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BioID of the proteins CGP and FRM1 from Toxoplasma gondii

ABSTRACT: The conoid complex, a unique structure in the phylum Apicomplexa, is crucial for host cell invasion, egress, and motility. Despite its importance, the detailed molecular composition and assembly mechanisms of the conoid complex remain poorly understood. In previous research, we identified an essential conoidal protein, CGP, which is required for parasite motility activation through a splitCas9 phenotypic screen. Here, using proximity-dependent biotin identification of CGP and FRM1, we uncovered novel components localizing at the preconoidal rings. Furthermore, we identified a novel daughter-specific protein localizing at the APRs. Depletion of this protein resulted in severe morphological defects and failure in daughter bud formation. Ultrastructure expansion microscopy revealed highly disorganized or absent nascent tubulin. Although conoidal proteins could form, they were defective in assembling the conoid complex. Collectively, our findings identify a novel daughter-specific apical polar ring protein that provides the base for the initiation and growth of nascent tubulin, which in turn provides the scaffold for daughter bud formation.

INSTRUMENT(S):

ORGANISM(S): Toxoplasma Gondii Rh

SUBMITTER: Ignasi Forne

LAB HEAD: Prof. Dr. rer. nat. Markus Meissne

PROVIDER: PXD053452 | Pride | 2025-09-17

REPOSITORIES: Pride

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			Action	DRS
	Groups.txt	Txt
	Ref7090_MS_EJ_10_20211210.raw	Raw
	Ref7090_MS_LW_01_20211210.raw	Raw
	Ref7090_MS_LW_02_20211210.raw	Raw
	Ref7090_MS_LW_03_20211210.raw	Raw

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