Search

Plasmodium vivax reticulocyte binding protein 2b (PvRBP2b) is important for invasion of reticulocytes and PvRBP2b antibodies correlate with protection. Here, Chan et al. isolate and characterize anti-PvRBP2b human monoclonal antibodies and describe mechanisms by which these antibodies inhibit invasion.

Apicomplexan parasites such as Toxoplasma gondii and Plasmodium form a tight, moving junction with host cells before invading them. Here the authors show that the proteins AMA1 and RON2 of T. gondiicooperate during junction formation and identify additional proteins that have a role in this process.

Apicomplexa include important human pathogens and possess a unique cellular machinery that promotes gliding motility and is called the glideosome. In this Review, Soldati-Favre and colleagues discuss the principles that govern gliding motility, the characterization of the molecular machinery that comprises the glideosome, and its impact on parasite invasion and egress from infected cells.

The authors uncover one of the largest mitoribosomes, dedicated to translating only three proteins in lethal human eukaryotic pathogens of the Apicomplexa phylum. All members of mitochondrial DNA-containing Myzozoa, including Toxoplasma gondii, have commandeered three lineage-specific families of RNA-binding proteins to meticulously piece together over 40 mitochondrial rRNA fragments to build an operational mitoribosome.

Here, Chen et al. bypass the critical metabolic pathways of the remnant plastid organelle of Toxoplasma gondii. A subsequent detailed characterization of parasites devoid of the apicoplast organelle provides unprecedented insights into its constituents, evolution and functions, uncovering new vulnerabilities.

The authors identified a series of cytoskeletal proteins involved in the discharge of invasion-related organelles in Toxoplasma gondii. They successfully delineated their functions through the utilization of expansion and cryo-electron microscopy.

In apicomplexan parasites, the conoid is a dynamic organelle of enigmatic function. This study establishes that the conoid movement is essential to control the flux of F-actin needed for myosin-dependent motility that powers invasion and egress.

Coenzyme A (CoA) is an essential metabolite found in all organisms and its synthesis involves five conserved enzymatic steps and uses pantothenate (Pan) as a precursor. Here, Lunghi et al. examine the Pan synthesis pathway in Toxoplasma gondii and find that Pan is crucial for the establishment of chronic but not acute infection.

Host cell invasion by Toxoplasma gondii depends on the heavily phosphorylated RON complex, but the relevance and regulation of these modifications are not understood. Here, the authors identify the kinase RON13 as a key virulence factor, determine its structure and show that it phosphorylates the RON complex.

The mechanism by whichToxoplasma gondiiachieves synchronized cell division is incompletely understood. Here, the authors identify an intravacuolar cell-cell communication that ensures synchronized division and depends on myosin I.

Parasite access to the central nervous system is a severe complication of infection. Toxoplasma gondii can achieve this by directly infecting, replicating in and lysing blood–brain barrier endothelial cells.

During Toxoplasma gondii infection, diacylglycerol kinase 2 is secreted into the parasitophorous vacuole, leading to the production of phosphatidic acid, which is sensed by an atypical guanylate cyclase in the parasite plasma membrane, triggering egress from the host cell.

Current expansion microscopy approaches need further optimization to achieve the precision of nanoscopy techniques. Here, the authors develop an iterative ultrastructure expansion microscopy (iU-ExM) approach that achieves SMLM-level resolution.

Apicomplexan parasites utilize a unique actomyosin system to mediate motility and host cell invasion. Here, the authors apply cryo-ET to Cryptosporidium parvum and Toxoplasma gondii to visualize the F-actin architecture in the native cellular context.

Toxoplasma gondii uses its proteins RON2, RON4 and RON5 to recruit host proteins, including the ESCRT-I components ALIX and TSG101 to the moving junction, a multimolecular structure that enables invasion.