TY - JOUR
T1 - Plasmodium falciparum enolase
T2 - Stage-specific expression and sub-cellular localization
AU - Pal Bhowmick, Ipsita
AU - Kumar, Nirbhay
AU - Sharma, Shobhona
AU - Coppens, Isabelle
AU - Jarori, Gotam K.
N1 - Funding Information:
We thank Eiji Nagayasu for help with parasite cultures for IFA, immuno-EM; MR4 for providing Pfs-48/45 Mab, anti-tubulin-II antibody; Dr. Victor Nus-senzweig, for the kind gift of rabbit anti-P. falciparum aldolase antibody and P. yoelii sporozoites and Dr. David Sibley for providing anti-Toxoplasma gon-dii actin antibody. We acknowledge Mr. Arpan Rai of TIFR for preparing goat brain tubulin and help in the GST-enolase pull down experiments. Research on gametocyte biology in the NK lab was supported by NIH RO1-AI46760.
PY - 2009
Y1 - 2009
N2 - Background. In an earlier study, it was observed that the vaccination with Plasmodium falciparum enolase can confer partial protection against malaria in mice. Evidence has also build up to indicate that enolases may perform several non-glycolytic functions in pathogens. Investigating the stage-specific expression and sub-cellular localization of a protein may provide insights into its moonlighting functions. Methods. Sub-cellular localization of P. falciparum enolase was examined using immunofluorescence assay, immuno-gold electron microscopy and western blotting. Results. Enolase protein was detected at every stage in parasite life cycle examined. In asexual stages, enolase was predominantly (≥8590%) present in soluble fraction, while in sexual stages it was mostly associated with particulate fraction. Apart from cytosol, enolase was found to be associated with nucleus, food vacuole, cytoskeleton and plasma membrane. Conclusion. Diverse localization of enolase suggests that apart from catalyzing the conversion of 2-phosphoglycericacid into phosphoenolpyruvate in glycolysis, enolase may be involved in a host of other biological functions. For instance, enolase localized on the merozoite surface may be involved in red blood cell invasion; vacuolar enolase may be involved in food vacuole formation and/or development; nuclear enolase may play a role in transcription.
AB - Background. In an earlier study, it was observed that the vaccination with Plasmodium falciparum enolase can confer partial protection against malaria in mice. Evidence has also build up to indicate that enolases may perform several non-glycolytic functions in pathogens. Investigating the stage-specific expression and sub-cellular localization of a protein may provide insights into its moonlighting functions. Methods. Sub-cellular localization of P. falciparum enolase was examined using immunofluorescence assay, immuno-gold electron microscopy and western blotting. Results. Enolase protein was detected at every stage in parasite life cycle examined. In asexual stages, enolase was predominantly (≥8590%) present in soluble fraction, while in sexual stages it was mostly associated with particulate fraction. Apart from cytosol, enolase was found to be associated with nucleus, food vacuole, cytoskeleton and plasma membrane. Conclusion. Diverse localization of enolase suggests that apart from catalyzing the conversion of 2-phosphoglycericacid into phosphoenolpyruvate in glycolysis, enolase may be involved in a host of other biological functions. For instance, enolase localized on the merozoite surface may be involved in red blood cell invasion; vacuolar enolase may be involved in food vacuole formation and/or development; nuclear enolase may play a role in transcription.
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U2 - 10.1186/1475-2875-8-179
DO - 10.1186/1475-2875-8-179
M3 - Article
C2 - 19642995
AN - SCOPUS:69449107551
SN - 1475-2875
VL - 8
JO - Malaria journal
JF - Malaria journal
IS - 1
M1 - 179
ER -