title: Peritrophic membrane protein in the larval stingless bee Melipona quadrifasciata anthidioides: immunolocalization of secretory sites.
abstract: The origin of the peritrophic membrane (PM) in bees is still a matter of debate. It is either of type I (synthesized by the entire midgut epithelium) or of type II (released from the anterior midgut end). The present study identified secretory sites of peritrophin-55 kDa, a PM protein in larvae of Melipona quadrifasciata anthidioides. Peritrophin-55 was isolated from PMs and was used for the production of a polyclonal antibody. Our study demonstrates the presence of peritrophin-55 in vesicles and on microvilli of digestive cells and in the PM. It suggests that the PM is of type-I, being specific for the larval phase of this stingless bee.
authors.affiliation: Departamento de Biologia Animal, Setor de Entomologia, Universidade Federal de Viçosa, MG, Brazil.
authors.forename: Solange
authors.initials: S
authors.lastname: Marques-Silva
authors.forename: José Eduardo
authors.initials: JE
authors.lastname: Serrão
authors.forename: José Mario S
authors.initials: JM
authors.lastname: Mezêncio
mesh_terms: D000818:Animals; D001516:Bees; D002462:Cell Membrane / Q000737:chemistry / Q000648:ultrastructure; D004064:Digestive System / Q000737:chemistry / Q000648:ultrastructure; D005455:Fluorescent Antibody Technique; D007150:Immunohistochemistry; D019476:Insect Proteins / Q000032:analysis / Q000096:biosynthesis* / Q000378:metabolism; D007814:Larva; D008562:Membrane Glycoproteins / Q000032:analysis / Q000096:biosynthesis* / Q000378:metabolism; D008871:Microvilli / Q000737:chemistry / Q000648:ultrastructure; D013194:Staining and Labeling; D022161:Transport Vesicles / Q000737:chemistry / Q000648:ultrastructure
chemical_list: D019476:Insect Proteins; D008562:Membrane Glycoproteins