Evaluation of vaccine delivery systems for inducing long-lived antibody responses to Dermanyssus gallinae antigen in laying hens
Dermanyssus gallinae, the poultry red mite, is a global threat to the commercial egg-laying industry. Control of D. gallinae is difficult, with only a limited number of effective pesticides and non-chemical treatments available. Here, we characterize the candidate vaccine antigen D. gallinae catheps...
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| creator | Price, Daniel R. G. Küster, Tatiana Øines, Øivind E. Margaret Oliver Bartley, Kathryn Nunn, Francesca Barbero, José Francisco Lima Pritchard, James Karp-Tatham, Eleanor Hauge, Helena Damer P. Blake Tomley, Fiona M. Nisbet, Alasdair J. |
| description | Dermanyssus gallinae, the poultry red mite, is a global threat to the commercial egg-laying industry. Control of D. gallinae is difficult, with only a limited number of effective pesticides and non-chemical treatments available. Here, we characterize the candidate vaccine antigen D. gallinae cathepsin D-1 (Dg-CatD-1) and demonstrate that purified refolded recombinant Dg-Cat-D1 (rDg-CatD-1) is an active aspartyl proteinase which digests haemoglobin with a pH optimum of pH 4. Soluble protein extracts from D. gallinae also have haemoglobinase activity, with a pH optimum comparable to the recombinant protein, and both proteinase activities were inhibited by the aspartyl proteinase inhibitor Pepstatin A. Enzyme activity and the ubiquitous localization of Dg-CatD-1 protein in sections of adult female mites is consistent with Dg-CatD-1 being a lysosomal proteinase. Using Dg-CatD-1 as a model vaccine antigen, we compared vaccine delivery methods in laying hens via vaccination with: (i) purified rDg-CatD-1 with Montanide™ ISA 71 VG adjuvant; (ii) recombinant DNA vaccines for expression of rDg-CatD-1 and (iii) transgenic coccidial parasite Eimeria tenella expressing rDg-CatD-1. In two independent trials, only birds vaccinated with rDg-CatD-1 with Montanide™ ISA 71 VG produced a strong and long-lasting serum anti-rDg-Cat-D1 IgY response, which was significantly higher than that in control birds vaccinated with adjuvant only. Furthermore, we showed that egg-laying rates of D. gallinae mites fed on birds vaccinated with rDg-CatD-1 in Montanide™ ISA 71 VG was reduced significantly compared with mites fed on unvaccinated birds. RESEARCH HIGHLIGHTSDermanyssus gallinae cathepsin D-1 (Dg-CatD-1) digests haemoglobinVaccination of hens with rDg-CatD-1 in Montanide™ ISA 71 VG results in long-lasting IgY levelsSerum anti-rDg-CatD-1 antibodies reduce egg laying in D. gallinae after a single blood meal Dermanyssus gallinae cathepsin D-1 (Dg-CatD-1) digests haemoglobin Vaccination of hens with rDg-CatD-1 in Montanide™ ISA 71 VG results in long-lasting IgY levels Serum anti-rDg-CatD-1 antibodies reduce egg laying in D. gallinae after a single blood meal |
| doi_str_mv | 10.6084/m9.figshare.8427062 |
| format | Dataset |
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G. ; Küster, Tatiana ; Øines, Øivind ; E. Margaret Oliver ; Bartley, Kathryn ; Nunn, Francesca ; Barbero, José Francisco Lima ; Pritchard, James ; Karp-Tatham, Eleanor ; Hauge, Helena ; Damer P. Blake ; Tomley, Fiona M. ; Nisbet, Alasdair J.</creator><creatorcontrib>Price, Daniel R. G. ; Küster, Tatiana ; Øines, Øivind ; E. Margaret Oliver ; Bartley, Kathryn ; Nunn, Francesca ; Barbero, José Francisco Lima ; Pritchard, James ; Karp-Tatham, Eleanor ; Hauge, Helena ; Damer P. Blake ; Tomley, Fiona M. ; Nisbet, Alasdair J.