Unique apicomplexan IMC sub-compartment proteins are early markers for apical polarity in the malaria parasite

The phylum Apicomplexa comprises over 5000 intracellular protozoan parasites, including Plasmodium and Toxoplasma, that are clinically important pathogens affecting humans and livestock. Malaria parasites belonging to the genus Plasmodium possess a pellicle comprised of a plasmalemma and inner membr...

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Published inBiology open Vol. 2; no. 11; pp. 1160 - 1170
Main Authors Poulin, Benoit, Patzewitz, Eva-Maria, Brady, Declan, Silvie, Olivier, Wright, Megan H, Ferguson, David J P, Wall, Richard J, Whipple, Sarah, Guttery, David S, Tate, Edward W, Wickstead, Bill, Holder, Anthony A, Tewari, Rita
Format Journal Article
LanguageEnglish
Published England The Company of Biologists Ltd 15.11.2013
The Company of Biologists
Subjects
Apicomplexa
Developmental stages
Gene disruption
Genetics
ISP
Livestock
Malaria
Membranes
Parasites
Pellicle
Plasma membranes
Plasmodium
Polarity
Proteins
Sporozoites
Toxoplasma
Vector-borne diseases
Zygotes
Plasmodium
Polarity
ISP
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Summary:The phylum Apicomplexa comprises over 5000 intracellular protozoan parasites, including Plasmodium and Toxoplasma, that are clinically important pathogens affecting humans and livestock. Malaria parasites belonging to the genus Plasmodium possess a pellicle comprised of a plasmalemma and inner membrane complex (IMC), which is implicated in parasite motility and invasion. Using live cell imaging and reverse genetics in the rodent malaria model P. berghei, we localise two unique IMC sub-compartment proteins (ISPs) and examine their role in defining apical polarity during zygote (ookinete) development. We show that these proteins localise to the anterior apical end of the parasite where IMC organisation is initiated, and are expressed at all developmental stages, especially those that are invasive. Both ISP proteins are N-myristoylated, phosphorylated and membrane-bound. Gene disruption studies suggest that ISP1 is likely essential for parasite development, whereas ISP3 is not. However, an absence of ISP3 alters the apical localisation of ISP1 in all invasive stages including ookinetes and sporozoites, suggesting a coordinated function for these proteins in the organisation of apical polarity in the parasite.
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These authors contributed equally to this work
ISSN:2046-6390
2046-6390
DOI:10.1242/bio.20136163