title: Reprolysin metalloproteases from Ixodes persulcatus, Rhipicephalus sanguineus and Rhipicephalus microplus ticks.
abstract: Metalloproteases (MPs) have been considered essential for blood feeding and other physiological functions in several hematophagous animals, including ticks. We report the characterization of MP sequences of three important ticks from Asia, Africa and America: Ixodes persulcatus (Ip-MPs), Rhipicephalus sanguineus (Rs-MPs) and R. microplus (BrRm-MPs). Amino acid sequence identity between R. microplus and R. sanguineus MPs ranged from 76 to 100 %, and identities among I. persulcatus, I. ricinus and I. scapularis MP sequences ranged from 88 to 97 %. This high sequence identity and typical functional motifs show that all sequences are MPs. The presence of a zinc binding site, a Met-turn and cysteine rich domain at the C-terminal region indicates that these proteins belong to the reproplysin family of MPs. Differences in amino acid sequences of BrRm-MP1, BrRm-MP2, BrRm-MP4 and BrRm-MP5 (from Porto Alegre strain ticks) were 6, 2, 7 and 5 %, respectively, when compared with sequences deposited in GenBank for the same genes from other R. microplus isolates. Analyses of MPs predicted that they have various highly antigenic regions. Semi-quantitative RT-PCR analysis revealed the presence of transcripts in salivary glands of partially and fully fed female ticks. None of these transcripts were observed in males (except BrRm-MP4) and eggs. These enzymes may be functional components required during tick feeding to manipulate host defenses and support tick hematophagy.
authors.affiliation: Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Avenida Bento Gonçalves, 9500, Prédio 43421, C.P. 15005, Porto Alegre, RS, 91501-970, Brazil.
authors.forename: Abid
authors.initials: A
authors.lastname: Ali
authors.forename: Lucas
authors.initials: L
authors.lastname: Tirloni
authors.forename: Masayoshi
authors.initials: M
authors.lastname: Isezaki
authors.forename: Adriana
authors.initials: A
authors.lastname: Seixas
authors.forename: Satoru
authors.initials: S
authors.lastname: Konnai
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Ohashi
authors.forename: Itabajara
authors.initials: I
authors.lastname: da Silva Vaz Junior
authors.forename: Carlos
authors.initials: C
authors.lastname: Termignoni
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D005260:Female; D026863:Ixodidae / Q000201:enzymology* / Q000235:genetics; D008297:Male; D045726:Metalloproteases / Q000235:genetics*; D008969:Molecular Sequence Data; D010802:Phylogeny; D012313:RNA / Q000737:chemistry / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction / Q000662:veterinary; D012469:Salivary Glands / Q000201:enzymology*; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
chemical_list: D012313:RNA; D045726:Metalloproteases