title: How schistosomes alter the human serum proteome.
abstract: Schistosomes are intravascular parasitic worms that cause the debilitating disease schistosomiasis. To better understand how these long-lived parasites may subvert host immune and hemostatic capabilities, we examine here the impact of adult Schistosoma mansoni worms on the human serum proteome. Normal human serum (150μl) was incubated at 37°C for one hour either in the presence or absence of adult worms (∼50 pairs). Thereafter parasites were removed, serum samples were labeled and their proteins resolved for comparative analysis by 2D-Differential in-Gel Electrophoresis (2D-DIGE). Several differences were noted between the two samples. Twenty protein spots were recovered and identified following trypsin digestion and mass spectroscopy. Strikingly, most of these (11/20) are associated with the complement system and include complement components C3, C4, factor B, complement factor H related protein 1 and clusterin. Western blot analysis confirms the impact of the worms on C3, C4 and factor B in serum. The data suggest that schistosomes engage complement but can rapidly degrade selected complement proteins which may help explain the worm's refractoriness towards complement-mediated attack. Other serum proteins identified as being impinged upon by schistosomes are alpha 2 macroglobulin, alpha 1 anti-chymotrypsin, actin cytoplasmic 2, serum amyloid A-4, protein DDX26B, hemoglobin subunit B and serum albumin. While the molecular nature of the interaction between these proteins and schistosomes is not known, possible roles for some of them in hemostasis, immune evasion and in the host response to serum stress are suggested.
authors.affiliation: Molecular Helminthology Laboratory, Department of Infectious Disease and Global Health, Cummings School of Veterinary Medicine, Tufts University, North Grafton, MA 01536, USA. Electronic address: Akram.Da_darah@Tufts.edu.
authors.forename: Akram A
authors.initials: AA
authors.lastname: Da'dara
authors.affiliation: Molecular Helminthology Laboratory, Department of Infectious Disease and Global Health, Cummings School of Veterinary Medicine, Tufts University, North Grafton, MA 01536, USA. Electronic address: Giles.Siddons@Tufts.edu.
authors.forename: Giles
authors.initials: G
authors.lastname: Siddons
authors.affiliation: Molecular Helminthology Laboratory, Department of Infectious Disease and Global Health, Cummings School of Veterinary Medicine, Tufts University, North Grafton, MA 01536, USA. Electronic address: Melissa.Icaza@Tufts.edu.
authors.forename: Melissa
authors.initials: M
authors.lastname: Icaza
authors.affiliation: Molecular Helminthology Laboratory, Department of Infectious Disease and Global Health, Cummings School of Veterinary Medicine, Tufts University, North Grafton, MA 01536, USA. Electronic address: Qiang.Wang@Tufts.edu.
authors.forename: Qiang
authors.initials: Q
authors.lastname: Wang
authors.affiliation: Molecular Helminthology Laboratory, Department of Infectious Disease and Global Health, Cummings School of Veterinary Medicine, Tufts University, North Grafton, MA 01536, USA. Electronic address: Patrick.Skelly@Tufts.edu.
authors.forename: Patrick J
authors.initials: PJ
authors.lastname: Skelly
mesh_terms: D000818:Animals; D001798:Blood Proteins / Q000032:analysis*; D015153:Blotting, Western; D015180:Electrophoresis, Gel, Two-Dimensional; D054884:Host-Pathogen Interactions; D006801:Humans; D013058:Mass Spectrometry; D020543:Proteome / Q000032:analysis*; D012550:Schistosoma mansoni / Q000502:physiology*; D044967:Serum / Q000737:chemistry* / Q000469:parasitology*; D013696:Temperature
chemical_list: D001798:Blood Proteins; D020543:Proteome
keywords: Complement; Host-parasite interaction; Schistosoma; Serum proteomics