Plasmodium RESA, N-terminal | |||||||||
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Identifiers | |||||||||
Symbol | PRESAN | ||||||||
Pfam | PF09687 | ||||||||
InterPro | IPR019111 | ||||||||
CATH | 4jle | ||||||||
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Also IPR006526. The structure is chain-swapped: each side of the blue line is a "solution" monomer. |
The Plasmodium helical interspersed subtelomeric proteins (PHIST) or ring-infected erythrocyte surface antigens (RESA) are a family of protein domains found in the malaria-causing Plasmodium species. It was initially identified as a short four-helical conserved region in the single-domain export proteins, [1] but the identification of this part associated with a DnaJ domain in P. falciparum RESA (named after the ring stage of the parasite) has led to its reclassification as the RESA N-terminal domain. This domain has been classified into three subfamilies, PHISTa, PHISTb, and PHISTc. [2]
The PHIST proteins are exported to the cytoplasm of the infected erythrocyte. The human malaria parasites P. falciparum and P. vivax have shown a lineage-specific expansion of proteins with this domain. [1] Of the two PHIST genes in the mouse parasite P. berghei, only one is required for infection. [3] The PHIST domain folds into three long helices (forming a bundle) and two smaller N-terminal helices, and is monomeric in solution. It binds PfEMP1 ATS C-terminus and plays a role in "knob" formation. [4]
Ring-infected erythrocyte surface antigen | |||||||
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Identifiers | |||||||
Organism | |||||||
Symbol | RESA | ||||||
Alt. symbols | Pf155, RESA-1 | ||||||
UniProt | P13830 | ||||||
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The full RESA protein in P. falciparum also contains a few other domains, namely the DnaJ domain and the DnaJ-associated X domain. A part of the X-domain, RESA/P13830663-670, appears to bind and reinforce spectrin cytoskeleton so that each erythrocyte only hosts one parasite. [5]
P. falciparum isolate 3D7 encodes three RESA-family proteins, RESA-1 (P13830/
Plasmodium RESA, N-terminal | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() | |||||||||
Identifiers | |||||||||
Symbol | PRESAN | ||||||||
Pfam | PF09687 | ||||||||
InterPro | IPR019111 | ||||||||
CATH | 4jle | ||||||||
| |||||||||
Also IPR006526. The structure is chain-swapped: each side of the blue line is a "solution" monomer. |
The Plasmodium helical interspersed subtelomeric proteins (PHIST) or ring-infected erythrocyte surface antigens (RESA) are a family of protein domains found in the malaria-causing Plasmodium species. It was initially identified as a short four-helical conserved region in the single-domain export proteins, [1] but the identification of this part associated with a DnaJ domain in P. falciparum RESA (named after the ring stage of the parasite) has led to its reclassification as the RESA N-terminal domain. This domain has been classified into three subfamilies, PHISTa, PHISTb, and PHISTc. [2]
The PHIST proteins are exported to the cytoplasm of the infected erythrocyte. The human malaria parasites P. falciparum and P. vivax have shown a lineage-specific expansion of proteins with this domain. [1] Of the two PHIST genes in the mouse parasite P. berghei, only one is required for infection. [3] The PHIST domain folds into three long helices (forming a bundle) and two smaller N-terminal helices, and is monomeric in solution. It binds PfEMP1 ATS C-terminus and plays a role in "knob" formation. [4]
Ring-infected erythrocyte surface antigen | |||||||
---|---|---|---|---|---|---|---|
Identifiers | |||||||
Organism | |||||||
Symbol | RESA | ||||||
Alt. symbols | Pf155, RESA-1 | ||||||
UniProt | P13830 | ||||||
|
The full RESA protein in P. falciparum also contains a few other domains, namely the DnaJ domain and the DnaJ-associated X domain. A part of the X-domain, RESA/P13830663-670, appears to bind and reinforce spectrin cytoskeleton so that each erythrocyte only hosts one parasite. [5]
P. falciparum isolate 3D7 encodes three RESA-family proteins, RESA-1 (P13830/