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Expression of Single-Domain Soluble and Disulfide-Folded PfEMP1 Antigens in the Escherichia coli SHuffle Expression System.
Quintana, Maria Del Pilar.
Affiliation
  • Quintana MDP; Department of Immunology and Microbiology, Faculty of Health and Medical Sciences, Centre for Medical Parasitology, University of Copenhagen, Copenhagen, Denmark. pilar@sund.ku.dk.
Methods Mol Biol ; 2470: 273-282, 2022.
Article in En | MEDLINE | ID: mdl-35881352
The genome of Plasmodium falciparum has an A/T content of around 81%. This, together with a high cysteine content and the high molecular weight of several proteins, make the expression of recombinant parasite proteins in heterologous systems challenging. P. falciparum erythrocyte membrane protein 1 (PfEMP1) is a family of proteins composed of several Duffy-binding like (DBL) and cysteine-rich inter-domain region (CIDR) domains involved in cytoadhesion to human host receptors and development of severe malaria. Expression of correctly folded single- and multiple-domain PfEMP1 fragment regions containing cysteines forming disulfide bonds, remains particularly difficult. Nevertheless, expression of single DBL and CIDR domains has been successful and this protocol describes the expression and purification of single-domain soluble PfEMP1 fragments using the Escherichia coli SHuffle expression system.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protozoan Proteins / Malaria, Falciparum Limits: Humans Language: En Journal: Methods Mol Biol Journal subject: BIOLOGIA MOLECULAR Year: 2022 Document type: Article Affiliation country: Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protozoan Proteins / Malaria, Falciparum Limits: Humans Language: En Journal: Methods Mol Biol Journal subject: BIOLOGIA MOLECULAR Year: 2022 Document type: Article Affiliation country: Country of publication: