The serine-rich Entamoeba histolytica protein is a phosphorylated membrane protein containing O-linked terminal N-acetylglucosamine residues

• Published in: The Journal of biological chemistry Vol. 270; no. 8; pp. 4121 - 4126
• Main Authors: Stanley, S.L. Jr. (Washington University School of Medicine, St. Louis, MO.), Tian, K, Koester, J.P, Li, E
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 24.02.1995
• Subjects: Acetylglucosamine - analysis; Acylation; Amino Acid Sequence; AMINOAZUCARES; AMINOSUCRE; Animals; BACULOVIRIDAE; Baculoviridae - genetics; Base Sequence; Cells, Cultured; Chemotactic Factors; Cloning, Molecular; DNA Primers; ENTAMOEBA; Entamoeba histolytica; Entamoeba histolytica - metabolism; Esters; EXPRESION GENICA; EXPRESSION DES GENES; FOSFORILACION; Glycosylation; Immunohistochemistry; MECANISME CHIMIOTACTIQUE; Membrane Proteins - chemistry; Membrane Proteins - genetics; Membrane Proteins - metabolism; Molecular Sequence Data; PHOSPHORYLATION; Protein Processing, Post-Translational; PROTEINAS; PROTEINE; Protozoan Proteins - chemistry; Protozoan Proteins - genetics; Protozoan Proteins - metabolism; QUIMIOTACTISMO; SERINA; SERINE; Spodoptera; TRANSFORMACION GENETICA; TRANSFORMATION GENETIQUE
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.270.8.4121

Previously, we described the isolation of a cDNA clone and the gene encoding a protective antigen of the protozoan parasite Entamoeba histolytica, the serine-rich Entamoeba histolytica protein (SREHP). The derived amino acid sequence of the SREHP cDNA clone was remarkable for a high serine content (52/233 amino acids), a putative signal sequence, multiple hydrophilic dodecapeptide and octapeptide tandem repeats, and a hydrophobic C-terminal putative membrane-spanning region. Here, we show that SREHP is modified by the addition of phosphate at serine residues, O-linked terminal N-acetylglucosamine residues, and by acylation. When the SREHP gene is expressed in baculovirus transformed Sf-9 cells, the product is also phosphorylated and glycosylated and is localized to the plasma membrane of the insect cells. The native SREHP molecule also serves as a potent chemoattractant for amebic trophozoites. The data presented here suggest that SREHP is a unique membrane protein with phosphorylation and glycosylation patterns usually associated with nuclear or cytoplasmic proteins