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Molecular and Cellular Biology, October 2000, p. 7332-7341, Vol. 20, No. 19
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Two Conserved Amino Acid Motifs Mediate Protein Targeting to the Micronemes of the Apicomplexan Parasite Toxoplasma gondii

Manlio Di Cristina,1 Roberta Spaccapelo,1 Dominique Soldati,2 Francesco Bistoni,3 and Andrea Crisanti1,*

Imperial College of Science, Technology, and Medicine, Department of Biology, London SW7 2AZ, United Kingdom1; Zentrum Moleculare Biologie, University of Heidelberg, Heidelberg, Germany2; and Dipartimento di Medicina Sperimentale, Sezione di Microbiologia, Università di Perugia, Perugia, Italy3

Received 4 April 2000/Returned for modification 8 June 2000/Accepted 7 July 2000

The micronemal protein 2 (MIC2) of Toxoplasma gondii shares sequence and structural similarities with a series of adhesive molecules of different apicomplexan parasites. These molecules accumulate, through a yet unknown mechanism, in secretory vesicles (micronemes), which together with tubular and membrane structures form the locomotion and invasion machinery of apicomplexan parasites. Our findings indicated that two conserved motifs placed within the cytoplasmic domain of MIC2 are both necessary and sufficient for targeting proteins to T. gondii micronemes. The first motif is based around the amino acid sequence SYHYY. Database analysis revealed that a similar sequence is present in the cytoplasmic tail of all transmembrane micronemal proteins identified so far in different apicomplexan species. The second signal consists of a stretch of acidic residues, EIEYE. The creation of an artificial tail containing only the two motifs SYHYY and EIEYE in a preserved spacing configuration is sufficient to target the surface protein SAG1 to the micronemes of T. gondii. These findings shed new light on the molecular mechanisms that control the formation of the microneme content and the functional relationship that links these organelles with the endoplasmic reticulum of the parasite.

* Corresponding author. Mailing address: Department of Biology, Imperial College of Science, Technology, & Medicine, Imperial College Rd., London SW7 2AZ, United Kingdom. Phone: 44 171 5945426. Fax: 44 171 5945439. E-mail: a.drcrisanti{at}ic.ac.uk.

Molecular and Cellular Biology, October 2000, p. 7332-7341, Vol. 20, No. 19
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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