Muñoz, MCoveñas, RKramer, M2023-01-252023-01-2520190001-723Xhttp://hdl.handle.net/10668/14496The human immunodeficiency virus (HIV) envelope, via a key extracellular amino acid sequence, may simulate the functionality of native undecapeptide substance P (SP) acting through the host's neurokinin 1 (SP preferring) receptor (NK-1R). Human monocytes and macrophages express both NK-1Rs and SP. In HIV/AIDS the NK-1R may function as a chemokine-like G-protein coupled co-receptor that: 1) fuses to the outer envelope of HIV; 2) enables intracellular entry of the envelope-capsid-NK-1R complex; 3) co-opts immune defence via its physiological interaction with the SP-like envelope; 4) may contribute to resistance of CD4/chemokine entry inhibitor type drugs; 5) relaxes the blood-brain barrier to support entry of the HIV into the central nervous system, and 6) mediates most of the common clinical sequelae of HIV/AIDS (encephalopathy and AIDS dementia complex). The data support the idea that NK-1R antagonists could be useful to treat HIV/AIDS. Keywords: human immunodeficiency virus; NK-1 receptor; NK-1 receptor antagonist; aprepitant; fusion protein; virus.enDipeptidesHIV Envelope Protein gp120HIV InfectionsHumansMacrophagesMonocytesNeurokinin-1 Receptor AntagonistsReceptors, Neurokinin-1Substance PViral Fusion Proteinsresearch article31507190open access10.4149/av_2019_302http://www.elis.sk/download_file.php?product_id=6274&session_id=5oii85bqi8ifp6dnba6ncmrv64