Novel putative saposin-like proteins of Entamoeba histolytica different from amoebapores.
Amoebapores, the pore-forming proteins of Entamoeba histolytica, have been shown to play a pivotal role in the pathogenicity of the protozoan parasite. They belong to the functionally diverse family of saposin-like proteins (SAPLIPs) characterized by a conserved pattern of cysteine residues and the ability to interact with lipids. Here, we report the identification of genomic sequences encoding presumably novel SAPLIPs in E. histolytica and classify them in the structural and functional context provided by known family members. The genes of altogether 15 SAPLIPs are transcribed in the axenically cultured trophozoites as evidenced by reverse transcriptase-polymerase chain reaction. Interestingly, a remarkable sequence variety with a strong resemblance to that of known, functionally diverse SAPLIPs is present in this archaic, unicellular organism.
Bruhn
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Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Strasse 74, D-20359 Hamburg, Germany.
Leippe
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D000595:Amino Acid Sequence; D000818:Animals; D004748:Entamoeba histolytica / Q000235:genetics / Q000378:metabolism*; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism*; D007473:Ion Channels; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D021382:Protein Sorting Signals; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D049231:Saposins; D016415:Sequence Alignment; D055672:Static Electricity
D006023:Glycoproteins; D007473:Ion Channels; D008565:Membrane Proteins; D021382:Protein Sorting Signals; D015800:Protozoan Proteins; D049231:Saposins; C041670:amoebapore proteins, protozoan