title: Stage-specific expression of a Schistosoma mansoni polypeptide similar to the vertebrate regulatory protein stathmin.
abstract: The ubiquitous vertebrate protein stathmin is expressed and phosphorylated in response to a variety of external and internal signals. Stathmin, in turn, controls cell growth and differentiation through its capacity to regulate microtubule assembly dynamics. This is the first report on the molecular cloning and characterization of a stathmin-like protein (SmSLP) in an invertebrate, the human blood fluke Schistosoma mansoni. SmSLP is first synthesized at high levels in the intermediate molluscan host and completely disappears 48 h after penetration into the mammalian host. The protein is preferentially iodinated in intact immature parasites using the Bolton-Hunter reagent, can be quantitatively extracted in high salt buffers, and remains soluble after boiling. Native SmSLP was partially sequenced, and its complete structure was derived from the cloning and sequencing of its cDNA. The sequence is up to 26% identical to vertebrate stathmin sequences and contains two potential phosphorylation sites. Native SmSLP is indeed phosphorylated because phosphatase digestion shifts its mobility in electrofocusing gels. SmSLP associates with tubulin, as suggested by immune co-precipitation results. In vitro experiments demonstrated that SmSLP inhibits tubulin assembly and causes the depolymerization of preassembled microtubules, thus probably fulfilling regulatory roles in critical steps of schistosome development.
authors.affiliation: Institute of Cell Biology, National Research Council, 43 Viale Marx, 00137 Rome, Italy.
authors.forename: C
authors.initials: C
authors.lastname: Valle
authors.forename: A
authors.initials: A
authors.lastname: Festucci
authors.forename: A
authors.initials: A
authors.lastname: Calogero
authors.forename: P
authors.initials: P
authors.lastname: Macrì
authors.forename: B
authors.initials: B
authors.lastname: Mecozzi
authors.forename: P
authors.initials: P
authors.lastname: Liberti
authors.forename: D
authors.initials: D
authors.lastname: Cioli
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D018507:Gene Expression Regulation, Developmental; D006031:Glycosylation; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008018:Life Cycle Stages; D051379:Mice; D008868:Microtubule Proteins; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000235:genetics*; D012550:Schistosoma mansoni / Q000737:chemistry / Q000235:genetics* / Q000254:growth & development; D016415:Sequence Alignment; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D012908:Snails / Q000378:metabolism / Q000469:parasitology; D050777:Stathmin; D013388:Succinimides; D014404:Tubulin / Q000378:metabolism; D014714:Vertebrates
chemical_list: D018076:DNA, Complementary; D015801:Helminth Proteins; D008868:Microtubule Proteins; D010750:Phosphoproteins; D050777:Stathmin; C493994:Stmn1 protein, mouse; D013388:Succinimides; D014404:Tubulin; C022581:Bolton-Hunter reagent