PMID- 29312895 OWN - NLM STAT- MEDLINE DCOM- 20181217 LR - 20190307 IS - 2235-2988 (Electronic) IS - 2235-2988 (Linking) VI - 7 DP - 2017 TI - Tick-Host Range Adaptation: Changes in Protein Profiles in Unfed Adult Ixodes scapularis and Amblyomma americanum Saliva Stimulated to Feed on Different Hosts. PG - 517 LID - 10.3389/fcimb.2017.00517 [doi] LID - 517 AB - Understanding the molecular basis of how ticks adapt to feed on different animal hosts is central to understanding tick and tick-borne disease (TBD) epidemiology. There is evidence that ticks differentially express specific sets of genes when stimulated to start feeding. This study was initiated to investigate if ticks such as Ixodes scapularis and Amblyomma americanum that are adapted to feed on multiple hosts utilized the same sets of proteins to prepare for feeding. We exposed I. scapularis and A. americanum to feeding stimuli of different hosts (rabbit, human, and dog) by keeping unfed adult ticks enclosed in a perforated microfuge in close contact with host skin, but not allowing ticks to attach on host. Our data suggest that ticks of the same species differentially express tick saliva proteins (TSPs) when stimulated to start feeding on different hosts. SDS-PAGE and silver staining analysis revealed unique electrophoretic profiles in saliva of I. scapularis and A. americanum that were stimulated to feed on different hosts: rabbit, human, and dog. LC-MS/MS sequencing and pairwise analysis demonstrated that I. scapularis and A. americanum ticks expressed unique protein profiles in their saliva when stimulated to start feeding on different hosts: rabbit, dog, or human. Specifically, our data revealed TSPs that were unique to each treatment and those that were shared between treatments. Overall, we identified a total of 276 and 340 non-redundant I. scapularis and A. americanum TSPs, which we have classified into 28 functional classes including: secreted conserved proteins (unknown functions), proteinase inhibitors, lipocalins, extracellular matrix/cell adhesion, heme/iron metabolism, signal transduction and immunity-related proteins being the most predominant in saliva of unfed ticks. With exception of research on vaccines against Rhipicephalus microplus, which its natural host, cattle, research on vaccine against other ticks relies feeding ticks on laboratory animals. Data here suggest that relying on lab animal tick feeding data to select target antigens could result in prioritizing irrelevant anti-tick vaccine targets that are expressed when ticks feed on laboratory animals. This study provides the platform that could be utilized to identify relevant target anti-tick vaccine antigens, and will facilitate early stage tick feeding research. FAU - Tirloni, Lucas AU - Tirloni L AD - Department of Veterinary Pathobiology, College of Veterinary Medicine, Texas A&M University, College Station, TX, United States. AD - Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil. FAU - Kim, Tae K AU - Kim TK AD - Department of Veterinary Pathobiology, College of Veterinary Medicine, Texas A&M University, College Station, TX, United States. FAU - Pinto, Antonio F M AU - Pinto AFM AD - Mass Spectrometry Center, The Salk Institute for Biological Studies, La Jolla, CA, United States. AD - Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA, United States. FAU - Yates, John R 3rd AU - Yates JR 3rd AD - Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA, United States. FAU - da Silva Vaz, Itabajara Jr AU - da Silva Vaz I Jr AD - Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil. AD - Faculdade de Veterinaria, Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil. FAU - Mulenga, Albert AU - Mulenga A AD - Department of Veterinary Pathobiology, College of Veterinary Medicine, Texas A&M University, College Station, TX, United States. LA - eng GR - P41 GM103533/GM/NIGMS NIH HHS/United States GR - R01 AI093858/AI/NIAID NIH HHS/United States GR - R03 AI074789/AI/NIAID NIH HHS/United States GR - R21 AI081093/AI/NIAID NIH HHS/United States PT - Journal Article PT - Research Support, N.I.H., Extramural PT - Research Support, Non-U.S. Gov't DEP - 20171219 PL - Switzerland TA - Front Cell Infect Microbiol JT - Frontiers in cellular and infection microbiology JID - 101585359 RN - 0 (Arthropod Proteins) RN - 0 (Proteome) RN - 0 (Salivary Proteins and Peptides) SB - IM MH - Animals MH - Arthropod Proteins/*analysis MH - Chromatography, Liquid MH - Dogs MH - Electrophoresis, Polyacrylamide Gel MH - *Host Specificity MH - Humans MH - Ixodidae/*physiology MH - Proteome/analysis MH - Rabbits MH - Saliva/*chemistry MH - Salivary Proteins and Peptides/*analysis MH - Tandem Mass Spectrometry PMC - PMC5742094 OTO - NOTNLM OT - host adaptation OT - proteomic OT - saliva OT - tick OT - tick-host relationship EDAT- 2018/01/10 06:00 MHDA- 2018/12/18 06:00 PMCR- 2017/01/01 CRDT- 2018/01/10 06:00 PHST- 2017/08/30 00:00 [received] PHST- 2017/12/04 00:00 [accepted] PHST- 2018/01/10 06:00 [entrez] PHST- 2018/01/10 06:00 [pubmed] PHST- 2018/12/18 06:00 [medline] PHST- 2017/01/01 00:00 [pmc-release] AID - 10.3389/fcimb.2017.00517 [doi] PST - epublish SO - Front Cell Infect Microbiol. 2017 Dec 19;7:517. doi: 10.3389/fcimb.2017.00517. eCollection 2017.