title: Silkomics: Insight into the Silk Spinning Process of Spiders.
abstract: The proteins from the silk-producing glands were identified using both a bottom-up gel-based proteomic approach as well as from a shotgun proteomic approach. Additionally, the relationship between the functions of identified proteins and the spinning process was studied. A total of 125 proteins were identified in the major ampullate, 101 in the flagelliform, 77 in the aggregate, 75 in the tubuliform, 68 in the minor ampullate, and 23 in aciniform glands. On the basis of the functional classification using Gene Ontology, these proteins were organized into seven different groups according to their general function: (i) web silk proteins-spidroins, (ii) proteins related to the folding/conformation of spidroins, (iii) proteins that protect silk proteins from oxidative stress, (iv) proteins involved in fibrillar preservation of silks in the web, (v) proteins related to ion transport into and out of the glands during silk fiber spinning, (vi) proteins involved in prey capture and pre-digestion, and (vii) housekeeping proteins from all of the glands. Thus, a general mechanism of action for the identified proteins in the silk-producing glands from the Nephila clavipes spider was proposed; the current results also indicate that the webs play an active role in prey capture.
authors.affiliation: Center of Study of Social Insects, Department of Biology, Institute of Biosciences of Rio Claro, São Paulo State University (UNESP) , Rio Claro, São Paulo 13500, Brazil.|Department of Pediatrics, Medical University of Vienna , Vienna 1090, Austria.
authors.forename: José Roberto Aparecido
authors.initials: JR
authors.lastname: Dos Santos-Pinto
authors.affiliation: Center of Study of Social Insects, Department of Biology, Institute of Biosciences of Rio Claro, São Paulo State University (UNESP) , Rio Claro, São Paulo 13500, Brazil.
authors.forename: Ana Maria Caviquioli
authors.initials: AM
authors.lastname: Garcia
authors.affiliation: Center of Study of Social Insects, Department of Biology, Institute of Biosciences of Rio Claro, São Paulo State University (UNESP) , Rio Claro, São Paulo 13500, Brazil.
authors.forename: Helen Andrade
authors.initials: HA
authors.lastname: Arcuri
authors.affiliation: Center of Study of Social Insects, Department of Biology, Institute of Biosciences of Rio Claro, São Paulo State University (UNESP) , Rio Claro, São Paulo 13500, Brazil.
authors.forename: Franciele Grego
authors.initials: FG
authors.lastname: Esteves
authors.affiliation: Center of Study of Social Insects, Department of Biology, Institute of Biosciences of Rio Claro, São Paulo State University (UNESP) , Rio Claro, São Paulo 13500, Brazil.
authors.forename: Heliana Clara
authors.initials: HC
authors.lastname: Salles
authors.affiliation: Department of Pediatrics, Medical University of Vienna , Vienna 1090, Austria.
authors.forename: Gert
authors.initials: G
authors.lastname: Lubec
authors.affiliation: Center of Study of Social Insects, Department of Biology, Institute of Biosciences of Rio Claro, São Paulo State University (UNESP) , Rio Claro, São Paulo 13500, Brazil.
authors.forename: Mario Sergio
authors.initials: MS
authors.lastname: Palma
mesh_terms: D000595:Amino Acid Sequence; D000825:Animal Structures / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D000818:Animals; D015870:Gene Expression; D063990:Gene Ontology; D019476:Insect Proteins / Q000145:classification / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D008968:Molecular Conformation; D058977:Molecular Sequence Annotation; D040901:Proteomics; D047011:Silk / Q000737:chemistry* / Q000378:metabolism; D013112:Spiders / Q000502:physiology*
chemical_list: D019476:Insect Proteins; D047011:Silk
keywords: Nephila clavipes; bottom-up gel-based proteomic approach; shotgun proteomic approach; silk proteins; silk-producing glands