Ke. Rabenau et al., TgM2AP participates in Toxoplasma gondii host cells and is tightly associated with the invasion of adhesive protein TgMIC2, MOL MICROB, 41(3), 2001, pp. 537-547
Like other members of the medically important phylum Apicomplexa, Toxoplasm
a gondii is an obligate intracellular parasite that secretes several classe
s of proteins involved in the active invasion of target host cells. Protein
s in apical secretory organelles known as micronemes have been strongly imp
licated in parasite attachment to host cells. TgMIC2 is a microneme protein
with multiple adhesive domains that bind target cells and is mobilized ont
o the parasite surface during parasite attachment. Here, we describe a nove
l parasite protein, TgM2AP, which is physically associated with TgMIC2. TgM
2AP complexes with TgMIC2 within 15 min of synthesis and remains associated
with TgMIC2 in the micronemes, on the parasite surface during invasion and
in the culture medium after release from the parasite plasma membrane. TgM
2AP is proteolytically processed initially when its propeptide is removed d
uring transit through the golgi and later while it occupies the parasite su
rface after discharge from the micronemes. We show that TgM2AP is a member
of a protein family expressed by coccidian parasites including Neospora can
inum and Eimeria tenella. This phylogenic conservation and association with
a key adhesive protein suggest that TgM2AP is a fundamental component of t
he T. gondii invasion machinery.