Immunogenicity of the Plasmodium falciparum PfEMP1-VarO Adhesin: Induction of Surface-Reactive and Rosette-Disrupting Antibodies to VarO Infected Erythrocytes
Adhesion of Plasmodium falciparum-infected red blood cells (iRBC) to human erythrocytes (i.e. rosetting) is associated with severe malaria. Rosetting results from interactions between a subset of variant PfEMP1 (Plasmodium falciparum erythrocyte membrane protein 1) adhesins and specific erythrocyte...
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| Veröffentlicht in: | PloS one 2015-07, Vol.10 (7), p.e0134292-e0134292 |
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| creator | Guillotte, Micheline Juillerat, Alexandre Igonet, Sébastien Hessel, Audrey Petres, Stéphane Crublet, Elodie Le Scanf, Cécile Lewit-Bentley, Anita Bentley, Graham A Vigan-Womas, Inès Mercereau-Puijalon, Odile |
| description | Adhesion of Plasmodium falciparum-infected red blood cells (iRBC) to human erythrocytes (i.e. rosetting) is associated with severe malaria. Rosetting results from interactions between a subset of variant PfEMP1 (Plasmodium falciparum erythrocyte membrane protein 1) adhesins and specific erythrocyte receptors. Interfering with such interactions is considered a promising intervention against severe malaria. To evaluate the feasibility of a vaccine strategy targetting rosetting, we have used here the Palo Alto 89F5 VarO rosetting model. PfEMP1-VarO consists of five Duffy-Binding Like domains (DBL1-5) and one Cysteine-rich Interdomain Region (CIDR1). The binding domain has been mapped to DBL1 and the ABO blood group was identified as the erythrocyte receptor. Here, we study the immunogenicity of all six recombinant PfEMP1-VarO domains and the DBL1- CIDR1 Head domain in BALB/c and outbred OF1 mice. Five readouts of antibody responses are explored: ELISA titres on the recombinant antigen, VarO-iRBC immunoblot reactivity, VarO-iRBC surface-reactivity, capacity to disrupt VarO rosettes and the capacity to prevent VarO rosette formation. For three domains, we explore influence of the expression system on antigenicity and immunogenicity. We show that correctly folded PfEMP1 domains elicit high antibody titres and induce a homogeneous response in outbred and BALB/c mice after three injections. High levels of rosette-disrupting and rosette-preventing antibodies are induced by DBL1 and the Head domain. Reduced-alkylated or denatured proteins fail to induce surface-reacting and rosette-disrupting antibodies, indicating that surface epitopes are conformational. We also report limited cross-reactivity between some PfEMP1 VarO domains. These results highlight the high immunogenicity of the individual domains in outbred animals and provide a strong basis for a rational vaccination strategy targeting rosetting. |
| doi_str_mv | 10.1371/journal.pone.0134292 |
| format | Article |
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Rosetting results from interactions between a subset of variant PfEMP1 (Plasmodium falciparum erythrocyte membrane protein 1) adhesins and specific erythrocyte receptors. Interfering with such interactions is considered a promising intervention against severe malaria. To evaluate the feasibility of a vaccine strategy targetting rosetting, we have used here the Palo Alto 89F5 VarO rosetting model. PfEMP1-VarO consists of five Duffy-Binding Like domains (DBL1-5) and one Cysteine-rich Interdomain Region (CIDR1). The binding domain has been mapped to DBL1 and the ABO blood group was identified as the erythrocyte receptor. Here, we study the immunogenicity of all six recombinant PfEMP1-VarO domains and the DBL1- CIDR1 Head domain in BALB/c and outbred OF1 mice. Five readouts of antibody responses are explored: ELISA titres on the recombinant antigen, VarO-iRBC immunoblot reactivity, VarO-iRBC surface-reactivity, capacity to disrupt VarO rosettes and the capacity to prevent VarO rosette formation. For three domains, we explore influence of the expression system on antigenicity and immunogenicity. We show that correctly folded PfEMP1 domains elicit high antibody titres and induce a homogeneous response in outbred and BALB/c mice after three injections. High levels of rosette-disrupting and rosette-preventing antibodies are induced by DBL1 and the Head domain. Reduced-alkylated or denatured proteins fail to induce surface-reacting and rosette-disrupting antibodies, indicating that surface epitopes are conformational. We also report limited cross-reactivity between some PfEMP1 VarO domains. These results highlight the high immunogenicity of the individual domains in outbred animals and provide a strong basis for a rational vaccination strategy targeting rosetting.