Genetic polymorphism of the Duffy receptor binding domain of Plasmodium vivax in Colombian wild isolates
The Plasmodium vivax Duffy receptor binding protein (DBP) is a member of the protein family localized in the Plasmodium parasite micronemes that binds to erythrocytes carrying this receptor. Given its importance in the parasite life cycle, it is being considered as a potential candidate in vaccine d...
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| Veröffentlicht in: | Molecular and biochemical parasitology 1996-06, Vol.78 (1-2), p.269-272 |
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| creator | Ampudia, Elizabeth Patarroyo, Manuel Alfonso Patarroyo, Manuel Elkin Murillo, Luis Angel |
| description | The Plasmodium vivax Duffy receptor binding protein (DBP) is a member of the protein family localized in the Plasmodium parasite micronemes that binds to erythrocytes carrying this receptor. Given its importance in the parasite life cycle, it is being considered as a potential candidate in vaccine development against P. vivax infection. Its molecular weight is 140 kDa and the primary structure has been previously reported for the Sal-I strain. This protein is divided into five important regions: a leader peptide sequence, two cysteine rich regions separated by a non-homologous hydrophilic region, and a transmembrane domain. The amino terminal cysteine-rich region has been implicated in the binding process to red blood cells (RBCs) carrying the Duffy receptor in a way analagous to what has been demonstrated with the EBA-175 protein of P. falciparum. A previous report showed natural variation within this critical ligand domain in the P. vivax Sal-I strain. Polymorphism studies within this region are highly significant for the rational design vaccines against asexual blood stages of P. vivax. |
| doi_str_mv | 10.1016/S0166-6851(96)02611-4 |
| format | Article |
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Given its importance in the parasite life cycle, it is being considered as a potential candidate in vaccine development against P. vivax infection. Its molecular weight is 140 kDa and the primary structure has been previously reported for the Sal-I strain. This protein is divided into five important regions: a leader peptide sequence, two cysteine rich regions separated by a non-homologous hydrophilic region, and a transmembrane domain. The amino terminal cysteine-rich region has been implicated in the binding process to red blood cells (RBCs) carrying the Duffy receptor in a way analagous to what has been demonstrated with the EBA-175 protein of P. falciparum. A previous report showed natural variation within this critical ligand domain in the P. vivax Sal-I strain. Polymorphism studies within this region are highly significant for the rational design vaccines against asexual blood stages of P. vivax.</description><identifier>ISSN: 0166-6851</identifier><identifier>EISSN: 1872-9428</identifier><identifier>DOI: 10.1016/S0166-6851(96)02611-4</identifier><identifier>PMID: 8813697</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Antigens, Protozoan ; Base Sequence ; Binding Sites ; Carrier Proteins - genetics ; Colombia ; DBP ; DNA, Protozoan - genetics ; Duffy Blood-Group System ; Duffy receptor ; Erythrocytes - parasitology ; Genetic Variation ; Malaria ; Malaria Vaccines - isolation & purification ; Malaria, Vivax - parasitology ; Molecular Sequence Data ; P. vivax ; PCR ; Plasmodium vivax ; Plasmodium vivax - genetics ; Plasmodium vivax - isolation & purification ; Plasmodium vivax - physiology ; Polymorphism ; Polymorphism, Genetic ; Protozoan Proteins ; Receptors, Cell Surface - genetics</subject><ispartof>Molecular and biochemical parasitology, 1996-06, Vol.78 (1-2), p.269-272</ispartof><rights>1996</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-b9204f010237caca101df7f5e771c035240b9a8643f952dec886190ff287a9a63</citedby><cites>FETCH-LOGICAL-c443t-b9204f010237caca101df7f5e771c035240b9a8643f952dec886190ff287a9a63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0166-6851(96)02611-4$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8813697$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ampudia, Elizabeth</creatorcontrib><creatorcontrib>Patarroyo, Manuel Alfonso</creatorcontrib><creatorcontrib>Patarroyo, Manuel Elkin</creatorcontrib><creatorcontrib>Murillo, Luis Angel</creatorcontrib><title>Genetic polymorphism of the Duffy receptor binding domain of Plasmodium vivax in Colombian wild isolates</title><title>Molecular and biochemical parasitology</title><addtitle>Mol Biochem Parasitol</addtitle><description>The Plasmodium vivax Duffy receptor binding protein (DBP) is a member of the protein family localized in the Plasmodium parasite micronemes that binds to erythrocytes carrying this receptor. Given its importance in the parasite life cycle, it is being considered as a potential candidate in vaccine development against P. vivax infection. Its molecular weight is 140 kDa and the primary structure has been previously reported for the Sal-I strain. This protein is divided into five important regions: a leader peptide sequence, two cysteine rich regions separated by a non-homologous hydrophilic region, and a transmembrane domain. The amino terminal cysteine-rich region has been implicated in the binding process to red blood cells (RBCs) carrying the Duffy receptor in a way analagous to what has been demonstrated with the EBA-175 protein of P. falciparum. A previous report showed natural variation within this critical ligand domain in the P. vivax Sal-I strain. Polymorphism studies within this region are highly significant for the rational design vaccines against asexual blood stages of P. vivax.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigens, Protozoan</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Carrier Proteins - genetics</subject><subject>Colombia</subject><subject>DBP</subject><subject>DNA, Protozoan - genetics</subject><subject>Duffy Blood-Group System</subject><subject>Duffy receptor</subject><subject>Erythrocytes - parasitology</subject><subject>Genetic Variation</subject><subject>Malaria</subject><subject>Malaria Vaccines - isolation & purification</subject><subject>Malaria, Vivax - parasitology</subject><subject>Molecular Sequence Data</subject><subject>P. vivax</subject><subject>PCR</subject><subject>Plasmodium vivax</subject><subject>Plasmodium vivax - genetics</subject><subject>Plasmodium vivax - isolation & purification</subject><subject>Plasmodium vivax - physiology</subject><subject>Polymorphism</subject><subject>Polymorphism, Genetic</subject><subject>Protozoan Proteins</subject><subject>Receptors, Cell Surface - genetics</subject><issn>0166-6851</issn><issn>1872-9428</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2LFDEQhoMo6-zqT1jISfTQmq_Ox0lkdFdhQUE9h3Q-nEin0ybdo_PvzewMe91LFVQ9VUW9LwDXGL3FCPN331vgHZc9fq34G0Q4xh17AjZYCtIpRuRTsHlAnoPLWn8jhHrB-QW4kBJTrsQG7G795Jdo4ZzHQ8pl3sWaYA5w2Xn4cQ3hAIu3fl5ygUOcXJx-QZeTidMR-jaamrKLa4L7uDf_YCtv85jTEM0E_8bRwVjzaBZfX4BnwYzVvzznK_Dz5tOP7efu7uvtl-2Hu84yRpduUASxgDAiVFhjTXvVBRF6LwS2iPaEoUEZyRkNqifOWyk5VigEIoVRhtMr8Oq0dy75z-rrolOs1o-jmXxeqxaSEkW5fBTEvWC0wQ3sT6Atudbig55LTKYcNEb6aIW-t0IfddaK63srNGtz1-cD65C8e5g6a9_670993-TYR190tdFP1rvYJF-0y_GRC_8BAjGZKQ</recordid><startdate>19960601</startdate><enddate>19960601</enddate><creator>Ampudia, Elizabeth</creator><creator>Patarroyo, Manuel Alfonso</creator><creator>Patarroyo, Manuel Elkin</creator><creator>Murillo, Luis Angel</creator><general>Elsevier B.V</general><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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19960601</creationdate><title>Genetic polymorphism of the Duffy receptor binding domain of Plasmodium vivax in Colombian wild isolates</title><author>Ampudia, Elizabeth ; Patarroyo, Manuel Alfonso ; Patarroyo, Manuel Elkin ; Murillo, Luis