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Cited by 14Toxoplasma gondii Research StudiesCoccidia and coccidiosis researchMalaria Research and Control

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An apical protein, Pcr2, is required for persistent movement by the human parasite Toxoplasma gondii

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Munera Lopez, Jonathan, Tengganu, Isadonna F., Liu, Jun, Murray, John M., Arias Padilla, Luisa F., Zhang, Ying, Brown, Peter T., Florens, Laurence, Hu, Ke·2022·PLOS Pathogens
DOI 10.1371/journal.ppat.1010776PMC PMC9436145

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Abstract

The phylum Apicomplexa includes thousands of species of unicellular parasites that cause a wide range of human and animal diseases such as malaria and toxoplasmosis. To infect, the parasite must first initiate active movement to disseminate through tissue and invade into a host cell, and then cease moving once inside. The parasite moves by gliding on a surface, propelled by an internal cortical actomyosin-based motility apparatus. One of the most effective invaders in Apicomplexa is Toxoplasma gondii , which can infect any nucleated cell and any warm-blooded animal. During invasion, the parasite first makes contact with the host cell "head-on" with the apical complex, which features an elaborate cytoskeletal apparatus and associated structures. Here we report the identification and characterization of a new component of the apical complex, Preconoidal region protein 2 (Pcr2). Pcr2 knockout parasites replicate normally, but they are severely diminished in their capacity for host tissue destruction due to significantly impaired invasion and egress, two vital steps in the lytic cycle. When stimulated for calcium-induced egress, Pcr2 knockout parasites become active, and secrete effectors to lyse the host cell. Calcium-induced secretion of the major adhesin, MIC2, also appears to be normal. However, the movement of the Pcr2 knockout parasite is spasmodic, which drastically compromises egress. In addition to faulty motility, the ability of the Pcr2 knockout parasite to assemble the moving junction is impaired. Both defects likely contribute to the poor efficiency of invasion. Interestingly, actomyosin activity, as indicated by the motion of mEmerald tagged actin chromobody, appears to be largely unperturbed by the loss of Pcr2, raising the possibility that Pcr2 may act downstream of or in parallel with the actomyosin machinery.

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Metadata

Authors
Munera Lopez, J., Tengganu, I. F., Liu, J., Murray, J. M., Arias Padilla, L. F., Zhang, Y., Brown, P. T., Florens, L., & Hu, K.
Affiliations
  • Arizona State University (US)
  • Indiana University Bloomington (US)
  • Stowers Institute for Medical Research (US)
Corresponding author
Hu, Ke
ORCID
Venue
PLOS Pathogens
Publisher
Public Library of Science (PLoS)
Published
2022-08-22
Volume
18
Issue
8
Pages
e1010776
ISSN
  • 1553-7366 (ISSN-L)
  • 1553-7374
DOI
10.1371/journal.ppat.1010776
PMC
PMC9436145
OpenAlex
W4292635878
Cited by
14
References
2
Citations by year
2026: 2 · 2025: 3 · 2024: 4 · 2023: 2 · 2022: 3
FWCI
2.39
Type
journal article
Language
en
Update notices
new_version (2022-09-01)
Open access
Licence
Locations
  • PLoS Pathogens (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
National Institute of Allergy and Infectious Diseases (R01-AI132463)
Topics
  • Life Sciences › Immunology and Microbiology › Parasitology › Toxoplasma gondii Research Studies
  • Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Coccidia and coccidiosis research
  • Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Malaria Research and Control
Keywords
Toxoplasma gondii, apical complex, gliding motility, host cell invasion, egress, moving junction, actomyosin, host cell lysis, lytic cycle, Apicomplexa
MeSH terms
Actomyosin, Animals, Calcium, Host-Parasite Interactions, Humans, Parasites, Toxoplasma, Protozoan Proteins

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