Description of Loxtox protein family and identification of a new group of Phospholipases D from Loxosceles similis venom gland

• Published in: Toxicon (Oxford) 2016-09, Vol.120, p.97-106
• Main Authors: Dantas, Arthur Estanislau, Carmo, A.O., Horta, Carolina Campolina Rebello, Leal, Hortênsia Gomes, Oliveira-Mendes, Bárbara Bruna Ribeiro, Martins, Ana Paula Vimieiro, Chávez-Olórtegui, Carlos, Kalapothakis, Evanguedes
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Araneae; Bioinformatics; Brown Recluse Spider; Catalysis; Gene sequencing; High-Throughput Nucleotide Sequencing; Insect Proteins - genetics; Insect Proteins - metabolism; Loxosceles; Loxosceles similis; Loxtox; NGS; Pharmacology; Phospholipase; Phospholipase D; Phospholipase D - genetics; Phospholipase D - metabolism; Phosphoric Diester Hydrolases - genetics; Phylogeny; Proteins; Public health; RNA-seq; Sequence Homology, Amino Acid; Spider Venoms - enzymology; Spider Venoms - genetics; Spiders; Venom
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/j.toxicon.2016.08.002

Envenoming resulting from Loxosceles spider bites (loxoscelism) is a recognized public health problem in Brazil. However, the pathophysiology of loxoscelism caused by L. similis bites, which is widespread in Brazil, remains poorly understood. In the present work, the RNA sequencing (RNA-Seq – Next Generation sequencing - NGS) of the L. similis venom gland was performed to identify and analyze the sequences of the key component phospholipase D. The sequences were aligned based on their classical domains, and a phylogenetic tree was constructed. In the bioinformatics analysis, 23 complete sequences of phospholipase D proteins were found and classified as Loxtox proteins, as they contained the characteristic domains of phospholipase D: the active site, the Mg2+-binding domain, and the catalytic loop. Three phospholipase D sequences with non-canonical domains were also found in this work. They were analyzed separately and named PLDs from L. similis (PLD-Ls). This study is the first to characterize phospholipase D sequences from Loxosceles spiders by RNA-Seq. These results contribute new knowledge about the composition of L. similis venom, revealing novel tools that could be used for pharmacological, immunological, and biotechnological applications. •Characterization of 23 complete Loxtox proteins and 8 incomplete protein sequences from the Loxosceles similis spider.•Analysis of the expression pattern of each described Loxtox protein.•Identification of a new group of Phospholipases D for Loxosceles.