Choudhary, Jyoti

Collins, Mark O

Jones, Matthew L

Rayner, Julian C

English

PubMed

Matthew L Jones

Mark O Collins

Jyoti S Choudhary

Julian C Rayner

Crossref

Malaria Journal

A comprehensive survey of protein palmitoylation in late blood-stage Plasmodium falciparum

Rayner Julian C

Choudhary Jyoti

Collins Mark O

Jones Matthew L

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A comprehensive survey of protein palmitoylation in late blood-stage <it>Plasmodium falciparum</it>

Choudhary Jyoti S

Springer - Publisher Connector

POSTER PRESENTATIONS Open Access
A comprehensive survey of protein palmitoylation
in late blood-stage Plasmodium falciparum
Matthew L Jones, Mark O Collins, Jyoti S Choudhary, Julian C Rayner*
From Parasite to Prevention: Advances in the understanding of malaria
Edinburgh, UK. 20-22 October 2010
Protein palmitoylation, the addition of a 16-Carbon satu-
rated fatty acid to cysteine residues, is a common post-
translation modification of both peripheral and integral
membrane proteins. As a reversible modification, palmi-
toylation is essential for the dynamic regulation of protein
function—controlling, in many cases, protein localisation
both to and within specific membrane domains, protein
stability, and protein activity. Using two complementary
techniques, one relying on the exchange of palmitoyl
groups with a biotin linker and the other relying on
metabolic labelling of cells with a palmitic acid analogue,
we have purified the total catalogue of palmitoylated
protein from Plasmodium falciparum schizonts. The use
of these two complementary techniques in tandem with
SILAC based mass spectrometry to allow robust quantita-
tive MS have allowed the identification of more than 250
palmitoylated proteins in late blood-stage P. falciparum
parasites. This represents the first global analysis of pro-
tein palmitoylation in any Plasmodium parasite and has
identified palmitoyl-proteins involved in protein secretion,
protein export, drug resistance, signalling, development,
and invasion. Furthermore, we have found that palmitoy-
lation is essential for the completion of the blood-stage
life cycle and that this modification directly regulates the
stability of at least two proteins essential for invasion,
PfGAP45 and PfMTIP.
Published: 20 October 2010
doi:10.1186/1475-2875-9-S2-P16
Cite this article as: Jones et al.: A comprehensive survey of protein
palmitoylation in late blood-stage Plasmodium falciparum. Malaria Journal
2010 9(Suppl 2):P16.
Submit your next manuscript to BioMed Central
and take full advantage of: 
• Convenient online submission
• Thorough peer review
• No space constraints or color figure charges
• Immediate publication on acceptance
• Inclusion in PubMed, CAS, Scopus and Google Scholar
• Research which is freely available for redistribution
Submit your manuscript at 
www.biomedcentral.com/submitSanger Institute Malaria Programme, Wellcome Trust Sanger Institute,
Cambridge, Cambridgeshire CB10 1SA, UK
Jones et al. Malaria Journal 2010, 9(Suppl 2):P16
http://www.malariajournal.com/content/9/S2/P16
© 2010 Rayner et al; licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons
Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in
any medium, provided the original work is properly cited.


Jyoti Choudhary

ORAL PRESENTATION Open Access
A comprehensive survey of protein
palmitoylation in late blood-stage Plasmodium
falciparum
Matthew L Jones, Mark O Collins, Jyoti Choudhary, Julian C Rayner*
From Parasite to Prevention: Advances in the understanding of malaria
Edinburgh, UK. 20-22 October 2010
Protein palmitoylation, the addition of a 16-Carbon
saturated fatty acid to cysteine residues, is a common
post-translation modification of both peripheral and
integral membrane proteins. As a reversible modifica-
tion, palmitoylation is essential for the dynamic regula-
tion of protein function -controlling, in many cases,
protein localisation both to and within specific mem-
brane domains, protein stability, and protein activity.
Using two complementary techniques, one relying on
the exchange of palmitoyl groups with a biotin linker
and the other relying on metabolic labelling of cells with
a palmitic acid analogue, we have purified the total cata-
logue of palmitoylated protein from Plasmodium falci-
parum schizonts. The use of these two complementary
techniques in tandem with SILAC (stable isotope label-
ing by amino acids in cell culture) based mass spectro-
metry (MS) to allow robust quantitative MS have
allowed the identification of more than 250 palmitoy-
lated proteins in late blood-stage P. falciparum parasites.
This represents the first global analysis of protein palmi-
toylation in any Plasmodium parasite and has identified
palmitoyl-proteins involved in protein secretion, protein
export, drug resistance, signalling, development, and
invasion. Furthermore, we have found that palmitoyla-
tion is essential for the completion of the blood-stage
life cycle and that this modification directly regulates
the stability of at least two proteins essential for inva-
sion, PfGAP45 and PfMTIP.
Published: 20 October 2010
doi:10.1186/1475-2875-9-S2-O20
Cite this article as: Jones et al.: A comprehensive survey of protein
palmitoylation in late blood-stage Plasmodium falciparum. Malaria
Journal 2010 9(Suppl 2):O20.
Submit your next manuscript to BioMed Central
and take full advantage of: 
• Convenient online submission
• Thorough peer review
• No space constraints or color figure charges
• Immediate publication on acceptance
• Inclusion in PubMed, CAS, Scopus and Google Scholar
• Research which is freely available for redistribution
Submit your manuscript at 
www.biomedcentral.com/submitSanger Institute Malaria Programme, Wellcome Trust Sanger Institute,
Cambridge, Cambridgeshire CB10 1SA, UK
Jones et al. Malaria Journal 2010, 9(Suppl 2):O20
http://www.malariajournal.com/content/9/S2/O20
© 2010 Rayner et al; licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons
Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in
any medium, provided the original work is properly cited.


http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2963228

A comprehensive survey of protein palmitoylation in late blood-stage Plasmodium falciparum

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