</creatorcontrib><description>Dermanyssus gallinae, the poultry red mite, is a global threat to the commercial egg-laying industry. Control of D. gallinae is difficult, with only a limited number of effective pesticides and non-chemical treatments available. Here, we characterize the candidate vaccine antigen D. gallinae cathepsin D-1 (Dg-CatD-1) and demonstrate that purified refolded recombinant Dg-Cat-D1 (rDg-CatD-1) is an active aspartyl proteinase which digests haemoglobin with a pH optimum of pH 4. Soluble protein extracts from D. gallinae also have haemoglobinase activity, with a pH optimum comparable to the recombinant protein, and both proteinase activities were inhibited by the aspartyl proteinase inhibitor Pepstatin A. Enzyme activity and the ubiquitous localization of Dg-CatD-1 protein in sections of adult female mites is consistent with Dg-CatD-1 being a lysosomal proteinase. Using Dg-CatD-1 as a model vaccine antigen, we compared vaccine delivery methods in laying hens via vaccination with: (i) purified rDg-CatD-1 with Montanide™ ISA 71 VG adjuvant; (ii) recombinant DNA vaccines for expression of rDg-CatD-1 and (iii) transgenic coccidial parasite Eimeria tenella expressing rDg-CatD-1. In two independent trials, only birds vaccinated with rDg-CatD-1 with Montanide™ ISA 71 VG produced a strong and long-lasting serum anti-rDg-Cat-D1 IgY response, which was significantly higher than that in control birds vaccinated with adjuvant only. Furthermore, we showed that egg-laying rates of D. gallinae mites fed on birds vaccinated with rDg-CatD-1 in Montanide™ ISA 71 VG was reduced significantly compared with mites fed on unvaccinated birds. RESEARCH HIGHLIGHTSDermanyssus gallinae cathepsin D-1 (Dg-CatD-1) digests haemoglobinVaccination of hens with rDg-CatD-1 in Montanide™ ISA 71 VG results in long-lasting IgY levelsSerum anti-rDg-CatD-1 antibodies reduce egg laying in D. gallinae after a single blood meal Dermanyssus gallinae cathepsin D-1 (Dg-CatD-1) digests haemoglobin Vaccination of hens with rDg-CatD-1 in Montanide™ ISA 71 VG results in long-lasting IgY levels Serum anti-rDg-CatD-1 antibodies reduce egg laying in D. gallinae after a single blood meal</description><identifier>DOI: 10.6084/m9.figshare.8427062</identifier><language>eng</language><publisher>Taylor & Francis</publisher><subject>Biochemistry ; Biotechnology ; Cancer ; FOS: Biological sciences ; FOS: Clinical medicine ; FOS: Health sciences ; FOS: Physical sciences ; Immunology ; Infectious Diseases ; Microbiology ; Physical Sciences not elsewhere classified</subject><creationdate>2019</creationdate><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>776,1888</link.rule.ids><linktorsrc>$$Uhttps://commons.datacite.org/doi.org/10.6084/m9.figshare.8427062$$EView_record_in_DataCite.org$$FView_record_in_$$GDataCite.org$$Hfree_for_read</linktorsrc></links><search><creatorcontrib>Price, Daniel R. G.</creatorcontrib><creatorcontrib>Küster, Tatiana</creatorcontrib><creatorcontrib>Øines, Øivind</creatorcontrib><creatorcontrib>E. Margaret Oliver</creatorcontrib><creatorcontrib>Bartley, Kathryn</creatorcontrib><creatorcontrib>Nunn, Francesca</creatorcontrib><creatorcontrib>Barbero, José Francisco Lima</creatorcontrib><creatorcontrib>Pritchard, James</creatorcontrib><creatorcontrib>Karp-Tatham, Eleanor</creatorcontrib><creatorcontrib>Hauge, Helena</creatorcontrib><creatorcontrib>Damer P. Blake</creatorcontrib><creatorcontrib>Tomley, Fiona M.</creatorcontrib><creatorcontrib>Nisbet, Alasdair J.</creatorcontrib><title>Evaluation of vaccine delivery systems for inducing long-lived antibody responses to Dermanyssus gallinae antigen in laying hens</title><description>Dermanyssus gallinae, the poultry red mite, is a global threat to the commercial egg-laying industry. Control of D. gallinae is difficult, with only a limited number of effective pesticides and non-chemical treatments available. Here, we characterize the candidate vaccine antigen D. gallinae cathepsin D-1 (Dg-CatD-1) and demonstrate that purified refolded recombinant Dg-Cat-D1 (rDg-CatD-1) is an active aspartyl proteinase which digests haemoglobin with a pH optimum of pH 4. Soluble protein extracts from D. gallinae also have haemoglobinase activity, with a pH optimum comparable to the recombinant protein, and both proteinase activities were inhibited by the aspartyl proteinase inhibitor Pepstatin A. Enzyme activity and the ubiquitous localization of Dg-CatD-1 protein in sections of adult female mites