Proteomic analysis of cattle tick Rhipicephalus (Boophilus) microplus saliva: a comparison between partially and fully engorged females.
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.
Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil; Department of Entomology, Texas A&M University, College Station, Texas, United States of America.
Lucas
L
Tirloni
Instituto de Pesquisas Veterinárias Desidério Finamor, Fundação Estadual de Pesquisa Agropecuária, Eldorado do Sul, RS, Brazil.
José
J
Reck
Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil; Department of Microbiology, University of Virginia, Charlottesville, Virginia, United States of America; CAPES, Ministério da Educação do Brasil, Brasília, DF, Brasil.
Renata Maria Soares
RM
Terra
Instituto de Pesquisas Veterinárias Desidério Finamor, Fundação Estadual de Pesquisa Agropecuária, Eldorado do Sul, RS, Brazil.
João Ricardo
JR
Martins
Department of Entomology, Texas A&M University, College Station, Texas, United States of America.
Albert
A
Mulenga
Department of Microbiology, University of Virginia, Charlottesville, Virginia, United States of America.
Nicholas E
NE
Sherman
Department of Microbiology, University of Virginia, Charlottesville, Virginia, United States of America.
Jay W
JW
Fox
Department of Chemical Physiology, The Scripps Research Institute, La Jolla, California, United States of America.
John R
JR
Yates
Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil; Departamento de Bioquímica, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil.
Carlos
C
Termignoni
Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil; Department of Microbiology, University of Virginia, Charlottesville, Virginia, United States of America; CAPES, Ministério da Educação do Brasil, Brasília, DF, Brasil.
Antônio F M
AF
Pinto
Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil; Faculdade de Veterinária, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil.
Itabajara da Silva
Ida S
Vaz
D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000378:metabolism; D060829:Arthropod Proteins / Q000378:metabolism*; D002417:Cattle; D015891:Cystatins / Q000378:metabolism; D005260:Female; D020043:Genes, Essential; D054834:Lipocalins / Q000378:metabolism; D008074:Lipoproteins / Q000378:metabolism; D019518:Postprandial Period; D053491:Proteinase Inhibitory Proteins, Secretory / Q000378:metabolism; D020543:Proteome / Q000378:metabolism*; D048494:Rhipicephalus / Q000378:metabolism*; D012463:Saliva / Q000378:metabolism*
D023181:Antimicrobial Cationic Peptides; D060829:Arthropod Proteins; D015891:Cystatins; D054834:Lipocalins; D008074:Lipoproteins; D053491:Proteinase Inhibitory Proteins, Secretory; D020543:Proteome