TY - JOUR
T1 - A Conserved Subtilisin-like Protein TgSUB1 in Microneme Organelles of Toxoplasma gondii
AU - Miller, Steven A.
AU - Binder, Emily M.
AU - Blackman, Michael J.
AU - Carruthers, Vern B.
AU - Kim, Kami
PY - 2001/11/30
Y1 - 2001/11/30
N2 - Proteolytic processing plays a significant role in the process of invasion by the obligate intracellular parasite Toxoplasma gondii. We have cloned a gene, TgSUB1, encoding for a subtilisin-type serine protease found in T. gondii tachyzoites. TgSUB1 protein is homologous to other Apicomplexan and bacterial subtilisins and is processed within the secretory pathway of the parasite. Initial cleavage occurs in the endoplasmic reticulum, after which the protein is transported to micronemes, vesicles that secrete early during host cell invasion. Upon stimulation of microneme secretion, TgSUB1 is cleaved into smaller products that are secreted from the parasite. This secondary processing is inhibited by brefeldin A and serine protease inhibitors. TgSUB1 is a candidate processing enzyme for several microneme proteins cleaved within the secretory pathway or during invasion.
AB - Proteolytic processing plays a significant role in the process of invasion by the obligate intracellular parasite Toxoplasma gondii. We have cloned a gene, TgSUB1, encoding for a subtilisin-type serine protease found in T. gondii tachyzoites. TgSUB1 protein is homologous to other Apicomplexan and bacterial subtilisins and is processed within the secretory pathway of the parasite. Initial cleavage occurs in the endoplasmic reticulum, after which the protein is transported to micronemes, vesicles that secrete early during host cell invasion. Upon stimulation of microneme secretion, TgSUB1 is cleaved into smaller products that are secreted from the parasite. This secondary processing is inhibited by brefeldin A and serine protease inhibitors. TgSUB1 is a candidate processing enzyme for several microneme proteins cleaved within the secretory pathway or during invasion.
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U2 - 10.1074/jbc.M106665200
DO - 10.1074/jbc.M106665200
M3 - Article
C2 - 11564738
AN - SCOPUS:0035976961
SN - 0021-9258
VL - 276
SP - 45341
EP - 45348
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 48
ER -