INVESTIGADORES
PARUSSINI GIMENEZ silvana fabiola
artículos
Título:
Toxoplasma gondii transmembrane microneme proteins and their modular design
Autor/es:
LILACH SHEINER; JOANA M. SANTOS; NATACHA KLAGES; FABIOLA PARUSSINI; NOELLE JEMMELY; NIKOLAS FRIEDRICH; GARY E. WARD; DOMINIQUE SOLDATI-FAVRE
Revista:
MOLECULAR MICROBIOLOGY
Editorial:
WILEY-BLACKWELL PUBLISHING, INC
Referencias:
Lugar: Londres; Año: 2010 vol. 77 p. 912 - 929
ISSN:
0950-382X
Resumen:
Host cell invasion by the Apicomplexa critically relies on regulated secretion of transmembrane micronemal proteins (TM-MICs). Toxoplasma gondii
possesses functionally non-redundant MICs complexes that participate in
gliding motility, host cell attachment, moving junction formation,
rhoptry secretion and invasion. The TM-MICs are released onto the
parasite?s surface as complexes capable of interacting with host cell
receptors. Additionally, TgMIC2 simultaneously connects to the
actomyosin system via binding to aldolase. During invasion these
adhesive complexes are shed from the surface notably via intramembrane
cleavage of the TM-MICs by a rhomboid protease. Some TM-MICs act as
escorters and assure trafficking of the complexes to the micronemes. We
have investigated the properties of TgMIC6, TgMIC8, TgMIC8.2, TgAMA1 and
the new micronemal protein TgMIC16 with respect to interaction with
aldolase, susceptibility to rhomboid cleavage and presence of
trafficking signals. We conclude that several TM-MICs lack targeting
information within their C-terminal domains, indicating that trafficking
depends on yet unidentified proteins interacting with their
ectodomains. Most TM-MICs serve as substrates for a rhomboid protease
and some of them are able to bind to aldolase. We also show that the
residues responsible for binding to aldolase are essential for TgAMA1
but dispensable forTgMIC6 function during invasion.