Structural and immunological analysis of circumsporozoite protein peptides: A further step in the identification of potential components of a minimal subunit-based, chemically synthesised antimalarial vaccine
Abstract The Plasmodium falciparum circumsporozoite protein is considered a major antimalarial-vaccine target due to its involvement in sporozoite invasion of mosquito’s salivary glands and human hepatocytes. The 4383, 4388 and 4389 CSP-conserved high activity hepatocyte binding peptides and their m...
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| Veröffentlicht in: | Vaccine 2008-12, Vol.26 (52), p.6908-6918 |
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| creator | Bermúdez, Adriana Vanegas, Magnolia Patarroyo, Manuel Elkin |
| description | Abstract The Plasmodium falciparum circumsporozoite protein is considered a major antimalarial-vaccine target due to its involvement in sporozoite invasion of mosquito’s salivary glands and human hepatocytes. The 4383, 4388 and 4389 CSP-conserved high activity hepatocyte binding peptides and their modified analogues were synthesised and their immunogenicity was tested in Aotus monkeys. Peptide 4388 modified analogues induced higher and more permanent antibody titers against sporozoites in ∼40% of immunised monkeys; whilst peptides 4383 and 4389 modified analogues elicited high, long-lasting antibody titers as well as short-lived antibodies.1 H NMR studies showed that native peptides displayed random conformations, whereas most modified immunogenic HABPs contained type I, II and IV β-turn structures. HLA-DRβ1* molecule binding assays revealed that 4383 modified HABPs bound to HLA-DRβ1*0701/HLA-DRβ1*0401 molecules, whilst 4388 and 4389 modified HABPs bound to HLA-DRβ1*0401/HLA-DRβ1*0101, respectively. The results support these high-immunogenic CSP-derived modified peptides’ inclusion in a multi-antigenic, multistage, minimal subunit-based synthetic antimalarial vaccine. |
| doi_str_mv | 10.1016/j.vaccine.2008.09.071 |
| format | Article |
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The 4383, 4388 and 4389 CSP-conserved high activity hepatocyte binding peptides and their modified analogues were synthesised and their immunogenicity was tested in Aotus monkeys. Peptide 4388 modified analogues induced higher and more permanent antibody titers against sporozoites in ∼40% of immunised monkeys; whilst peptides 4383 and 4389 modified analogues elicited high, long-lasting antibody titers as well as short-lived antibodies.1 H NMR studies showed that native peptides displayed random conformations, whereas most modified immunogenic HABPs contained type I, II and IV β-turn structures. HLA-DRβ1* molecule binding assays revealed that 4383 modified HABPs bound to HLA-DRβ1*0701/HLA-DRβ1*0401 molecules, whilst 4388 and 4389 modified HABPs bound to HLA-DRβ1*0401/HLA-DRβ1*0101, respectively. The results support these high-immunogenic CSP-derived modified peptides’ inclusion in a multi-antigenic, multistage, minimal subunit-based synthetic antimalarial vaccine.</description><identifier>ISSN: 0264-410X</identifier><identifier>EISSN: 1873-2518</identifier><identifier>DOI: 10.1016/j.vaccine.2008.09.071</identifier><identifier>PMID: 18930095</identifier><identifier>CODEN: VACCDE</identifier><language>eng</language><publisher>Kidlington: Elsevier Ltd</publisher><subject>Allergy and Immunology ; Amino Acid Sequence ; Amino acids ; Animals ; Antigens, Protozoan - immunology ; Aotus ; Aotus trivirgatus - immunology ; Applied microbiology ; Biological and medical sciences ; Blotting, Western ; Cell adhesion & migration ; Circular Dichroism ; CSP ; Enzyme-Linked Immunosorbent Assay ; Fluorescent Antibody Technique, Indirect ; Fundamental and applied biological sciences. Psychology ; HLA-DR Antigens - chemistry ; HLA-DR Antigens - isolation & purification ; HLA-DR Antigens - metabolism ; HLA-DRB1 Chains ; Immunization ; Immunogenicity ; Immunology ; Magnetic Resonance Spectroscopy ; Malaria ; Malaria Vaccines - chemical synthesis ; Malaria Vaccines - immunology ; Malaria, Falciparum - immunology ; Malaria, Falciparum - prevention & control ; Merozoites - immunology ; MHC-II ; Microbiology ; Models, Molecular ; Molecular Conformation ; NMR ; Parasites ; Peptides ; Plasmodium falciparum ; Proteins ; Protozoan Proteins - immunology ; Structure ; Vaccines ; Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies (general aspects) ; Vaccines, Subunit - chemical synthesis ; Vaccines, Subunit - immunology</subject><ispartof>Vaccine, 2008-12, Vol.26 (52), p.6908-6918</ispartof><rights>Elsevier Ltd</rights><rights>2008 Elsevier Ltd</rights><rights>2009 INIST-CNRS</rights><rights>Copyright Elsevier Limited Dec 9, 2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c507t-fa7c9b25c3455b9ced717778de9b2e62fa6eab2e769233a1786ec3c36ae1ddb3</citedby><cites>FETCH-LOGICAL-c507t-fa7c9b25c3455b9ced717778de9b2e62fa6eab2e769233a1786ec3c36ae1ddb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0264410X08013418$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20942870$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18930095$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bermúdez, Adriana</creatorcontrib><creatorcontrib>Vanegas, Magnolia</creatorcontrib><creatorcontrib>Patarroyo, Manuel