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0134292</identifier><identifier>PMID: 26222304</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>ABO system ; Adaptive immunology ; Adhesins ; Adhesins, Bacterial - chemistry ; Adhesins, Bacterial - genetics ; Adhesins, Bacterial - immunology ; Alkylation ; Analysis ; Animals ; Antibodies ; Antibodies, Protozoan - blood ; Antigenicity ; Antigens ; Antigens, Protozoan - chemistry ; Antigens, Protozoan - genetics ; Binding ; Blood ; Blood cells ; Blood groups ; Cross Reactions ; Cross-reactivity ; Disruption ; E coli ; Enzyme-linked immunosorbent assay ; Epitopes ; Epitopes - chemistry ; Epitopes - genetics ; Erythrocyte membrane protein 1 ; Erythrocytes ; Erythrocytes - parasitology ; Escherichia coli ; Feasibility studies ; Female ; Human health and pathology ; Humans ; Immunogenicity ; Immunoglobulins ; Immunology ; Infectious diseases ; Laboratory animals ; Life Sciences ; Malaria ; Malaria Vaccines - chemistry ; Malaria Vaccines - genetics ; Malaria Vaccines - immunology ; Malaria, Falciparum - immunology ; Malaria, Falciparum - parasitology ; Malaria, Falciparum - prevention & control ; Membrane proteins ; Mice ; Mice, Inbred BALB C ; Microbial adhesion ; Microbiology and Parasitology ; Parasites ; Parasitology ; Physiological aspects ; Plasmodium falciparum ; Plasmodium falciparum - genetics ; Plasmodium falciparum - immunology ; Plasmodium falciparum - pathogenicity ; Protein Structure, Tertiary ; Proteins ; Protozoan Proteins - chemistry ; Protozoan Proteins - genetics ; Protozoan Proteins - immunology ; Reactivity ; Receptors ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Red blood cells ; Risk factors ; Rosette Formation ; Spectrum analysis ; Vaccination ; Vaccines ; Vector-borne diseases</subject><ispartof>PloS one, 2015-07, Vol.10 (7), p.e0134292-e0134292</ispartof><rights>COPYRIGHT 2015 Public Library of Science</rights><rights>2015 Guillotte et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Attribution</rights><rights>2015 Guillotte et al 2015 Guillotte et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c726t-dff3241139dbd760e4f6b09ba55650ebcc890be11bc3390b3b4d8ec375b032a03</citedby><cites>FETCH-LOGICAL-c726t-dff3241139dbd760e4f6b09ba55650ebcc890be11bc3390b3b4d8ec375b032a03</cites><orcidid>0000-0001-7848-9297 ; 0000-0002-4716-565X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4519321/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4519321/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,861,882,2096,2915,23847,27905,27906,53772,53774,79349,79350</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26222304$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02937184$$DView record in HAL$$Hfree_for_read</backlink></links><search><contributor>Tsuboi, Takafumi</contributor><creatorcontrib>Guillotte, Micheline</creatorcontrib><creatorcontrib>Juillerat, Alexandre</creatorcontrib><creatorcontrib>Igonet, Sébastien</creatorcontrib><creatorcontrib>Hessel, Audrey</creatorcontrib><creatorcontrib>Petres, Stéphane</creatorcontrib><creatorcontrib>Crublet, Elodie</creatorcontrib><creatorcontrib>Le Scanf, Cécile</creatorcontrib><creatorcontrib>Lewit-Bentley, Anita</creatorcontrib><creatorcontrib>Bentley, Graham A</creatorcontrib><creatorcontrib>Vigan-Womas, Inès</creatorcontrib><creatorcontrib>Mercereau-Puijalon, Odile</creatorcontrib><title>Immunogenicity of the Plasmodium falciparum PfEMP1-VarO Adhesin: Induction of Surface-Reactive and Rosette-Disrupting Antibodies to VarO Infected Erythrocytes</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Adhesion of Plasmodium falciparum-infected red blood cells (iRBC) to human erythrocytes (i.e. rosetting) is associated with severe malaria. Rosetting results from interactions between a subset of variant PfEMP1 (Plasmodium falciparum erythrocyte membrane protein 1) adhesins and specific