Characterization of a Gene Coding for the Complement System Component FB from Loxosceles laeta Spider Venom Glands

• Published in: PloS one Vol. 11; no. 1; p. e0146992
• Main Authors: Myamoto, Daniela Tiemi, Pidde-Queiroz, Giselle, Gonçalves-de-Andrade, Rute Maria, Pedroso, Aurélio, van den Berg, Carmen W, Tambourgi, Denise V
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 15-01-2016; Public Library of Science (PLoS)
• Subjects: Alternative pathway; Amino acid sequence; Amino acids; Analysis; Animals; Catalysis; Chordata; Cloning; Complement; Complement C3 - genetics; Complement component C3; Complement Factor B - genetics; Complement Factor B - metabolism; Complement system; Genes; Genetic aspects; Glands; Homology; Immune system; Immunology; Laboratories; Lectins; Liquid oxygen; Magnesium; Mammals; Pathogens; Phylogeny; Physiological aspects; Primers; Protease; Proteins; Ribonucleic acid; RNA; Serine; Serine proteinase; Shellfish; Similarity; Spider Venoms - genetics; Spiders; Spiders - classification; Spiders - genetics; Thrombin; Venom; Venom gland; Venoms; Vertebrates; Von Willebrand factor; United States; Brazil
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0146992

The human complement system is composed of more than 30 proteins and many of these have conserved domains that allow tracing the phylogenetic evolution. The complement system seems to be initiated with the appearance of C3 and factor B (FB), the only components found in some protostomes and cnidarians, suggesting that the alternative pathway is the most ancient. Here, we present the characterization of an arachnid homologue of the human complement component FB from the spider Loxosceles laeta. This homologue, named Lox-FB, was identified from a total RNA L. laeta spider venom gland library and was amplified using RACE-PCR techniques and specific primers. Analysis of the deduced amino acid sequence and the domain structure showed significant similarity to the vertebrate and invertebrate FB/C2 family proteins. Lox-FB has a classical domain organization composed of a control complement protein domain (CCP), a von Willebrand Factor domain (vWFA), and a serine protease domain (SP). The amino acids involved in Mg2+ metal ion dependent adhesion site (MIDAS) found in the vWFA domain in the vertebrate C2/FB proteins are well conserved; however, the classic catalytic triad present in the serine protease domain is not conserved in Lox-FB. Similarity and phylogenetic analyses indicated that Lox-FB shares a major identity (43%) and has a close evolutionary relationship with the third isoform of FB-like protein (FB-3) from the jumping spider Hasarius adansoni belonging to the Family Salcitidae.