About: The malaria parasite Plasmodium falciparum in red blood cells selectively takes up serum proteins that affect host pathogenicity

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About: The malaria parasite Plasmodium falciparum in red blood cells selectively takes up serum proteins that affect host pathogenicity Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The malaria parasite Plasmodium falciparum in red blood cells selectively takes up serum proteins that affect host pathogenicity
Creator	Morita, Masayuki Horii, Toshihiro Tougan, Takahiro Tsuboi, Takafumi Edula, Jyotheeswara Honma, Hajime Takashima, Eizo
Source	PMC
abstract	BACKGROUND: The malaria parasite Plasmodium falciparum is a protozoan that develops in red blood cells (RBCs) and requires various host factors. For its development in RBCs, nutrients not only from the RBC cytosol but also from the extracellular milieu must be acquired. Although the utilization of host nutrients by P. falciparum has been extensively analysed, only a few studies have reported its utilization of host serum proteins. Hence, the aim of the current study was to comprehensively identify host serum proteins taken up by P. falciparum parasites and to elucidate their role in pathogenesis. METHODS: Plasmodium falciparum was cultured with human serum in vitro. Uptake of serum proteins by parasites was comprehensively determined via shotgun liquid chromatography–mass spectrometry/mass spectrometry and western blotting. The calcium ion concentration in serum was also evaluated, and coagulation activity of the parasite lysate was assessed. RESULTS: Three proteins, vitamin K-dependent protein S, prothrombin, and vitronectin, were selectively internalized under sufficient Ca(2+) levels in the culture medium. The uptake of these proteins was initiated before DNA replication, and increased during the trophozoite and schizont stages, irrespective of the assembly/disassembly of actin filaments. Coagulation assay revealed that prothrombin was activated and thereby induced blood coagulation. CONCLUSIONS: Serum proteins were taken up by parasites under culture conditions with sufficient Ca(2+) levels. This uptake phenomenon was associated with their pathogenicity.
has issue date	2020-04-15(xsd:dateTime)
bibo:doi	10.1186/s12936-020-03229-1
bibo:pmid	32295584
has license	cc-by
sha1sum (hex)	d7fecefeaca5d38afd61ec61500596756f0fac35
schema:url	https://doi.org/10.1186/s12936-020-03229-1
resource representing a document's title	The malaria parasite Plasmodium falciparum in red blood cells selectively takes up serum proteins that affect host pathogenicity
has PubMed Central identifier	PMC7161009
has PubMed identifier	32295584
schema:publication	Malar J
resource representing a document's body	covid:d7fecefeaca5d38afd61ec61500596756f0fac35#body_text
is schema:about of	named entity 'falciparum' named entity 'extensively' named entity 'affect' named entity 'Plasmodium' named entity 'The' named entity 'THEIR' named entity 'IDENTIFY' named entity 'PATHOGENESIS' covid:arg/d7fecefeaca5d38afd61ec61500596756f0fac35 named entity 'serum proteins' named entity 'parasite' named entity 'Although' named entity 'host' named entity 'serum proteins' named entity 'parasites' named entity 'extracellular milieu' named entity 'serum proteins' named entity 'serum proteins' named entity 'malaria parasite' named entity 'millilitres' named entity 'NaCl' named entity 'parasite' named entity 'rodent' named entity 'Plasmodium' named entity 'lysate' named entity 'RBC' named entity 'precipitation' named entity 'ovalbumin' named entity 'Tokyo' named entity 'serum proteins' named entity 'Alexa Fluor' named entity 'negative control' named entity 'protein' named entity 'coagulation' named entity 'PBS' named entity 'serum proteins' named entity 'RBC' named entity 'β-Actin' named entity 'Plasma' named entity 'protein' named entity 'protease' named entity 'Serum proteins' named entity 'vitamin K-dependent protein' named entity 'Sigma-Aldrich' named entity 'amino acids' named entity 'Terumo' named entity 'purines' named entity 'Gla domain' named entity 'protein' named entity 'supernatants' named entity 'metabolism' named entity 'lysates' named entity 'Reducing Agent' named entity 'Serum proteins' named entity 'protease' named entity 'parasite' named entity 'coagulation' named entity 'prothrombin' named entity 'skim milk' named entity 'culture media' named entity 'digestion' named entity 'prothrombin' named entity 'antibodies' named entity 'vitronectin' named entity 'lysate' named entity 'host cells' named entity 'Band 3' named entity 'streptolysin' named entity 'calcium' named entity 'saline' named entity 'centrifugation' named entity 'serum proteins' named entity 'Confocal microscopy' named entity 'IgG' named entity 'serum proteins'

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