Angel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-b9204f010237caca101df7f5e771c035240b9a8643f952dec886190ff287a9a63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigens, Protozoan</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Carrier Proteins - genetics</topic><topic>Colombia</topic><topic>DBP</topic><topic>DNA, Protozoan - genetics</topic><topic>Duffy Blood-Group System</topic><topic>Duffy receptor</topic><topic>Erythrocytes - parasitology</topic><topic>Genetic Variation</topic><topic>Malaria</topic><topic>Malaria Vaccines - isolation & purification</topic><topic>Malaria, Vivax - parasitology</topic><topic>Molecular Sequence Data</topic><topic>P. vivax</topic><topic>PCR</topic><topic>Plasmodium vivax</topic><topic>Plasmodium vivax - genetics</topic><topic>Plasmodium vivax - isolation & purification</topic><topic>Plasmodium vivax - physiology</topic><topic>Polymorphism</topic><topic>Polymorphism, Genetic</topic><topic>Protozoan Proteins</topic><topic>Receptors, Cell Surface - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ampudia, Elizabeth</creatorcontrib><creatorcontrib>Patarroyo, Manuel Alfonso</creatorcontrib><creatorcontrib>Patarroyo, Manuel Elkin</creatorcontrib><creatorcontrib>Murillo, Luis Angel</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and biochemical parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ampudia, Elizabeth</au><au>Patarroyo, Manuel Alfonso</au><au>Patarroyo, Manuel Elkin</au><au>Murillo, Luis Angel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Genetic polymorphism of the Duffy receptor binding domain of Plasmodium vivax in Colombian wild isolates</atitle><jtitle>Molecular and biochemical parasitology</jtitle><addtitle>Mol Biochem Parasitol</addtitle><date>1996-06-01</date><risdate>1996</risdate><volume>78</volume><issue>1-2</issue><spage>269</spage><epage>272</epage><pages>269-272</pages><issn>0166-6851</issn><eissn>1872-9428</eissn><abstract>The Plasmodium vivax Duffy receptor binding protein (DBP) is a member of the protein family localized in the Plasmodium parasite micronemes that binds to erythrocytes carrying this receptor. Given its importance in the parasite life cycle, it is being considered as a potential candidate in vaccine development against P. vivax infection. Its molecular weight is 140 kDa and the primary structure has been previously reported for the Sal-I strain. This protein is divided into five important regions: a leader peptide sequence, two cysteine rich regions separated by a non-homologous hydrophilic region, and a transmembrane domain. The amino terminal cysteine-rich region has been implicated in the binding process to red blood cells (RBCs) carrying the Duffy receptor in a way analagous to what has been demonstrated with the EBA-175 protein of P. falciparum. A previous report showed natural variation within this critical ligand domain in the P. vivax Sal-I strain. Polymorphism studies within this region are highly significant for the rational design vaccines against asexual blood stages of P. vivax.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>8813697</pmid><doi>10.1016/S0166-6851(96)02611-4</doi><tpages>4</tpages></addata></record> |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Amino Acid Sequence Animals Antigens, Protozoan Base Sequence Binding Sites Carrier Proteins - genetics Colombia DBP DNA, Protozoan - genetics Duffy Blood-Group System Duffy receptor Erythrocytes - parasitology Genetic Variation Malaria Malaria Vaccines - isolation & purification Malaria, Vivax - parasitology Molecular Sequence Data P. vivax PCR Plasmodium vivax Plasmodium vivax - genetics Plasmodium vivax - isolation & purification Plasmodium vivax - physiology Polymorphism Polymorphism, Genetic Protozoan Proteins Receptors, Cell Surface - genetics |
| title | Genetic polymorphism of the Duffy receptor binding domain of Plasmodium vivax in Colombian wild isolates |
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