Comparative functional role of PC7 and furin in the processing of the HIV envelope glycoprotein gp160. NLM AIDSLINE Important note: Information in this article was accurate in 1997. The state of the art may have changed since the publication date.

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Comparative functional role of PC7 and furin in the processing of the HIV envelope glycoprotein gp160.

FEBS Lett. 1997 Mar 17;405(1):68-72. Unique Identifier : AIDSLINE MED/97248198
Decroly E; Benjannet S; Savaria D; Seidah NG; J.A. DeSeve Laboratory of Biochemical Neuroendocrinology, University; of Montreal, QC, Canada.

Abstract: The intracellular proteolytic processing of HIV envelope glycoprotein gp160 into gp120/gp41 is an essential step for virus infectivity. Several convertases, belonging to the pro-protein convertase family, have been proposed as candidate gp160 processing enzymes. Here we demonstrate using RT-PCR that resting human T4 lymphocytes weakly express PC7, furin, and PC5 mRNA whereas lymphocytes activated under conditions favoring HIV replication express 5-10-fold higher levels of furin and PC7. In this report, we examined the capability of the newly cloned convertase PC7 to cleave gp160 into gp120/gp41 and compared it to furin. This was carried out in a cell-based assay whereby both gp160 and the cognate convertase were co-expressed in the constitutively secreting BSC40 cells and in the regulated AtT20 cells, as well as using two in vitro assays which examined the cleavage of gp160 or of a synthetic peptide spanning the cleavage site. The data demonstrate that PC7 can cleave specifically and in a cell-type specific manner gp160 into gp120gp41, suggesting that both furin and PC7 are so far the major PC-like candidate gp160 convertase in T4 lymphocytes.
Keywords: *HIV Envelope Protein gp160/METABOLISM *Protein Processing, Post-Translational *Subtilisins/METABOLISMKWDhivenvelopeproteingp160/metabolismKWDproteinprocessing,post-translationalKWDsubtilisins/metabolism
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Copyright © 1997 - National Library of Medicine. Reproduced under license with the National Library of Medicine, Bethesda, MD.

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