is consistent with Dg-CatD-1 being a lysosomal proteinase. Using Dg-CatD-1 as a model vaccine antigen, we compared vaccine delivery methods in laying hens via vaccination with: (i) purified rDg-CatD-1 with Montanide™ ISA 71 VG adjuvant; (ii) recombinant DNA vaccines for expression of rDg-CatD-1 and (iii) transgenic coccidial parasite Eimeria tenella expressing rDg-CatD-1. In two independent trials, only birds vaccinated with rDg-CatD-1 with Montanide™ ISA 71 VG produced a strong and long-lasting serum anti-rDg-Cat-D1 IgY response, which was significantly higher than that in control birds vaccinated with adjuvant only. Furthermore, we showed that egg-laying rates of D. gallinae mites fed on birds vaccinated with rDg-CatD-1 in Montanide™ ISA 71 VG was reduced significantly compared with mites fed on unvaccinated birds. RESEARCH HIGHLIGHTSDermanyssus gallinae cathepsin D-1 (Dg-CatD-1) digests haemoglobinVaccination of hens with rDg-CatD-1 in Montanide™ ISA 71 VG results in long-lasting IgY levelsSerum anti-rDg-CatD-1 antibodies reduce egg laying in D. gallinae after a single blood meal Dermanyssus gallinae cathepsin D-1 (Dg-CatD-1) digests haemoglobin Vaccination of hens with rDg-CatD-1 in Montanide™ ISA 71 VG results in long-lasting IgY levels Serum anti-rDg-CatD-1 antibodies reduce egg laying in D. gallinae after a single blood meal</description><subject>Biochemistry</subject><subject>Biotechnology</subject><subject>Cancer</subject><subject>FOS: Biological sciences</subject><subject>FOS: Clinical medicine</subject><subject>FOS: Health sciences</subject><subject>FOS: Physical sciences</subject><subject>Immunology</subject><subject>Infectious Diseases</subject><subject>Microbiology</subject><subject>Physical Sciences not elsewhere classified</subject><fulltext>true</fulltext><rsrctype>dataset</rsrctype><creationdate>2019</creationdate><recordtype>dataset</recordtype><sourceid>PQ8</sourceid><recordid>eNo1kL1ugzAURlk6VGmfoMt9AajBBPBYpemPFKlLdnThXhNLxo5siMTWR29o0-kbvqMznCR5ykVWiaZ8HlWmzRBPGDhryqIWVXGffO8vaGecjHfgNVyw741jILbmwmGBuMSJxwjaBzCO5us7gPVuSFeAAN1kOk8LBI5n7yJHmDy8chjRLTHOEQa01jjkX3Rgd9WAxWX1nNjFh-ROo438eNtNcnzbH3cf6eHr_XP3ckipUUWaF5pZFJrKBvOy6lSpcqplh1wKarom76TsFDJJlHpLJGrFNcpKVaQ1KpSbRP5pCSfszcTtOZgRw9Lmol3ztKNq__O0tzzyB8kvZes</recordid><startdate>20190702</startdate><enddate>20190702</enddate><creator>Price, Daniel R. G.</creator><creator>Küster, Tatiana</creator><creator>Øines, Øivind</creator><creator>E. Margaret Oliver</creator><creator>Bartley, Kathryn</creator><creator>Nunn, Francesca</creator><creator>Barbero, José Francisco Lima</creator><creator>Pritchard, James</creator><creator>Karp-Tatham, Eleanor</creator><creator>Hauge, Helena</creator><creator>Damer P. Blake</creator><creator>Tomley, Fiona M.</creator><creator>Nisbet, Alasdair J.</creator><general>Taylor & Francis</general><scope>DYCCY</scope><scope>PQ8</scope></search><sort><creationdate>20190702</creationdate><title>Evaluation of vaccine delivery systems for inducing long-lived antibody responses to Dermanyssus gallinae antigen in laying hens</title><author>Price, Daniel R. G. ; Küster, Tatiana ; Øines, Øivind ; E. Margaret Oliver ; Bartley, Kathryn ; Nunn, Francesca ; Barbero, José Francisco Lima ; Pritchard, James ; Karp-Tatham, Eleanor ; Hauge, Helena ; Damer P. Blake ; Tomley, Fiona M. ; Nisbet, Alasdair J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-d892-12fee02fd48a146b9491d73bae40d8b81b33b9aed3a3f5dd079e7a3696dffa9a3</frbrgroupid><rsrctype>datasets</rsrctype><prefilter>datasets</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Biochemistry</topic><topic>Biotechnology</topic><topic>Cancer</topic><topic>FOS: Biological sciences</topic><topic>FOS: Clinical medicine</topic><topic>FOS: Health sciences</topic><topic>FOS: Physical sciences</topic><topic>Immunology</topic><topic>Infectious Diseases</topic><topic>Microbiology</topic><topic>Physical Sciences not elsewhere classified</topic><toplevel>online_resources</toplevel><creatorcontrib>Price, Daniel R. G.