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      Saliva from nymph and adult females of Haemaphysalis longicornis: a proteomic study

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          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.

          Electronic supplementary material

          The online version of this article (doi:10.1186/s13071-015-0918-y) contains supplementary material, which is available to authorized users.

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          Most cited references142

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          Phospholipase A2 structure/function, mechanism, and signaling.

          Tremendous advances in understanding the structure and function of the superfamily of phospholipase A2 (PLA2) enzymes has occurred in the twenty-first century. The superfamily includes 15 groups comprising four main types including the secreted sPLA2, cytosolic cPLA2, calcium-independent iPLA2, and platelet activating factor (PAF) acetyl hydrolase/oxidized lipid lipoprotein associated (Lp)PLA2. We review herein our current understanding of the structure and interaction with substrate phospholipids, which resides in membranes for a representative of each of these main types of PLA2. We will also briefly review the development of inhibitors of these enzymes and their roles in lipid signaling.
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            Role of arthropod saliva in blood feeding: sialome and post-sialome perspectives.

            This review addresses the problems insects and ticks face to feed on blood and the solutions these invertebrates engender to overcome these obstacles, including a sophisticated salivary cocktail of potent pharmacologic compounds. Recent advances in transcriptome and proteome research allow an unprecedented insight into the complexity of these compounds, indicating that their molecular diversity as well as the diversity of their targets is still larger than previously thought.
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              Moonlighting proteins: an intriguing mode of multitasking.

              Proteins are macromolecules, which perform a large variety of functions. Most of them have only a single function, but an increasing number of proteins are being identified as multifunctional. Moonlighting proteins form a special class of multifunctional proteins. They perform multiple autonomous and often unrelated functions without partitioning these functions into different domains of the protein. Striking examples are enzymes, which in addition to their catalytic function are involved in fully unrelated processes such as autophagy, protein transport or DNA maintenance. In this contribution we present an overview of our current knowledge of moonlighting proteins and discuss the significant implications for biomedical and fundamental research. 2010 Elsevier B.V. All rights reserved.
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                Author and article information

                Contributors
                ltirloni@gmail.com
                saifulhstu@gmail.com
                taekim009@gmail.com
                jdiedric@scripps.edu
                jyates@scripps.edu
                pinto.afm@gmail.com
                AMulenga@cvm.tamu.edu
                tick@jbnu.ac.kr
                +55 51 3308 6078 , itabajara.vaz@ufrgs.br
                Journal
                Parasit Vectors
                Parasit Vectors
                Parasites & Vectors
                BioMed Central (London )
                1756-3305
                24 June 2015
                24 June 2015
                2015
                : 8
                : 338
                Affiliations
                [ ]Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS Brazil
                [ ]Department of Veterinary Parasitology, College of Veterinary Medicine and Bio-safety Research Centre, Chonbuk National University, Jeonju, Republic of Korea
                [ ]Department of Medicine, Surgery and Obstetrics, Faculty of Veterinary and Animal Science, Hajee Mohammad Danesh Science and Technology University, Dinajpur, Bangladesh
                [ ]Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA USA
                [ ]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
                [ ]Department of Veterinary Pathobiology, College of Veterinary Medicine, Texas A&M University, College Station, TX USA
                [ ]Faculdade de Veterinária, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS Brazil
                Article
                918
                10.1186/s13071-015-0918-y
                4484640
                26104117
                b75678e2-6416-45ea-befd-9db64c970a07
                © Tirloni et al. 2015

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

                History
                : 29 March 2015
                : 27 May 2015
                Categories
                Research
                Custom metadata
                © The Author(s) 2015

                Parasitology
                tick,proteomic,saliva,tick-host relationship
                Parasitology
                tick, proteomic, saliva, tick-host relationship

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