early-stage locus for SARS-CoV-2 infection and replication, as reflected by ACE2 expression by a variety of non-neuronal cell types [9], followed by orthograde transport within the primary olfactory pathway into CNS structures [12]. Additionally, CNS entry of SARS-CoV-2/nAChR complexes may involve retrograde transport from peripheral trigeminal sensory terminal structures located within the olfactory epithelium [13,14,26,27]. Interestingly, similar lines of empirical evidence support a mechanism for RABV infection within the CNS via retrograde transport of RABV/nAChR complexes from sensory terminals of trigeminal ganglia [28,29], trigeminal nerve terminals within the olfactory epithelium, or primary olfactory neurons [30].\nFrom a biochemical perspective, a conserved nAChR-binding motif within the primary amino acid sequences of the RABV glycoprotein, HIV-1 gp120, and snake venom neurotoxins has been observed [31–33]. The HIV-1 envelope, gp120, has been reported to induce neuropathological changes similar to those in patients with HIV-1-associated neurocognitive disorders and triggers an upregulation of the α7-nAChR [34]. Importantly, snake venom toxins have been demonstrated to be high-affinity competitive antagonists of the nAChR. Sequence analysis of the SARS-CoV-2 spike protein identified homologous regions of 4-5 amino acids with aligned sequences in alpha-bungarotoxin and alpha-cobratoxin, thereby suggesting potential binding affinity and antagonism of the α7-nACh receptor [11]. Sequence homologies between putative nAChR-binding domains within the SARS-CoV-2 spike protein and HIV-1 gp120 have yet to be determined, although there are recent indications for shared CNS comorbidities [35]. In sum, convergent lines of evidence presented here support the potential construction and testing of novel homologous vaccines employing non-replicating RABV particles expressing chimeric capsid proteins containing antigenic sequences from SARS-CoV-2 spike protein and RABV 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