Plasmodium protease ROM1 is important for proper formation of the parasitophorous vacuole.

Apicomplexans are obligate intracellular parasites that invade host cells by an active process leading to the formation of a non-fusogenic parasitophorous vacuole (PV) where the parasite replicates within the host cell. The rhomboid family of proteases cleaves substrates within their transmembrane d...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Iset Medina Vera, Wandy L Beatty, Photini Sinnis, Kami Kim
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2011
Materias:
Acceso en línea:https://doaj.org/article/4c00ca6305e74593bc885540bcab7883
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:4c00ca6305e74593bc885540bcab7883
record_format dspace
spelling oai:doaj.org-article:4c00ca6305e74593bc885540bcab78832021-11-18T06:03:03ZPlasmodium protease ROM1 is important for proper formation of the parasitophorous vacuole.1553-73661553-737410.1371/journal.ppat.1002197https://doaj.org/article/4c00ca6305e74593bc885540bcab78832011-09-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21909259/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Apicomplexans are obligate intracellular parasites that invade host cells by an active process leading to the formation of a non-fusogenic parasitophorous vacuole (PV) where the parasite replicates within the host cell. The rhomboid family of proteases cleaves substrates within their transmembrane domains and has been implicated in the invasion process. Although its exact function is unknown, Plasmodium ROM1 is hypothesized to play a role during invasion based on its microneme localization and its ability to cleave essential invasion adhesins. Using the rodent malaria model, Plasmodium yoelii, we carried out detailed quantitative analysis of pyrom1 deficient parasites during the Plasmodium lifecycle. Pyrom1(-) parasites are attenuated during erythrocytic and hepatic stages but progress normally through the mosquito vector with normal counts of oocyst and salivary gland sporozoites. Pyrom1 steady state mRNA levels are upregulated 20-fold in salivary gland sporozoites compared to blood stages. We show that pyrom1(-) sporozoites are capable of gliding motility and traversing host cells normally. Wildtype and pyrom1(-) sporozoites do not differ in the rate of entry into Hepa1-6 hepatocytes. Within the first twelve hours of hepatic development, however, only 50% pyrom1(-) parasites have developed into exoerythrocytic forms. Immunofluorescence microscopy using the PVM marker UIS4 and transmission electron microscopy reveal that the PV of a significant fraction of pyrom1(-) parasites are morphologically aberrant shortly after invasion. We propose a novel function for PyROM1 as a protease that promotes proper PV modification to allow parasite development and replication in a suitable environment within the mammalian host.Iset Medina VeraWandy L BeattyPhotini SinnisKami KimPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 7, Iss 9, p e1002197 (2011)
institution DOAJ
collection DOAJ
language EN
topic Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
spellingShingle Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
Iset Medina Vera
Wandy L Beatty
Photini Sinnis
Kami Kim
Plasmodium protease ROM1 is important for proper formation of the parasitophorous vacuole.
description Apicomplexans are obligate intracellular parasites that invade host cells by an active process leading to the formation of a non-fusogenic parasitophorous vacuole (PV) where the parasite replicates within the host cell. The rhomboid family of proteases cleaves substrates within their transmembrane domains and has been implicated in the invasion process. Although its exact function is unknown, Plasmodium ROM1 is hypothesized to play a role during invasion based on its microneme localization and its ability to cleave essential invasion adhesins. Using the rodent malaria model, Plasmodium yoelii, we carried out detailed quantitative analysis of pyrom1 deficient parasites during the Plasmodium lifecycle. Pyrom1(-) parasites are attenuated during erythrocytic and hepatic stages but progress normally through the mosquito vector with normal counts of oocyst and salivary gland sporozoites. Pyrom1 steady state mRNA levels are upregulated 20-fold in salivary gland sporozoites compared to blood stages. We show that pyrom1(-) sporozoites are capable of gliding motility and traversing host cells normally. Wildtype and pyrom1(-) sporozoites do not differ in the rate of entry into Hepa1-6 hepatocytes. Within the first twelve hours of hepatic development, however, only 50% pyrom1(-) parasites have developed into exoerythrocytic forms. Immunofluorescence microscopy using the PVM marker UIS4 and transmission electron microscopy reveal that the PV of a significant fraction of pyrom1(-) parasites are morphologically aberrant shortly after invasion. We propose a novel function for PyROM1 as a protease that promotes proper PV modification to allow parasite development and replication in a suitable environment within the mammalian host.
format article
author Iset Medina Vera
Wandy L Beatty
Photini Sinnis
Kami Kim
author_facet Iset Medina Vera
Wandy L Beatty
Photini Sinnis
Kami Kim
author_sort Iset Medina Vera
title Plasmodium protease ROM1 is important for proper formation of the parasitophorous vacuole.
title_short Plasmodium protease ROM1 is important for proper formation of the parasitophorous vacuole.
title_full Plasmodium protease ROM1 is important for proper formation of the parasitophorous vacuole.
title_fullStr Plasmodium protease ROM1 is important for proper formation of the parasitophorous vacuole.
title_full_unstemmed Plasmodium protease ROM1 is important for proper formation of the parasitophorous vacuole.
title_sort plasmodium protease rom1 is important for proper formation of the parasitophorous vacuole.
publisher Public Library of Science (PLoS)
publishDate 2011
url https://doaj.org/article/4c00ca6305e74593bc885540bcab7883
work_keys_str_mv AT isetmedinavera plasmodiumproteaserom1isimportantforproperformationoftheparasitophorousvacuole
AT wandylbeatty plasmodiumproteaserom1isimportantforproperformationoftheparasitophorousvacuole
AT photinisinnis plasmodiumproteaserom1isimportantforproperformationoftheparasitophorousvacuole
AT kamikim plasmodiumproteaserom1isimportantforproperformationoftheparasitophorousvacuole
_version_ 1718424663261970432