Rhipicephalus microplus lipocalins (LRMs): genomic identification and analysis of the bovine immune response using in silico predicted B and T cell epitopes

Rodriguez-Valle, Manuel, Moolhuijzen, Paula, Piper, Emily K., Weiss, Olivia, Vance, Megan, Bellgard, Matthew and Lew-Tabor, Ala (2013) Rhipicephalus microplus lipocalins (LRMs): genomic identification and analysis of the bovine immune response using in silico predicted B and T cell epitopes. International Journal for Parasitology, 43 9: 739-752. doi:10.1016/j.ijpara.2013.04.005


Author Rodriguez-Valle, Manuel
Moolhuijzen, Paula
Piper, Emily K.
Weiss, Olivia
Vance, Megan
Bellgard, Matthew
Lew-Tabor, Ala
Title Rhipicephalus microplus lipocalins (LRMs): genomic identification and analysis of the bovine immune response using in silico predicted B and T cell epitopes
Formatted title
Rhipicephalus microplus lipocalins (LRMs): genomic identification and analysis of the bovine immune response using in silico predicted B and T cell epitopes
Journal name International Journal for Parasitology   Check publisher's open access policy
ISSN 0020-7519
1879-0135
Publication date 2013-08-01
Sub-type Article (original research)
DOI 10.1016/j.ijpara.2013.04.005
Volume 43
Issue 9
Start page 739
End page 752
Total pages 14
Place of publication United Kingdom
Publisher Elsevier
Collection year 2014
Language eng
Formatted abstract
Highlights
• In silico analysis of the Rhipicephalus microplus genome database identified 12 lipocalins.
• B and T cell epitopes were predicted within this lipocalin family.
• The dynamic interactions of epitopes with the bovine immune system were studied.
Bos taurus and Bos indicus lymphocytes showed differential cytokine expression patterns.

The attachment to host skin by Rhipicephalus microplus larvae induces a series of physiological events at the attachment site. The host–parasite interaction might induce a rejection of the larvae, as is frequently observed in Bos taurus indicus cattle, and under certain conditions in Bos taurus taurus cattle. Ticks deactivate the host rejection response by secreting specific proteins and lipids that play an essential role in manipulation of the host immune response. The available genomic information on the R. microplus tick was mined using bioinformatics approaches to identify R. microplus lipocalins (LRMs). This in silico examination revealed a total of 12 different putative R. microplus LRMs (LRM1–LRM12). The identity of the LRM family showed high sequence variability: from 6% between LRM7 and LRM8 to 55.9% between LRM2 and LRM6. However, the three-dimensional structure of the lipocalin family was conserved in the LRMs. The B and T cell epitopes in these lipocalins were then predicted, and six of the LRMs (5, 6, 9, 10, 11 and 12) were used to examine the host immune interactions with sera and peripheral blood mononuclear cells (PBMCs) collected from tick-susceptible and tick-resistant cattle challenged with R. microplus. On days 28–60 after tick infestation, the anti-LRM titres were higher in the resistant group compared with the susceptible cattle. After 60 day, the anti-LRM titres (except LRM9 and LRM11) decreased to zero in the sera of both the tick-resistant and tick-susceptible cattle. Using cell proliferation assays, the PBMCs challenged with some of the predicted T cell epitopes (LRM1_T1, T2; LRM_T1, T2 and LRM12_T) exhibited a significantly higher number of IFN-γ-secreting cells (Th1) in tick-susceptible Holstein–Friesians compared with tick-resistant Brahman cattle. In contrast, expression of the Th2 cytokine (IL-4) was lower in Holstein–Friesians cattle compared with Brahman cattle. Moreover, this study found that LRM6, LRM9 and LRM11 play important roles in the mechanism by which R. microplus interferes with the host’s haemostasis mechanisms.
Keyword Rhipicephalus (Boophilus) microplus
Lipocalin
B and T cell epitopes
Histamine binding protein
Tick Boophilus-microplus
Serine proteinase-inhibitor
Previously unexposed cattle
Salivary-gland extract
Bos-indicus cattle
Ixodes-ricinus
Host-resistance
Swiss-model
Soft tick
Anticomplement proteins
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Queensland Alliance for Agriculture and Food Innovation
Official 2014 Collection
School of Veterinary Science Publications
 
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