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Apical membrane antigen 1

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AMA-1
solution structure of plasmodium falciparum apical membrane antigen 1 (residues 436-545)
Identifiers
SymbolAMA-1
PfamPF02430
InterProIPR003298
SCOP21hn6 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, apical membrane antigen 1 is a novel antigen of Plasmodium falciparum which has been cloned. It contains a hydrophobic domain typical of an integral membrane protein. The antigen is designated apical membrane antigen 1 (AMA-1) by virtue of appearing to be located in the apical complex.[1] AMA-1 appears to be transported to the merozoite surface close to the time of schizont rupture.

The 66kDa merozoite surface antigen (PK66) of Plasmodium knowlesi, a simian malaria, possesses vaccine-related properties believed to originate from a receptor-like role in parasite invasion of erythrocytes.[2] The sequence of PK66 is conserved throughout Plasmodium, and shows high similarity to P. falciparum AMA-1. Following schizont rupture, the distribution of PK66 changes in a coordinate manner associated with merozoite invasion. Prior to rupture, the protein is concentrated at the apical end, following which it distributes itself entirely across the surface of the free merozoite. Immunofluorescence studies suggest that, during invasion, PK66 is excluded from the erythrocyte at, and behind, the invasion interface.[2]

References

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  1. ^ Peterson MG, Marshall VM, Smythe JA, Crewther PE, Lew A, Silva A, Anders RF, Kemp DJ (July 1989). "Integral membrane protein located in the apical complex of Plasmodium falciparum". Mol. Cell. Biol. 9 (7): 3151–4. doi:10.1128/MCB.9.7.3151. PMC 362792. PMID 2701947.
  2. ^ a b Waters AP, Thomas AW, Deans JA, Mitchell GH, Hudson DE, Miller LH, McCutchan TF, Cohen S (October 1990). "A merozoite receptor protein from Plasmodium knowlesi is highly conserved and distributed throughout Plasmodium". J. Biol. Chem. 265 (29): 17974–9. doi:10.1016/S0021-9258(18)38259-0. PMID 2211675.
This article incorporates text from the public domain Pfam and InterPro: IPR003298