Elkin</creatorcontrib><title>Structural and immunological analysis of circumsporozoite protein peptides: A further step in the identification of potential components of a minimal subunit-based, chemically synthesised antimalarial vaccine</title><title>Vaccine</title><addtitle>Vaccine</addtitle><description>Abstract The Plasmodium falciparum circumsporozoite protein is considered a major antimalarial-vaccine target due to its involvement in sporozoite invasion of mosquito’s salivary glands and human hepatocytes. The 4383, 4388 and 4389 CSP-conserved high activity hepatocyte binding peptides and their modified analogues were synthesised and their immunogenicity was tested in Aotus monkeys. Peptide 4388 modified analogues induced higher and more permanent antibody titers against sporozoites in ∼40% of immunised monkeys; whilst peptides 4383 and 4389 modified analogues elicited high, long-lasting antibody titers as well as short-lived antibodies.1 H NMR studies showed that native peptides displayed random conformations, whereas most modified immunogenic HABPs contained type I, II and IV β-turn structures. HLA-DRβ1* molecule binding assays revealed that 4383 modified HABPs bound to HLA-DRβ1*0701/HLA-DRβ1*0401 molecules, whilst 4388 and 4389 modified HABPs bound to HLA-DRβ1*0401/HLA-DRβ1*0101, respectively. The results support these high-immunogenic CSP-derived modified peptides’ inclusion in a multi-antigenic, multistage, minimal subunit-based synthetic antimalarial vaccine.</description><subject>Allergy and Immunology</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antigens, Protozoan - immunology</subject><subject>Aotus</subject><subject>Aotus trivirgatus - immunology</subject><subject>Applied microbiology</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Cell adhesion & migration</subject><subject>Circular Dichroism</subject><subject>CSP</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Fluorescent Antibody Technique, Indirect</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HLA-DR Antigens - chemistry</subject><subject>HLA-DR Antigens - isolation & purification</subject><subject>HLA-DR Antigens - metabolism</subject><subject>HLA-DRB1 Chains</subject><subject>Immunization</subject><subject>Immunogenicity</subject><subject>Immunology</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Malaria</subject><subject>Malaria Vaccines - chemical synthesis</subject><subject>Malaria Vaccines - immunology</subject><subject>Malaria, Falciparum - immunology</subject><subject>Malaria, Falciparum - prevention & control</subject><subject>Merozoites - immunology</subject><subject>MHC-II</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>Molecular Conformation</subject><subject>NMR</subject><subject>Parasites</subject><subject>Peptides</subject><subject>Plasmodium falciparum</subject><subject>Proteins</subject><subject>Protozoan Proteins - immunology</subject><subject>Structure</subject><subject>Vaccines</subject><subject>Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies (general aspects)</subject><subject>Vaccines, Subunit - chemical synthesis</subject><subject>Vaccines, Subunit - immunology</subject><issn>0264-410X</issn><issn>1873-2518</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFks1u1TAQhSMEoqXwCCBLCFbkMo7zZxagquJPqsSiXbCzfJ0J9SWxU9updHlKHolJb0SlbrpKPP58Znx8suwlhw0HXr_fbW60MdbhpgBoNyA30PBH2TFvG5EXFW8fZ8dQ1GVecvh5lD2LcQcAleDyaXbEWykAZHWc_b1IYTZpDnpg2nXMjuPs_OB_WXNb0cM-2sh8z4wNZh7j5IP_421CNgWf0Do24ZRsh_EDO2X9HNIVBhYTToz2aMFozyXbk2Cy3i1SEx2kEjUwfpy8o8VtC81G6-xI9ThvZ2dTvtURu3fMXOG4DDTsWdw7EqWZsKPx0kLrsEitdjzPnvR6iPhi_Z5kl18-X559y89_fP1-dnqemwqalPe6MXJbVEaUVbWVBruGN03TdkhVrIte16jpr6llIYTmTVujEUbUGnnXbcVJ9vYgSy5czxiTGm00OAzaoZ-jqmVbQVXCgyCXogFeSAJf3wN3fg70AMTURdWWUIuaqOpAmeBjDNirKZAHYa84qCUYaqdWJ9QSDAVSUTDo3KtVfd6O2N2dWpNAwJsV0JGc7oN2xsb_XAGyLNpmuc-nA4dk7o3FoKKx6MhAG9Ak1Xn74Cgf7ymYgZ6dmv7GPca7W6tYKFAXS4qXEEMLXJS8Ff8AezD1Gg</recordid><startdate>20081209</startdate><enddate>20081209</enddate><creator>Bermúdez, Adriana</creator><creator>Vanegas, Magnolia</creator><creator>Patarroyo, Manuel Elkin</creator><general>Elsevier Ltd</general><general>Elsevier</general><general>Elsevier Limited</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7RV</scope><scope>7T2</scope><scope>7T5</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88C</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9-</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0R</scope><scope>M0S</scope><scope>M0T</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20081209</creationdate><title>Structural and immunological analysis of circumsporozoite protein peptides: A further step in the identification of potential components of a minimal subunit-based, chemically synthesised antimalarial vaccine</title><author>Bermúdez, Adriana ; Vanegas, Magnolia ; Patarroyo, Manuel Elkin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c507t-fa7c9b25c3455b9ced717778de9b2e62fa6eab2e769233a1786ec3c36ae1ddb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Allergy and Immunology</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Antigens, Protozoan - immunology</topic><topic>Aotus</topic><topic>Aotus trivirgatus - immunology</topic><topic>Applied microbiology</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Cell adhesion & migration</topic><topic>Circular Dichroism</topic><topic>CSP</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Fluorescent Antibody Technique, Indirect</topic><topic>Fundamental and applied biological sciences. 