Legitimate and illegitimate cleavage of human immunodeficiency virus glycoproteins by furin.
Coexpression of human immunodeficiency virus type 1 glycoproteins with the subtilisin-like protease furin leads to processing of gp160 and gp140, a truncated form of gp160, to gp120. In addition, we show that gp120 itself is further cleaved by furin at sites near the primary cleavage site and within the V3 loop.
NERC Institute of Virology, Oxford, United Kingdom.
Y
Y
Morikawa
E
E
Barsov
I
I
Jones
D000595:Amino Acid Sequence; D045683:Furin; D015686:Gene Products, env / Q000235:genetics / Q000378:metabolism*; D015699:HIV Envelope Protein gp120 / Q000378:metabolism; D019302:HIV Envelope Protein gp160; D015497:HIV-1 / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D011498:Protein Precursors / Q000235:genetics / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000096:biosynthesis; D013381:Subtilisins / Q000235:genetics / Q000378:metabolism*
D015686:Gene Products, env; D015699:HIV Envelope Protein gp120; D019302:HIV Envelope Protein gp160; D011498:Protein Precursors; D011994:Recombinant Proteins; D013381:Subtilisins; D045683:Furin