Natural antibody responses to the capsid protein in sera of Dengue infected patients from Sri Lanka
This study aims to characterize the antigenicity of the Capsid (C) protein and the human antibody responses to C protein from the four dengue virus (DENV) serotypes. Parker hydrophilicity prediction, Emini surface accessibility prediction and Karplus & Schulz flexibility predictions were used to...
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| Veröffentlicht in: | PloS one 2017-06, Vol.12 (6), p.e0178009-e0178009 |
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| creator | Nadugala, Mahesha N Jeewandara, Chandima Malavige, Gathsaurie N Premaratne, Prasad H Goonasekara, Charitha L |
| description | This study aims to characterize the antigenicity of the Capsid (C) protein and the human antibody responses to C protein from the four dengue virus (DENV) serotypes. Parker hydrophilicity prediction, Emini surface accessibility prediction and Karplus & Schulz flexibility predictions were used to bioinformatically characterize antigenicity. The human antibody response to C protein was assessed by ELISA using immune sera and an array of overlapping DENV2 C peptides. DENV2 C protein peptides P1 (located on C protein at 2-18 a.a), P11 (79-95 a.a) and P12 (86-101 a.a) were recognized by most individuals exposed to infections with only one of the 4 DENV serotypes as well as people exposed to infections with two serotypes. These conserved peptide epitopes are located on the amino (1-40 a.a) and carboxy (70-100 a.a) terminal regions of C protein, which were predicted to be antigenic using different bioinformatic tools. DENV2 C peptide P6 (39-56 a.a) was recognized by all individuals exposed to DENV2 infections, some individuals exposed to DENV4 infections and none of the individuals exposed to DENV1 or 3 infections. Thus, unlike C peptides P1, P11 and P12, which contain epitopes, recognized by DENV serotype cross-reactive antibodies, DENV2 peptide P6 contains an epitope that is preferentially recognized by antibodies in people exposed to this serotype compared to other serotypes. We discuss our results in the context of the known structure of C protein and recent work on the human B-cell response to DENV infection. |
| doi_str_mv | 10.1371/journal.pone.0178009 |
| format | Article |
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Parker hydrophilicity prediction, Emini surface accessibility prediction and Karplus & Schulz flexibility predictions were used to bioinformatically characterize antigenicity. The human antibody response to C protein was assessed by ELISA using immune sera and an array of overlapping DENV2 C peptides. DENV2 C protein peptides P1 (located on C protein at 2-18 a.a), P11 (79-95 a.a) and P12 (86-101 a.a) were recognized by most individuals exposed to infections with only one of the 4 DENV serotypes as well as people exposed to infections with two serotypes. These conserved peptide epitopes are located on the amino (1-40 a.a) and carboxy (70-100 a.a) terminal regions of C protein, which were predicted to be antigenic using different bioinformatic tools. DENV2 C peptide P6 (39-56 a.a) was recognized by all individuals exposed to DENV2 infections, some individuals exposed to DENV4 infections and none of the individuals exposed to DENV1 or 3 infections. Thus, unlike C peptides P1, P11 and P12, which contain epitopes, recognized by DENV serotype cross-reactive antibodies, DENV2 peptide P6 contains an epitope that is preferentially recognized by antibodies in people exposed to this serotype compared to other serotypes. We discuss our results in the context of the known structure of C protein and recent work on the human B-cell response to DENV infection.