Structural basis of Toxoplasma gondii MIC2-Associated Protein interaction with MIC2

J Biol Chem. 2014 Nov 19. pii: jbc.M114.613646. [Epub ahead of print]

Huynh MH1, Liu B2, Henry M2, Liew L2, Matthews SJ2, Carruthers VB3.

Author information 

Abstract

Toxoplasma gondii parasites must actively invade host cells to propagate. Secretory microneme proteins have been shown to be important for both gliding motility and active invasion. MIC2-M2AP is a protein complex that is essential for productive motility and rapid invasion by binding to host cell surface receptors. To investigate the architecture of the MIC2 and M2AP complex, we identified the minimal domains sufficient for interaction and solved the NMR solution structure of the globular domain of M2AP. We found that M2AP adopts a modified galectin fold similar to the C-terminal domain of another microneme protein, MIC1. NMR and immunoprecipitation analyses implicated hydrophobic residues on one face of the M2AP galectin fold in binding to the membrane proximal 6th thrombospondin type I repeat (TSR) domain of MIC2. Our findings provide a second example of a galectin fold adapted for microneme protein-protein interactions and suggest a conserved strategy for the assembly and folding of diverse protein complexes.

Copyright © 2014, The American Society for Biochemistry and Molecular Biology.

KEYWORDS: 

M2AP; MIC2; Toxoplasma gondii; cell invasion; galectin; microneme; nuclear magnetic resonance (NMR); protein complex

PMID:

 

25411252

 

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