The cattle tick Rhipicephalus (Boophilus) microplus is one of the most harmful parasites affecting bovines. Similarly to other hematophagous ectoparasites, R. microplus saliva contains a collection of bioactive compounds that inhibit host defenses against tick feeding activity. Thus, the study of tick salivary components offers opportunities for the development of immunological based tick control methods and medicinal applications. So far, only a few proteins have been identified in cattle tick saliva. The aim of this work was to identify proteins present in R. microplus female tick saliva at different feeding stages. Proteomic analysis of R. microplus saliva allowed identifying peptides corresponding to 187 and 68 tick and bovine proteins, respectively. Our data confirm that (i) R. microplus saliva is complex, and (ii) that there are remarkable differences in saliva composition between partially engorged and fully engorged female ticks. R. microplus saliva is rich mainly in (i) hemelipoproteins and other transporter proteins, (ii) secreted cross-tick species conserved proteins, (iii) lipocalins, (iv) peptidase inhibitors, (v) antimicrobial peptides, (vii) glycine-rich proteins, (viii) housekeeping proteins and (ix) host proteins. This investigation represents the first proteomic study about R. microplus saliva, and reports the most comprehensive Ixodidae tick saliva proteome published to date. Our results improve the understanding of tick salivary modulators of host defense to tick feeding, and provide novel information on the tick-host relationship.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3998978 | PMC |
| http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0094831 | PLOS |
Publication Analysis
Top Keywords
Similar Publications
In vitro identification of neutralizing epitopes of Rhipicephalus microplus serpin 17 (RmS-17).
Vaccine
August 2024
Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), RS, Brazil; Faculdade de Veterinária, Universidade Federal do Rio Grande do Sul (UFRGS), RS, Brazil; Instituto Nacional de Ciência e Tecnologia - Entomologia Molecular, Rio de Janeiro, RJ, Brazil. Electronic address:
Background: Rhipicephalus microplus poses a significant problem for livestock worldwide and is primarily controlled with synthetic acaricides. The continuous use of acaricides results in the selection of resistance and causes environmental harm. Vaccination presents an alternative solution to this problem, although searching for the suitable antigen is still a work in progress.
View Article and Find Full Text PDFImmunologic characterization of the Bm05br protein using the Rhipicephalus linnaei (Audouin, 1826) species as a tick model.
Vet Parasitol
August 2024
Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Avenida Bento Gonçalves, 9500, Porto Alegre, RS 91501-970, Brazil; Faculdade de Veterinária, Universidade Federal do Rio Grande do Sul, Avenida Bento Gonçalves, 9090, Porto Alegre, RS 91540-000,, Brazil; Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular (INCT-EM), Rio de Janeiro, RJ 21941-853, Brazil. Electronic address:
The identification and characterization of tick proteins allow us to discover new physiological targets useful for the development of tick control methods. Bm05br (Brazil Rhipicephalus microplus protein 05) is a protein with unknown function identified in the saliva of R. microplus.
View Article and Find Full Text PDFRhipicephalus microplus thyropin-like protein: Structural and immunologic analyzes.
Vet Parasitol
April 2024
Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Avenida Bento Gonçalves, 9500, Prédio 43421, Porto Alegre 91501-970, RS, Brazil; Instituto Nacional de Ciência e Tecnologia - Entomologia Molecular, Rio de Janeiro, RJ, Brazil; Faculdade de Veterinária, Universidade Federal do Rio Grande do Sul, Avenida Bento Gonçalves, 9090, Porto Alegre 91540-000, RS, Brazil. Electronic address:
Tick saliva has a pivotal function in parasitism. It has pharmacological and immunomodulatory properties, with several proteins reported in its composition. Thyroglobulin type-1 domain protease inhibitor (thyropin)-like proteins are found in tick saliva, but their function, properties and structures are poorly characterized.
View Article and Find Full Text PDFChanges in saliva protein profile throughout Rhipicephalus microplus blood feeding.
Parasit Vectors
January 2024
Tick-Pathogen Transmission Unit, Laboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, Hamilton, MT, USA.
Background: When feeding on a vertebrate host, ticks secrete saliva, which is a complex mixture of proteins, lipids, and other molecules. Tick saliva assists the vector in modulating host hemostasis, immunity, and tissue repair mechanisms. While helping the vector to feed, its saliva modifies the site where pathogens are inoculated and often facilitates the infection process.
View Article and Find Full Text PDFBiochemical characterization of a novel sphingomyelinase-like protein from the Rhipicephalus microplus tick.
Exp Parasitol
November 2023
Departamento de Bioquímica, Escola Paulista de Medicina, Universidade de Federal de São Paulo (UNIFESP), São Paulo, SP, Brazil; Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular (INCT-EM), RJ, Brazil. Electronic address:
Sphingomyelinase D is a toxin present in venomous spiders and bacteria and is associated with infection symptoms in patients affected by spider bites. It was observed that in Ixodes scapularis ticks, sphingomyelinase-like protein secreted in saliva can modulate the host immune response, affecting the transmission of flavivirus to the host via exosomes. In this work, a sphingomyelinase D-like protein (RmSMase) from R.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!