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0178009</identifier><identifier>PMID: 28582388</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Accessibility ; Adolescent ; Adult ; Aged ; Amino Acid Sequence ; Amino acids ; Antibodies ; Antibodies, Viral - biosynthesis ; Antibodies, Viral - chemistry ; Antibody response ; Antigenicity ; Antigens ; Antigens, Viral - chemistry ; Antigens, Viral - genetics ; Antigens, Viral - immunology ; Antisera ; Binding Sites ; Biology and Life Sciences ; C protein ; Capsid protein ; Capsid Proteins - chemistry ; Capsid Proteins - genetics ; Capsid Proteins - immunology ; Care and treatment ; Child ; Dengue ; Dengue - immunology ; Dengue - virology ; Dengue fever ; Dengue virus ; Dengue Virus - classification ; Dengue Virus - genetics ; Dengue Virus - immunology ; Dosage and administration ; Enzyme-linked immunosorbent assay ; Epitope Mapping ; Epitopes ; Epitopes - chemistry ; Epitopes - genetics ; Exposure ; Female ; Flexibility ; Genomes ; Health aspects ; Humans ; Hydrophilicity ; Immune Sera - chemistry ; Immune serum ; Immunity, Innate ; Immunoglobulins ; Infections ; Lymphocytes B ; Male ; Medicine and Health Sciences ; Methods ; Middle Aged ; Patients ; Peptides ; Peptides - chemistry ; Peptides - genetics ; Peptides - immunology ; Phylogenetics ; Phylogeny ; Predictions ; Prevention ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein structure ; Protein Structure, Secondary ; Proteins ; Research and Analysis Methods ; Serogroup ; Serotypes ; Sri Lanka ; Vector-borne diseases ; Viral diseases ; Viral infections ; Viral proteins ; Viruses</subject><ispartof>PloS one, 2017-06, Vol.12 (6), p.e0178009-e0178009</ispartof><rights>COPYRIGHT 2017 Public Library of Science</rights><rights>2017 Nadugala 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>2017 Nadugala et al 2017 Nadugala et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-5d6f980ba615fca915f3d69af8022c123c0f7284c170b7e4cdb01cf3053b14693</citedby><cites>FETCH-LOGICAL-c758t-5d6f980ba615fca915f3d69af8022c123c0f7284c170b7e4cdb01cf3053b14693</cites><orcidid>0000-0002-6956-0095</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/PMC5459338/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5459338/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79569,79570</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28582388$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nadugala, Mahesha N</creatorcontrib><creatorcontrib>Jeewandara, Chandima</creatorcontrib><creatorcontrib>Malavige, Gathsaurie N</creatorcontrib><creatorcontrib>Premaratne, Prasad H</creatorcontrib><creatorcontrib>Goonasekara, Charitha L</creatorcontrib><title>Natural antibody responses to the capsid protein in sera of Dengue infected patients from Sri Lanka</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>This study aims to characterize the antigenicity of the Capsid (C) protein and the human antibody responses to C protein from the four dengue virus (DENV) serotypes. Parker hydrophilicity prediction, Emini surface accessibility prediction and Karplus & Schulz flexibility predictions were used to bioinformatically characterize antigenicity. The human antibody response to C protein was assessed by ELISA using immune sera and an array of overlapping DENV2 C peptides. DENV2 C protein peptides P1 (located on C protein at 2-18 a.a), P11 (79-95 a.a) and P12 (86-101 a.a) were recognized by most individuals exposed to infections with only one of the 4 DENV serotypes as well as people exposed to infections with two serotypes. These conserved peptide epitopes are located on the amino (1-40 a.a) and carboxy (70-100 a.a) terminal regions of C protein, which were predicted to be antigenic using different bioinformatic tools. DENV2 C peptide P6 (39-56 a.a) was recognized by all individuals exposed to DENV2 infections, some individuals exposed to DENV4 infections and none of the individuals exposed to DENV1 or 3 infections. Thus, unlike C peptides P1, P11 and P12, which contain epitopes, recognized by DENV serotype cross-reactive antibodies, DENV2 peptide P6 contains an epitope that is preferentially recognized by antibodies in people exposed to this serotype compared to other serotypes. We discuss our results in the context of the known structure of C protein and recent work on the human B-cell response to DENV infection.