Inhibition of the retroviral HIV-proteinase impairs maturation to infectious human immunodeficiency virus (HIV).
Newly developed inhibitors block the aspartic-type retroviral proteinase of the human immunodeficiency virus (HIV) at nanomolar concentration. The viral proteinase is responsible for the processing of viral encoded proteins. Applied to HIV infected cell culture, these inhibitors exhibit antiviral effects. The detailed analysis of these antiviral effects demonstrated that the synthesis of viral particles is only minimally decreased while the rate of infectious HIV particles is substantially reduced. The lack of infectivity is due to a failure in particle maturation which again is caused by the inhibition of the viral proteinase.
Nitschko
H
H
Max-von-Pettenkofer Institute, University of Munich, FRG.
Schätzl
H
H
Gelderblom
H R
HR
Oswald
M
M
von der Helm
K
K
D000998:Antiviral Agents / Q000494:pharmacology; D004151:Dipeptides / Q000494:pharmacology; D006678:HIV / Q000187:drug effects* / Q000254:growth & development / Q000502:physiology; D016655:HIV Core Protein p24 / Q000096:biosynthesis; D017320:HIV Protease Inhibitors; D014779:Virus Replication / Q000187:drug effects
D000998:Antiviral Agents; D004151:Dipeptides; D016655:HIV Core Protein p24; D017320:HIV Protease Inhibitors; C071114:EMD 57464