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(Received for publication, July 24, 1996)
From the The human immunodeficiency virus HIV envelope
glycoprotein gp160 is synthesized as an inactive precursor, which is
processed into its fusiogenic form gp120/gp41 by host cell proteinases
during its intracellular trafficking. Kexin/subtilisin-related
endoproteases have been proposed to be enzyme candidates for this
maturation process. In the present study, 1) we examined the ability of
partially purified precursor convertases and their isoforms to cleave
gp160 in vitro. The data demonstrate that all the
convertases tested specifically cleave the HIV envelope glycoprotein
into gp120 and gp41. 2) We demonstrated that a 19-amino acid model
peptide spanning the gp120/gp41 junction is cleaved by all convertases
at the same gp160 site as that recognized in HIV-infected cells. 3) In
an effort to evaluate specific convertase inhibitors, we showed that the
Volume 271, Number 48,
Issue of November 29, 1996
pp. 30442-30450
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
,
,
and
Laboratoire de Chimie Physique des
Macromolécules aux Interfaces, CP206/2, Université libre de
Bruxelles, 1050, Brussels, Belgium, the ¶ Institute of Industrial
Chemistry, University of Padua, 35131-Padua, Italy, and the
Laboratory of Peptide Metabolism and Structure, and the
§ Laboratory of Biochemical Neuroendocrinology, Clinical
Research Institute of Montreal, 110 Pine Avenue West, Montréal,
Québec H2W 1R7, Canada
1-antitrypsin variant,
1-PDX,
inhibits equally well the ability of the tested convertases to cleave
gp160 in vitro. 4) Three lymphocyte cell lines were
screened by reverse transcription polymerase chain reaction in an
effort to identify which are the convertases expressed in the most
common HIV target, the CD4+ lymphocytes. The data
demonstrate that furin, PC5/6, and the newly cloned PC7 are the main
transcribed convertases, suggesting that these proteinases are the
major gp160-converting enzymes in T4 lymphocytes.
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