</creatorcontrib><creatorcontrib>Küster, Tatiana</creatorcontrib><creatorcontrib>Øines, Øivind</creatorcontrib><creatorcontrib>E. Margaret Oliver</creatorcontrib><creatorcontrib>Bartley, Kathryn</creatorcontrib><creatorcontrib>Nunn, Francesca</creatorcontrib><creatorcontrib>Barbero, José Francisco Lima</creatorcontrib><creatorcontrib>Pritchard, James</creatorcontrib><creatorcontrib>Karp-Tatham, Eleanor</creatorcontrib><creatorcontrib>Hauge, Helena</creatorcontrib><creatorcontrib>Damer P. Blake</creatorcontrib><creatorcontrib>Tomley, Fiona M.</creatorcontrib><creatorcontrib>Nisbet, Alasdair J.</creatorcontrib><collection>DataCite (Open Access)</collection><collection>DataCite</collection></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Price, Daniel R. G.</au><au>Küster, Tatiana</au><au>Øines, Øivind</au><au>E. Margaret Oliver</au><au>Bartley, Kathryn</au><au>Nunn, Francesca</au><au>Barbero, José Francisco Lima</au><au>Pritchard, James</au><au>Karp-Tatham, Eleanor</au><au>Hauge, Helena</au><au>Damer P. Blake</au><au>Tomley, Fiona M.</au><au>Nisbet, Alasdair J.</au><format>book</format><genre>unknown</genre><ristype>DATA</ristype><title>Evaluation of vaccine delivery systems for inducing long-lived antibody responses to Dermanyssus gallinae antigen in laying hens</title><date>2019-07-02</date><risdate>2019</risdate><abstract>Dermanyssus gallinae, the poultry red mite, is a global threat to the commercial egg-laying industry. Control of D. gallinae is difficult, with only a limited number of effective pesticides and non-chemical treatments available. Here, we characterize the candidate vaccine antigen D. gallinae cathepsin D-1 (Dg-CatD-1) and demonstrate that purified refolded recombinant Dg-Cat-D1 (rDg-CatD-1) is an active aspartyl proteinase which digests haemoglobin with a pH optimum of pH 4. Soluble protein extracts from D. gallinae also have haemoglobinase activity, with a pH optimum comparable to the recombinant protein, and both proteinase activities were inhibited by the aspartyl proteinase inhibitor Pepstatin A. Enzyme activity and the ubiquitous localization of Dg-CatD-1 protein in sections of adult female mites is consistent with Dg-CatD-1 being a lysosomal proteinase. Using Dg-CatD-1 as a model vaccine antigen, we compared vaccine delivery methods in laying hens via vaccination with: (i) purified rDg-CatD-1 with Montanide™ ISA 71 VG adjuvant; (ii) recombinant DNA vaccines for expression of rDg-CatD-1 and (iii) transgenic coccidial parasite Eimeria tenella expressing rDg-CatD-1. In two independent trials, only birds vaccinated with rDg-CatD-1 with Montanide™ ISA 71 VG produced a strong and long-lasting serum anti-rDg-Cat-D1 IgY response, which was significantly higher than that in control birds vaccinated with adjuvant only. Furthermore, we showed that egg-laying rates of D. gallinae mites fed on birds vaccinated with rDg-CatD-1 in Montanide™ ISA 71 VG was reduced significantly compared with mites fed on unvaccinated birds. RESEARCH HIGHLIGHTSDermanyssus gallinae cathepsin D-1 (Dg-CatD-1) digests haemoglobinVaccination of hens with rDg-CatD-1 in Montanide™ ISA 71 VG results in long-lasting IgY levelsSerum anti-rDg-CatD-1 antibodies reduce egg laying in D. gallinae after a single blood meal Dermanyssus gallinae cathepsin D-1 (Dg-CatD-1) digests haemoglobin Vaccination of hens with rDg-CatD-1 in Montanide™ ISA 71 VG results in long-lasting IgY levels Serum anti-rDg-CatD-1 antibodies reduce egg laying in D. gallinae after a single blood meal</abstract><pub>Taylor & Francis</pub><doi>10.6084/m9.figshare.8427062</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Biochemistry Biotechnology Cancer FOS: Biological sciences FOS: Clinical medicine FOS: Health sciences FOS: Physical sciences Immunology Infectious Diseases Microbiology Physical Sciences not elsewhere classified |
| title | Evaluation of vaccine delivery systems for inducing long-lived antibody responses to Dermanyssus gallinae antigen in laying hens |
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