Cloning, Monoclonal Antibody Production, and Bodily Distribution Pattern of a Bovine Lipocalin

Japaridze, Tamar; Senda, Akitsugu; Nozaki, Hirofumi; Yanagida, Mitsuaki; Suzuki, Takumi; Ganzorig, Khuukhenbaatar; Kushi, Yasunori; Kida, Katsuya; Urashima, Tadasu; Bruckmaier, Rupert M.; Fukuda, Kenji

doi:10.1271/bbb.110840

Cited by 4 publications

(6 citation statements)

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“…The ABP genes have undergone repeated bursts of gene duplication and adaptive sequence diversification driven by their participation in chemosensation and/or sexual identification [ 54 ]. Skin glands are known to be sources of semiochemicals and of olfactory profiles for species-specific vector-host interactions [ 55 , 56 ]. Skin microbiota, by acting upon androgens [ 56 ], also participate in production of body odor.…”

Section: Discussionmentioning

confidence: 99%

“…Bovine odorant-binding protein (bOBP), an orthologue of ABPβ-like, is a lipocalin that binds 1-octen-3-ol, a VOC of bovine breath and body odor and a potent attractant for blood-feeding vectors like Anopheles mosquitos or Glossina flies [ 57 ]. Interestingly, bOBP was found in milk, urine and plasma of Holstein cattle (the susceptible breed in our model) but not in the sweat of this breed [ 55 ]. bOBPs are also known allergens present in bovine skin danders [ 58 ].…”

Section: Discussionmentioning

confidence: 99%

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Immune and biochemical responses in skin differ between bovine hosts genetically susceptible and resistant to the cattle tick Rhipicephalus microplus

et al. 2017

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BackgroundTicks attach to and penetrate their hosts’ skin and inactivate multiple components of host responses in order to acquire a blood meal. Infestation loads with the cattle tick, Rhipicephalus microplus, are heritable: some breeds carry high loads of reproductively successful ticks, whereas in others, few ticks feed and reproduce efficiently.MethodsIn order to elucidate the mechanisms that result in the different outcomes of infestations with cattle ticks, we examined global gene expression and inflammation induced by tick bites in skins from one resistant and one susceptible breed of cattle that underwent primary infestations with larvae and nymphs of R. microplus. We also examined the expression profiles of genes encoding secreted tick proteins that mediate parasitism in larvae and nymphs feeding on these breeds.ResultsFunctional analyses of differentially expressed genes in the skin suggest that allergic contact-like dermatitis develops with ensuing production of IL-6, CXCL-8 and CCL-2 and is sustained by HMGB1, ISG15 and PKR, leading to expression of pro-inflammatory chemokines and cytokines that recruit granulocytes and T lymphocytes. Importantly, this response is delayed in susceptible hosts. Histopathological analyses of infested skins showed inflammatory reactions surrounding tick cement cones that enable attachment in both breeds, but in genetically tick-resistant bovines they destabilized the cone. The transcription data provided insights into tick-mediated activation of basophils, which have previously been shown to be a key to host resistance in model systems. Skin from tick-susceptible bovines expressed more transcripts encoding enzymes that detoxify tissues. Interestingly, these enzymes also produce volatile odoriferous compounds and, accordingly, skin rubbings from tick-susceptible bovines attracted significantly more tick larvae than rubbings from resistant hosts. Moreover, transcripts encoding secreted modulatory molecules by the tick were significantly more abundant in larval and in nymphal salivary glands from ticks feeding on susceptible bovines.ConclusionsCompared with tick-susceptible hosts, genes encoding enzymes producing volatile compounds exhibit significantly lower expression in resistant hosts, which may render them less attractive to larvae; resistant hosts expose ticks to an earlier inflammatory response, which in ticks is associated with significantly lower expression of genes encoding salivary proteins that suppress host immunity, inflammation and coagulation.Electronic supplementary materialThe online version of this article (doi:10.1186/s13071-016-1945-z) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Immune and biochemical responses in skin differ between bovine hosts genetically susceptible and resistant to the cattle tick Rhipicephalus microplus

et al. 2017

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“…Therefore, it is possible that the natural presentation of Can f 4 in dog dander also includes oligomers, a property shared with some other lipocalins. 36 , 39 , 40 To some extent, this property can also be a factor underlying the sensitivity of Can f 4 to denaturation.…”

