title: Saliva from nymph and adult females of Haemaphysalis longicornis: a proteomic study.
abstract: BACKGROUND
  Haemaphysalis longicornis is a major vector of Theileria spp., Anaplasma phagocytophilum, Babesia spp. and Coxiella burnetti in East Asian countries. All life stages of ixodid ticks have a destructive pool-feeding style in which they create a pool-feeding site by lacerating host tissue and secreting a variety of biologically active compounds that allows the tick to evade host responses, enabling the uptake of a blood meal. The identification and functional characterization of tick saliva proteins can be useful to elucidate the molecular mechanisms involved in tick development and to conceive new anti-tick control methods.
  
  
  METHODS
  H. longicornis tick saliva was collected from fully engorged nymphs and fully engorged adults induced by dopamine or pilocarpine, respectively. Saliva was digested with trypsin for LC-MS/MS sequencing and peptides were searched against tick and rabbit sequences.
  
  
  RESULTS
  A total of 275 proteins were identified, of which 135 were tick and 100 were rabbit proteins. Of the tick proteins, 30 proteins were identified exclusively in fully engorged nymph saliva, 74 in fully engorged adult females, and 31 were detected in both stages. The identified tick proteins include heme/iron metabolism-related proteins, oxidation/detoxification proteins, enzymes, proteinase inhibitors, tick-specific protein families, and cytoskeletal proteins. Proteins involved in signal transduction, transport and metabolism of carbohydrate, energy, nucleotide, amino acids and lipids were also detected. Of the rabbit proteins, 13 were present in nymph saliva, 48 in adult saliva, and 30 were present in both. The host proteins include immunoglobulins, complement system proteins, antimicrobial proteins, serum albumin, peroxiredoxin, serotransferrin, apolipoprotein, hemopexin, proteinase inhibitors, and hemoglobin/red blood cells-related products.
  
  
  CONCLUSIONS
  This study allows the identification of H. longicornis saliva proteins. In spontaneously detached tick saliva various proteins were identified, although results obtained with saliva of fully engorged ticks need to be carefully interpreted. However, it is interesting to note that proteins identified in this study were also described in other tick saliva proteomes using partially engorged tick saliva, including hemelipoprotein, proteases, protease inhibitors, proteins related to structural functions, transporter activity, metabolic processes, and others. In conclusion, these data can provide a deeper understanding to the biology of H. longicornis.
authors.affiliation: Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil. ltirloni@gmail.com.
authors.forename: Lucas
authors.initials: L
authors.lastname: Tirloni
authors.affiliation: Department of Veterinary Parasitology, College of Veterinary Medicine and Bio-safety Research Centre, Chonbuk National University, Jeonju, Republic of Korea. saifulhstu@gmail.com.|Department of Medicine, Surgery and Obstetrics, Faculty of Veterinary and Animal Science, Hajee Mohammad Danesh Science and Technology University, Dinajpur, Bangladesh. saifulhstu@gmail.com.
authors.forename: Mohammad Saiful
authors.initials: MS
authors.lastname: Islam
authors.affiliation: Department of Veterinary Pathobiology, College of Veterinary Medicine, Texas A&M University, College Station, TX, USA. taekim009@gmail.com.
authors.forename: Tae Kwon
authors.initials: TK
authors.lastname: Kim
authors.affiliation: Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA, USA. jdiedric@scripps.edu.
authors.forename: Jolene K
authors.initials: JK
authors.lastname: Diedrich
authors.affiliation: Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA, USA. jyates@scripps.edu.
authors.forename: John R
authors.initials: JR
authors.lastname: Yates
authors.affiliation: Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA, USA. pinto.afm@gmail.com.|Centro de Pesquisas em Biologia Molecular e Funcional, Instituto Nacional de Ciência e Tecnologia em Tuberculose (INCT-TB), Pontifícia Universidade Católica do Rio Grande do Sul (PUCRS), Porto Alegre, RS, Brazil. pinto.afm@gmail.com.
authors.forename: Antônio F M
authors.initials: AF
authors.lastname: Pinto
authors.affiliation: Department of Veterinary Pathobiology, College of Veterinary Medicine, Texas A&M University, College Station, TX, USA. AMulenga@cvm.tamu.edu.
authors.forename: Albert
authors.initials: A
authors.lastname: Mulenga
authors.affiliation: Department of Veterinary Parasitology, College of Veterinary Medicine and Bio-safety Research Centre, Chonbuk National University, Jeonju, Republic of Korea. tick@jbnu.ac.kr.
authors.forename: Myung-Jo
authors.initials: MJ
authors.lastname: You
authors.affiliation: Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil. itabajara.vaz@ufrgs.br.|Faculdade de Veterinária, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil. itabajara.vaz@ufrgs.br.
authors.forename: Itabajara
authors.initials: I
authors.lastname: Da Silva Vaz
mesh_terms: D000818:Animals; D060829:Arthropod Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D005260:Female; D026863:Ixodidae / Q000737:chemistry / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism*; D008297:Male; D009758:Nymph / Q000737:chemistry / Q000235:genetics / Q000254:growth & development / Q000378:metabolism; D020543:Proteome / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D040901:Proteomics; D011817:Rabbits; D012463:Saliva / Q000737:chemistry; D012471:Salivary Proteins and Peptides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D060829:Arthropod Proteins; D020543:Proteome; D012471:Salivary Proteins and Peptides