The malaria secretome: from algorithms to essential function in blood stage infection.

The malaria agent Plasmodium falciparum is predicted to export a "secretome" of several hundred proteins to remodel the host erythrocyte. Prediction of protein export is based on the presence of an ER-type signal sequence and a downstream Host-Targeting (HT) motif (which is similar to, but...

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Main Authors: Christiaan van Ooij, Pamela Tamez, Souvik Bhattacharjee, N Luisa Hiller, Travis Harrison, Konstantinos Liolios, Taco Kooij, Jai Ramesar, Bharath Balu, John Adams, Andrew P Waters, Chris J Janse, Kasturi Haldar
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2008-06-01
Series:PLoS Pathogens
Online Access:https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1000084&type=printable
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author Christiaan van Ooij
Pamela Tamez
Souvik Bhattacharjee
N Luisa Hiller
Travis Harrison
Konstantinos Liolios
Taco Kooij
Jai Ramesar
Bharath Balu
John Adams
Andrew P Waters
Chris J Janse
Kasturi Haldar
author_facet Christiaan van Ooij
Pamela Tamez
Souvik Bhattacharjee
N Luisa Hiller
Travis Harrison
Konstantinos Liolios
Taco Kooij
Jai Ramesar
Bharath Balu
John Adams
Andrew P Waters
Chris J Janse
Kasturi Haldar
author_sort Christiaan van Ooij
collection DOAJ
description The malaria agent Plasmodium falciparum is predicted to export a "secretome" of several hundred proteins to remodel the host erythrocyte. Prediction of protein export is based on the presence of an ER-type signal sequence and a downstream Host-Targeting (HT) motif (which is similar to, but distinct from, the closely related Plasmodium Export Element [PEXEL]). Previous attempts to determine the entire secretome, using either the HT-motif or the PEXEL, have yielded large sets of proteins, which have not been comprehensively tested. We present here an expanded secretome that is optimized for both P. falciparum signal sequences and the HT-motif. From the most conservative of these three secretome predictions, we identify 11 proteins that are preserved across human- and rodent-infecting Plasmodium species. The conservation of these proteins likely indicates that they perform important functions in the interaction with and remodeling of the host erythrocyte important for all Plasmodium parasites. Using the piggyBac transposition system, we validate their export and find a positive prediction rate of approximately 70%. Even for proteins identified by all secretomes, the positive prediction rate is not likely to exceed approximately 75%. Attempted deletions of the genes encoding the conserved exported proteins were not successful, but additional functional analyses revealed the first conserved secretome function. This gave new insight into mechanisms for the assembly of the parasite-induced tubovesicular network needed for import of nutrients into the infected erythrocyte. Thus, genomic screens combined with functional assays provide unexpected and fundamental insights into host remodeling by this major human pathogen.
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spelling doaj-art-e81e08155fee4067a21b131a882534732025-08-20T03:22:26ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742008-06-0146e100008410.1371/journal.ppat.1000084The malaria secretome: from algorithms to essential function in blood stage infection.Christiaan van OoijPamela TamezSouvik BhattacharjeeN Luisa HillerTravis HarrisonKonstantinos LioliosTaco KooijJai RamesarBharath BaluJohn AdamsAndrew P WatersChris J JanseKasturi HaldarThe malaria agent Plasmodium falciparum is predicted to export a "secretome" of several hundred proteins to remodel the host erythrocyte. Prediction of protein export is based on the presence of an ER-type signal sequence and a downstream Host-Targeting (HT) motif (which is similar to, but distinct from, the closely related Plasmodium Export Element [PEXEL]). Previous attempts to determine the entire secretome, using either the HT-motif or the PEXEL, have yielded large sets of proteins, which have not been comprehensively tested. We present here an expanded secretome that is optimized for both P. falciparum signal sequences and the HT-motif. From the most conservative of these three secretome predictions, we identify 11 proteins that are preserved across human- and rodent-infecting Plasmodium species. The conservation of these proteins likely indicates that they perform important functions in the interaction with and remodeling of the host erythrocyte important for all Plasmodium parasites. Using the piggyBac transposition system, we validate their export and find a positive prediction rate of approximately 70%. Even for proteins identified by all secretomes, the positive prediction rate is not likely to exceed approximately 75%. Attempted deletions of the genes encoding the conserved exported proteins were not successful, but additional functional analyses revealed the first conserved secretome function. This gave new insight into mechanisms for the assembly of the parasite-induced tubovesicular network needed for import of nutrients into the infected erythrocyte. Thus, genomic screens combined with functional assays provide unexpected and fundamental insights into host remodeling by this major human pathogen.https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1000084&type=printable
spellingShingle Christiaan van Ooij
Pamela Tamez
Souvik Bhattacharjee
N Luisa Hiller
Travis Harrison
Konstantinos Liolios
Taco Kooij
Jai Ramesar
Bharath Balu
John Adams
Andrew P Waters
Chris J Janse
Kasturi Haldar
The malaria secretome: from algorithms to essential function in blood stage infection.
PLoS Pathogens
title The malaria secretome: from algorithms to essential function in blood stage infection.
title_full The malaria secretome: from algorithms to essential function in blood stage infection.
title_fullStr The malaria secretome: from algorithms to essential function in blood stage infection.
title_full_unstemmed The malaria secretome: from algorithms to essential function in blood stage infection.
title_short The malaria secretome: from algorithms to essential function in blood stage infection.
title_sort malaria secretome from algorithms to essential function in blood stage infection
url https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1000084&type=printable
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