Human glutaredoxin-1 catalyzes the reduction of HIV-1 gp120 and CD4 disulfides and its inhibition reduces HIV-1 replication

Reduction of intramolecular disulfides in the HIV-1 envelope protein gp120 occurs after its binding to the CD4 receptor. Protein disulfide isomerase (PDI) catalyzes the disulfide reduction in vitro and inhibition of this enzyme blocks viral entry. PDI belongs to the thioredoxin protein superfamily t...

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Veröffentlicht in:	The international journal of biochemistry & cell biology 2009-06, Vol.41 (6), p.1269-1275
Hauptverfasser:	Auwerx, Joeri, Isacsson, Ola, Söderlund, Johan, Balzarini, Jan, Johansson, Magnus, Lundberg, Mathias
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Catalysis Cattle CD4 Antigens - metabolism Disulfide reduction Disulfides - metabolism Glutaredoxin-1 Glutaredoxins - antagonists & inhibitors Glutaredoxins - metabolism Glutaredoxins - pharmacology Glutathione - metabolism HIV Envelope Protein gp120 - metabolism HIV-1 - metabolism HIV-1 - physiology HIV-1 gp120 Humans Naphthalenesulfonates - pharmacology Oxidation-Reduction Polymers - pharmacology Protein disulfide isomerase Protein Disulfide-Isomerases - metabolism Recombinant Proteins - pharmacology Thioredoxin-1 Virus Internalization - drug effects Virus Replication - drug effects Virus Replication - physiology
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