Section: Discussionmentioning

confidence: 99%

IgE Reactivity of the Dog Lipocalin Allergen Can f 4 and the Development of a Sandwich ELISA for Its Quantification

Rytkönen‐Nissinen

Saarelainen

Randell

et al. 2015

Allergy Asthma Immunol Res

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PurposeDivergent results on the IgE reactivity of dog-allergic subjects to Can f 4 have been reported. The aim of this study was to evaluate the significance of Can f 4 in dog allergy and to develop an immunochemical method for measuring Can f 4 content in environmental samples.MethodsWe purified the natural dog allergen Can f 4 from a dog dander extract by monoclonal antibody-based affinity chromatography and generated its variant in a recombinant form. Sixty-three dog-allergic patients and 12 nonallergic control subjects were recruited in the study. The IgE-binding capacity of natural Can f 4 and its recombinant variant was assessed by ELISA, immunoblotting, and skin prick tests (SPT).ResultsEighty-one percent of the dog-allergic patients showed a positive result to the immunoaffinity-purified natural Can f 4 in IgE ELISA, but only 46% in IgE immunoblotting. Respective results with the recombinant Can f 4 variant were 54% and 49%. SPT results reflected those obtained in ELISA and immunoblotting. The overall IgE reactivity of the immunoaffinity-purified natural Can f 4 was found to depend strongly on the integrity of the allergen's conformation. A sandwich ELISA based on monoclonal antibodies was found to be functional for measuring Can f 4 in environmental samples.ConclusionsCan f 4 is a major allergen of dog together with Can f 1 and Can f 5. In combination with other dog allergens, it improves the reliability of allergy tests in dog allergy.

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“…They produced a monoclonal antibody for bcOBP and showed bcOBP to be constantly secreted at 181 AE 39 mg/L into milk on day of parturition until at least 10 days postpartum (Japaridze et al, 2012). Besides milk, bcOBP was found in the nasal mucus, saliva, amniotic fluid, vaginal discharge and blood plasma (Japaridze et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

“…In 2009, a novel protein in bovine colostrum was found by Japanese research groups, which was named bovine colostral odorant‐binding protein (bcOBP) (Fukuda et al, ). They produced a monoclonal antibody for bcOBP and showed bcOBP to be constantly secreted at 181 ± 39 µg/L into milk on day of parturition until at least 10 days postpartum (Japaridze et al, ). Besides milk, bcOBP was found in the nasal mucus, saliva, amniotic fluid, vaginal discharge and blood plasma (Japaridze et al, ).…”

Section: Introductionmentioning

confidence: 99%

Localisation of bovine colostral odorant‐binding protein (bcOBP) mRNAs in several tissues of bovine body

Katayama

Japaridze

2013

Cell Biology International

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Bovine colostral odorant-binding protein (bcOBP) is a novel protein found in bovine colostrum and belonging to the lipocalin superfamily. Most of them are secretory proteins. We have examined the localisation of bcOBP messenger RNA in several tissues. The expression of bcOBP messenger RNAs was followed in bovine principal organs and female reproductive tracts with in situ hybridisation, but the localisation of it was not detected. The expression levels of bcOBP mRNAs were also extremely low in those tissues. On the other hand, the expression of bcOBP messenger RNAs has not been found in the airway epithelia and the gallbladder. These results suggest that bcOBP messenger RNAs are expressed in bovine several tissues without its localisation. In conclusion, the localisation of bcOBP messenger RNAs in bovine several tissues was not found.

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Cloning, Monoclonal Antibody Production, and Bodily Distribution Pattern of a Bovine Lipocalin

Cited by 4 publications

References 1 publication

Immune and biochemical responses in skin differ between bovine hosts genetically susceptible and resistant to the cattle tick Rhipicephalus microplus

Immune and biochemical responses in skin differ between bovine hosts genetically susceptible and resistant to the cattle tick Rhipicephalus microplus

IgE Reactivity of the Dog Lipocalin Allergen Can f 4 and the Development of a Sandwich ELISA for Its Quantification

Localisation of bovine colostral odorant‐binding protein (bcOBP) mRNAs in several tissues of bovine body

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