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chemical synthesis</topic><topic>Vaccines, Subunit - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bermúdez, Adriana</creatorcontrib><creatorcontrib>Vanegas, Magnolia</creatorcontrib><creatorcontrib>Patarroyo, Manuel Elkin</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nursing & Allied Health Database</collection><collection>Health and Safety Science Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Healthcare Administration Database (Alumni)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>Consumer Health Database (Alumni Edition)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Consumer Health Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Healthcare Administration Database</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Vaccine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bermúdez, Adriana</au><au>Vanegas, Magnolia</au><au>Patarroyo, Manuel Elkin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural and immunological analysis of circumsporozoite protein peptides: A further step in the identification of potential components of a minimal subunit-based, chemically synthesised antimalarial vaccine</atitle><jtitle>Vaccine</jtitle><addtitle>Vaccine</addtitle><date>2008-12-09</date><risdate>2008</risdate><volume>26</volume><issue>52</issue><spage>6908</spage><epage>6918</epage><pages>6908-6918</pages><issn>0264-410X</issn><eissn>1873-2518</eissn><coden>VACCDE</coden><abstract>Abstract The Plasmodium falciparum circumsporozoite protein is considered a major antimalarial-vaccine target due to its involvement in sporozoite invasion of mosquito’s salivary glands and human hepatocytes. The 4383, 4388 and 4389 CSP-conserved high activity hepatocyte binding peptides and their modified analogues were synthesised and their immunogenicity was tested in Aotus monkeys. Peptide 4388 modified analogues induced higher and more permanent antibody titers against sporozoites in ∼40% of immunised monkeys; whilst peptides 4383 and 4389 modified analogues elicited high, long-lasting antibody titers as well as short-lived antibodies.1 H NMR studies showed that native peptides displayed random conformations, whereas most modified immunogenic HABPs contained type I, II and IV β-turn structures. HLA-DRβ1* molecule binding assays revealed that 4383 modified HABPs bound to HLA-DRβ1*0701/HLA-DRβ1*0401 molecules, whilst 4388 and 4389 modified HABPs bound to HLA-DRβ1*0401/HLA-DRβ1*0101, respectively. The results support these high-immunogenic CSP-derived modified peptides’ inclusion in a multi-antigenic, multistage, minimal subunit-based synthetic antimalarial vaccine.</abstract><cop>Kidlington</cop><pub>Elsevier Ltd</pub><pmid>18930095</pmid><doi>10.1016/j.vaccine.2008.09.071</doi><tpages>11</tpages></addata></record> |
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| ispartof | Vaccine, 2008-12, Vol.26 (52), p.6908-6918 |
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| subjects | Allergy and Immunology Amino Acid Sequence Amino acids Animals Antigens, Protozoan - immunology Aotus Aotus trivirgatus - immunology Applied microbiology Biological and medical sciences Blotting, Western Cell adhesion & migration Circular Dichroism CSP Enzyme-Linked Immunosorbent Assay Fluorescent Antibody Technique, Indirect Fundamental and applied biological sciences. Psychology HLA-DR Antigens - chemistry HLA-DR Antigens - isolation & purification HLA-DR Antigens - metabolism HLA-DRB1 Chains Immunization Immunogenicity Immunology Magnetic Resonance Spectroscopy Malaria Malaria Vaccines - chemical synthesis Malaria Vaccines - immunology Malaria, Falciparum - immunology Malaria, Falciparum - prevention & control Merozoites - immunology MHC-II Microbiology Models, Molecular Molecular Conformation NMR Parasites Peptides Plasmodium falciparum Proteins Protozoan Proteins - immunology Structure Vaccines Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies (general aspects) Vaccines, Subunit - chemical synthesis Vaccines, Subunit - immunology |
| title | Structural and immunological analysis of circumsporozoite protein peptides: A further step in the identification of potential components of a minimal subunit-based, chemically synthesised antimalarial vaccine |
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