NDLI: Plasmodium falciparum merozoite surface protein 3: oligomerization, self-assembly, and heme complex formation.

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Plasmodium falciparum merozoite surface protein 3: oligomerization, self-assembly, and heme complex formation.

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Plasmodium falciparum merozoite surface protein 3: oligomerization, self-assembly, and heme complex formation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Chauhan, Virander Singh Singh, Shailja Kaushik, Naveen Kumar Imam, Maryam
Description	Author Affiliation: Imam M ( From the Malaria Research Group, International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India.)
Abstract	Merozoite surface protein 3 of Plasmodium falciparum, a 40-kDa protein that also binds heme, has been biophysically characterized for its tendency to form highly elongated oligomers. This study aims to systematically analyze the regions in MSP3 sequence involved in oligomerization and correlate its aggregation tendency with its high affinity for binding with heme. Through size exclusion chromatography, dynamic light scattering, and transmission electron microscopy, we have found that MSP3, previously known to form elongated oligomers, actually forms self-assembled filamentous structures that possess amyloid-like characteristics. By expressing different regions of MSP3, we observed that the previously described leucine zipper region at the C terminus of MSP3 may not be the only structural element responsible for oligomerization and that other peptide segments like MSP3(192-196) (YILGW) may also be required. MSP3 aggregates on incubation were transformed to long unbranched amyloid fibrils. Using immunostaining methods, we found that 5-15-µm-long fibrillar structures stained by anti-MSP3 antibodies were attached to the merozoite surface and also associated with erythrocyte membrane. We also found MSP3 to bind several molecules of heme by UV spectrophotometry, HPLC, and electrophoresis. This study suggested that its ability to bind heme is somehow related to its inherent characteristics to form oligomers. Moreover, heme interaction with a surface protein like MSP3, which does not participate in hemozoin formation, may suggest a protective role against the heme released from unprocessed hemoglobin released after schizont egress. These studies point to the other roles that MSP3 may play during the blood stages of the parasite, in addition to be an important vaccine candidate.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	7
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-02-14
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Antigens, Protozoan Chemistry Heme Plasmodium Falciparum Protein Multimerization Physiology Protozoan Proteins Genetics Metabolism Erythrocytes Parasitology Hemeproteins Malaria, Falciparum Protein Structure, Tertiary Schizonts Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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