erythrocyte receptors. Interfering with such interactions is considered a promising intervention against severe malaria. To evaluate the feasibility of a vaccine strategy targetting rosetting, we have used here the Palo Alto 89F5 VarO rosetting model. PfEMP1-VarO consists of five Duffy-Binding Like domains (DBL1-5) and one Cysteine-rich Interdomain Region (CIDR1). The binding domain has been mapped to DBL1 and the ABO blood group was identified as the erythrocyte receptor. Here, we study the immunogenicity of all six recombinant PfEMP1-VarO domains and the DBL1- CIDR1 Head domain in BALB/c and outbred OF1 mice. Five readouts of antibody responses are explored: ELISA titres on the recombinant antigen, VarO-iRBC immunoblot reactivity, VarO-iRBC surface-reactivity, capacity to disrupt VarO rosettes and the capacity to prevent VarO rosette formation. For three domains, we explore influence of the expression system on antigenicity and immunogenicity. We show that correctly folded PfEMP1 domains elicit high antibody titres and induce a homogeneous response in outbred and BALB/c mice after three injections. High levels of rosette-disrupting and rosette-preventing antibodies are induced by DBL1 and the Head domain. Reduced-alkylated or denatured proteins fail to induce surface-reacting and rosette-disrupting antibodies, indicating that surface epitopes are conformational. We also report limited cross-reactivity between some PfEMP1 VarO domains. These results highlight the high immunogenicity of the individual domains in outbred animals and provide a strong basis for a rational vaccination strategy targeting rosetting.</description><subject>ABO system</subject><subject>Adaptive immunology</subject><subject>Adhesins</subject><subject>Adhesins, Bacterial - chemistry</subject><subject>Adhesins, Bacterial - genetics</subject><subject>Adhesins, Bacterial - immunology</subject><subject>Alkylation</subject><subject>Analysis</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Protozoan - blood</subject><subject>Antigenicity</subject><subject>Antigens</subject><subject>Antigens, Protozoan - chemistry</subject><subject>Antigens, Protozoan - genetics</subject><subject>Binding</subject><subject>Blood</subject><subject>Blood cells</subject><subject>Blood groups</subject><subject>Cross Reactions</subject><subject>Cross-reactivity</subject><subject>Disruption</subject><subject>E 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control</subject><subject>Membrane proteins</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Microbial adhesion</subject><subject>Microbiology and Parasitology</subject><subject>Parasites</subject><subject>Parasitology</subject><subject>Physiological aspects</subject><subject>Plasmodium falciparum</subject><subject>Plasmodium falciparum - genetics</subject><subject>Plasmodium falciparum - immunology</subject><subject>Plasmodium falciparum - pathogenicity</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Protozoan Proteins - chemistry</subject><subject>Protozoan Proteins - genetics</subject><subject>Protozoan Proteins - immunology</subject><subject>Reactivity</subject><subject>Receptors</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - immunology</subject><subject>Red blood cells</subject><subject>Risk factors</subject><subject>Rosette Formation</subject><subject>Spectrum analysis</subject><subject>Vaccination</subject><subject>Vaccines</subject><subject>Vector-borne 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of the Plasmodium falciparum PfEMP1-VarO Adhesin: Induction of Surface-Reactive and Rosette-Disrupting Antibodies to VarO Infected Erythrocytes</title><author>Guillotte, Micheline ; Juillerat, Alexandre ; Igonet, Sébastien ; Hessel, Audrey ; Petres, Stéphane ; Crublet, Elodie ; Le Scanf, Cécile ; Lewit-Bentley, Anita ; Bentley, Graham A ; Vigan-Womas, Inès ; Mercereau-Puijalon, Odile</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c726t-dff3241139dbd760e4f6b09ba55650ebcc890be11bc3390b3b4d8ec375b032a03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>ABO system</topic><topic>Adaptive immunology</topic><topic>Adhesins</topic><topic>Adhesins, Bacterial - chemistry</topic><topic>Adhesins, Bacterial - genetics</topic><topic>Adhesins, Bacterial - immunology</topic><topic>Alkylation</topic><topic>Analysis</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies, Protozoan - blood</topic><topic>Antigenicity</topic><topic>Antigens</topic><topic>Antigens, Protozoan - chemistry</topic><topic>Antigens, Protozoan - genetics</topic><topic>Binding</topic><topic>Blood</topic><topic>Blood cells</topic><topic>Blood groups</topic><topic>Cross Reactions</topic><topic>Cross-reactivity</topic><topic>Disruption</topic><topic>E coli</topic><topic>Enzyme-linked immunosorbent assay</topic><topic>Epitopes</topic><topic>Epitopes - chemistry</topic><topic>Epitopes - genetics</topic><topic>Erythrocyte membrane protein 1</topic><topic>Erythrocytes</topic><topic>Erythrocytes - parasitology</topic><topic>Escherichia coli</topic><topic>Feasibility studies</topic><topic>Female</topic><topic>Human health and pathology</topic><topic>Humans</topic><topic>Immunogenicity</topic><topic>Immunoglobulins</topic><topic>Immunology</topic><topic>Infectious diseases</topic><topic>Laboratory animals</topic><topic>Life Sciences</topic><topic>Malaria</topic><topic>Malaria Vaccines - chemistry</topic><topic>Malaria Vaccines - genetics</topic><topic>Malaria Vaccines - immunology</topic><topic>Malaria, Falciparum - immunology</topic><topic>Malaria, Falciparum - parasitology</topic><topic>Malaria, Falciparum - prevention & control</topic><topic>Membrane proteins</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Microbial adhesion</topic><topic>Microbiology and Parasitology</topic><topic>Parasites</topic><topic>Parasitology</topic><topic>Physiological aspects</topic><topic>Plasmodium falciparum</topic><topic>Plasmodium falciparum - genetics</topic><topic>Plasmodium falciparum - immunology</topic><topic>Plasmodium falciparum - pathogenicity</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Protozoan Proteins - chemistry</topic><topic>Protozoan Proteins - genetics</topic><topic>Protozoan Proteins - immunology</topic><topic>Reactivity</topic><topic>Receptors</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - immunology</topic><topic>Red blood cells</topic><topic>Risk factors</topic><topic>Rosette Formation</topic><topic>Spectrum analysis</topic><topic>Vaccination</topic><topic>Vaccines</topic><topic>Vector-borne diseases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Guillotte, Micheline</creatorcontrib><creatorcontrib>Juillerat, Alexandre</creatorcontrib><creatorcontrib>Igonet, Sébastien</creatorcontrib><creatorcontrib>Hessel, Audrey</creatorcontrib><creatorcontrib>Petres, Stéphane</creatorcontrib><creatorcontrib>Crublet, Elodie</creatorcontrib><creatorcontrib>Le Scanf, Cécile</creatorcontrib><creatorcontrib>Lewit-Bentley, Anita</creatorcontrib><creatorcontrib>Bentley, Graham A</creatorcontrib><creatorcontrib>Vigan-Womas, Inès</creatorcontrib><creatorcontrib>Mercereau-Puijalon, 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Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Guillotte, Micheline</au><au>Juillerat, Alexandre</au><au>Igonet, Sébastien</au><au>Hessel, Audrey</au><au>Petres, Stéphane</au><au>Crublet, Elodie</au><au>Le Scanf, Cécile</au><au>Lewit-Bentley, Anita</au><au>Bentley, Graham A</au><au>Vigan-Womas, Inès</au><au>Mercereau-Puijalon, Odile</au><au>Tsuboi, Takafumi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immunogenicity of the Plasmodium falciparum PfEMP1-VarO Adhesin: Induction of Surface-Reactive and Rosette-Disrupting Antibodies to VarO Infected Erythrocytes</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2015-07-29</date><risdate>2015</risdate><volume>10</volume><issue>7</issue><spage>e0134292</spage><epage>e0134292</epage><pages>e0134292-e0134292</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Adhesion of Plasmodium falciparum-infected red blood cells (iRBC) to human erythrocytes (i.e. rosetting) is associated with severe malaria. Rosetting results from interactions between a subset of variant PfEMP1 (Plasmodium falciparum erythrocyte membrane protein 1) adhesins and specific erythrocyte receptors. Interfering with such interactions is considered a promising intervention against severe malaria. To evaluate the feasibility of a vaccine strategy targetting rosetting, we have used here the Palo Alto 89F5 VarO rosetting model. PfEMP1-VarO consists of five Duffy-Binding Like domains (DBL1-5) and one Cysteine-rich Interdomain Region (CIDR1). The binding domain has been mapped to DBL1 and the ABO blood group was identified as the erythrocyte receptor. Here, we study the immunogenicity of all six recombinant PfEMP1-VarO domains and the DBL1- CIDR1 Head domain in BALB/c and outbred OF1 mice. Five readouts of antibody responses are explored: ELISA titres on the recombinant antigen, VarO-iRBC immunoblot reactivity, VarO-iRBC surface-reactivity, capacity to disrupt VarO rosettes and the capacity to prevent VarO rosette formation. For three domains, we explore influence of the expression system on antigenicity and immunogenicity. We show that correctly folded PfEMP1 domains elicit high antibody titres and induce a homogeneous response in outbred and BALB/c mice after three injections. High levels of rosette-disrupting and rosette-preventing antibodies are induced by DBL1 and the Head domain. Reduced-alkylated or denatured proteins fail to induce surface-reacting and rosette-disrupting antibodies, indicating that surface epitopes are conformational. We also report limited cross-reactivity between some PfEMP1 VarO domains. These results highlight the high immunogenicity of the individual domains in outbred animals and provide a strong basis for a rational vaccination strategy targeting rosetting.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26222304</pmid><doi>10.1371/journal.pone.0134292</doi><tpages>e0134292</tpages><orcidid>https://orcid.org/0000-0001-7848-9297</orcidid><orcidid>https://orcid.org/0000-0002-4716-565X</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2015-07, Vol.10 (7), p.e0134292-e0134292 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1700107652 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Public Library of Science (PLoS); PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | ABO system Adaptive immunology Adhesins Adhesins, Bacterial - chemistry Adhesins, Bacterial - genetics Adhesins, Bacterial - immunology Alkylation Analysis Animals Antibodies Antibodies, Protozoan - blood Antigenicity Antigens Antigens, Protozoan - chemistry Antigens, Protozoan - genetics Binding Blood Blood cells Blood groups Cross Reactions Cross-reactivity Disruption E coli Enzyme-linked immunosorbent assay Epitopes Epitopes - chemistry Epitopes - genetics Erythrocyte membrane protein 1 Erythrocytes Erythrocytes - parasitology Escherichia coli Feasibility studies Female Human health and pathology Humans Immunogenicity Immunoglobulins Immunology Infectious diseases Laboratory animals Life Sciences Malaria Malaria Vaccines - chemistry Malaria Vaccines - genetics Malaria Vaccines - immunology Malaria, Falciparum - immunology Malaria, Falciparum - parasitology Malaria, Falciparum - prevention & control Membrane proteins Mice Mice, Inbred BALB C Microbial adhesion Microbiology and Parasitology Parasites Parasitology Physiological aspects Plasmodium falciparum Plasmodium falciparum - genetics Plasmodium falciparum - immunology Plasmodium falciparum - pathogenicity Protein Structure, Tertiary Proteins Protozoan Proteins - chemistry Protozoan Proteins - genetics Protozoan Proteins - immunology Reactivity Receptors Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - immunology Red blood cells Risk factors Rosette Formation Spectrum analysis Vaccination Vaccines Vector-borne diseases |
| title | Immunogenicity of the Plasmodium falciparum PfEMP1-VarO Adhesin: Induction of Surface-Reactive and Rosette-Disrupting Antibodies to VarO Infected Erythrocytes |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T03%3A00%3A05IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Immunogenicity%20of%20the%20Plasmodium%20falciparum%20PfEMP1-VarO%20Adhesin:%20Induction%20of%20Surface-Reactive%20and%20Rosette-Disrupting%20Antibodies%20to%20VarO%20Infected%20Erythrocytes&rft.jtitle=PloS%20one&rft.au=Guillotte,%20Micheline&rft.date=2015-07-29&rft.volume=10&rft.issue=7&rft.spage=e0134292&rft.epage=e0134292&rft.pages=e0134292-e0134292&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0134292&rft_dat=%3Cgale_plos_%3EA455367890%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1700107652&rft_id=info:pmid/26222304&rft_galeid=A455367890&rft_doaj_id=oai_doaj_org_article_cff3771abc2046d38bc0f9436991bc3e&rfr_iscdi=true |