TY - JOUR
T1 - A novel PAN/apple domain-containing protein from Toxoplasma gondii
T2 - Characterization and receptor identification
AU - Gong, Haiyan
AU - Kobayashi, Kyousuke
AU - Sugi, Tatsuki
AU - Takemae, Hitoshi
AU - Kurokawa, Hitomi
AU - Horimoto, Taisuke
AU - Akashi, Hiroomi
AU - Kato, Kentaro
N1 - Copyright:
Copyright 2012 Elsevier B.V., All rights reserved.
PY - 2012/1/19
Y1 - 2012/1/19
N2 - Toxoplasma gondii is an intracellular parasite that invades nucleated cells, causing toxoplasmosis in humans and animals worldwide. The extremely wide range of hosts susceptible to T. gondii is thought to be the result of interactions between T. gondii ligands and receptors on its target cells. In this study, a host cell-binding protein from T. gondii was characterized, and one of its receptors was identified. P104 (GenBank Access. No. CAJ20677) is 991 amino acids in length, containing a putative 26 amino acid signal peptide and 10 PAN/apple domains, and shows low homology to other identified PAN/apple domain-containing molecules. A 104-kDa host cell-binding protein was detected in the T. gondii lysate. Immunofluorescence assays detected P104 at the apical end of extracellular T. gondii. An Fc-fusion protein of the P104 N-terminus, which contains two PAN/apple domains, showed strong affinity for the mammalian and insect cells evaluated. This binding was not related to protein-protein or protein-lipid interactions, but to a protein-glycosaminoglycan (GAG) interaction. Chondroitin sulfate (CS), a kind of GAG, was shown to be involved in adhesion of the Fc-P104 N-terminus fusion protein to host cells. These results suggest that P104, expressed at the apical end of the extracellular parasite, may function as a ligand in the attachment of T. gondii to CS or other receptors on the host cell, facilitating invasion by the parasite.
AB - Toxoplasma gondii is an intracellular parasite that invades nucleated cells, causing toxoplasmosis in humans and animals worldwide. The extremely wide range of hosts susceptible to T. gondii is thought to be the result of interactions between T. gondii ligands and receptors on its target cells. In this study, a host cell-binding protein from T. gondii was characterized, and one of its receptors was identified. P104 (GenBank Access. No. CAJ20677) is 991 amino acids in length, containing a putative 26 amino acid signal peptide and 10 PAN/apple domains, and shows low homology to other identified PAN/apple domain-containing molecules. A 104-kDa host cell-binding protein was detected in the T. gondii lysate. Immunofluorescence assays detected P104 at the apical end of extracellular T. gondii. An Fc-fusion protein of the P104 N-terminus, which contains two PAN/apple domains, showed strong affinity for the mammalian and insect cells evaluated. This binding was not related to protein-protein or protein-lipid interactions, but to a protein-glycosaminoglycan (GAG) interaction. Chondroitin sulfate (CS), a kind of GAG, was shown to be involved in adhesion of the Fc-P104 N-terminus fusion protein to host cells. These results suggest that P104, expressed at the apical end of the extracellular parasite, may function as a ligand in the attachment of T. gondii to CS or other receptors on the host cell, facilitating invasion by the parasite.
UR - http://www.scopus.com/inward/record.url?scp=84856005104&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84856005104&partnerID=8YFLogxK
U2 - 10.1371/journal.pone.0030169
DO - 10.1371/journal.pone.0030169
M3 - Article
C2 - 22276154
AN - SCOPUS:84856005104
VL - 7
JO - PLoS One
JF - PLoS One
SN - 1932-6203
IS - 1
M1 - e30169
ER -