</description><subject>Accessibility</subject><subject>Adolescent</subject><subject>Adult</subject><subject>Aged</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Antibodies</subject><subject>Antibodies, Viral - biosynthesis</subject><subject>Antibodies, Viral - chemistry</subject><subject>Antibody response</subject><subject>Antigenicity</subject><subject>Antigens</subject><subject>Antigens, Viral - chemistry</subject><subject>Antigens, Viral - genetics</subject><subject>Antigens, Viral - immunology</subject><subject>Antisera</subject><subject>Binding Sites</subject><subject>Biology and Life Sciences</subject><subject>C protein</subject><subject>Capsid protein</subject><subject>Capsid Proteins - chemistry</subject><subject>Capsid Proteins - genetics</subject><subject>Capsid Proteins - immunology</subject><subject>Care and treatment</subject><subject>Child</subject><subject>Dengue</subject><subject>Dengue - immunology</subject><subject>Dengue - virology</subject><subject>Dengue fever</subject><subject>Dengue virus</subject><subject>Dengue Virus - classification</subject><subject>Dengue Virus - genetics</subject><subject>Dengue Virus - immunology</subject><subject>Dosage and administration</subject><subject>Enzyme-linked immunosorbent assay</subject><subject>Epitope Mapping</subject><subject>Epitopes</subject><subject>Epitopes - chemistry</subject><subject>Epitopes - genetics</subject><subject>Exposure</subject><subject>Female</subject><subject>Flexibility</subject><subject>Genomes</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Hydrophilicity</subject><subject>Immune Sera - chemistry</subject><subject>Immune serum</subject><subject>Immunity, Innate</subject><subject>Immunoglobulins</subject><subject>Infections</subject><subject>Lymphocytes B</subject><subject>Male</subject><subject>Medicine and Health Sciences</subject><subject>Methods</subject><subject>Middle Aged</subject><subject>Patients</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>Peptides - immunology</subject><subject>Phylogenetics</subject><subject>Phylogeny</subject><subject>Predictions</subject><subject>Prevention</subject><subject>Protein Binding</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein structure</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Research and Analysis Methods</subject><subject>Serogroup</subject><subject>Serotypes</subject><subject>Sri Lanka</subject><subject>Vector-borne diseases</subject><subject>Viral diseases</subject><subject>Viral infections</subject><subject>Viral proteins</subject><subject>Viruses</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqNk9-L1DAQx4so3nn6H4gGBNGHXZMmTZMX4Th_LSweeOprmKbJbtZusyapeP-9Wbd3bOUepKUpk898JzOZKYqnBM8JrcmbjR9CD91853szx6QWGMt7xSmRtJzxEtP7R_8nxaMYNxhXVHD-sDgpRSVKKsRpoT9DGgJ0CPrkGt9eo2BilowmouRRWhukYRddi3bBJ-N6lN9oAiBv0TvTrwaTLdboZDICyZk-RWSD36Kr4NAS-h_wuHhgoYvmybieFd8-vP968Wm2vPy4uDhfznRdiTSrWm6lwA1wUlkNMn9pyyVYgctSk5JqbOtSME1q3NSG6bbBRFuas2oI45KeFc8PurvORzXWJyoiMS-FIIxlYnEgWg8btQtuC-FaeXDqr8GHlYKQnO6MorZpBDSkoQCsFhJKwgWmrcYVrqXda70dow3N1rQ6J57rOBGd7vRurVb-l6pYJSkVWeDVKBD8z8HEpLYuatN10Bs_HM7NuKB8H-vFP-jd2Y3UCnIC-VZ8jqv3ouqcSZaz4BXP1PwOKj-t2Tqdm8m6bJ84vJ44ZCaZ32kFQ4xqcfXl_9nL71P25RG7NtCldfTdkFxuvynIDqAOPsZg7G2RCVb7WbiphtrPghpnIbs9O76gW6eb5qd_AIyCA-A</recordid><startdate>20170605</startdate><enddate>20170605</enddate><creator>Nadugala, Mahesha N</creator><creator>Jeewandara, Chandima</creator><creator>Malavige, Gathsaurie N</creator><creator>Premaratne, Prasad H</creator><creator>Goonasekara, Charitha L</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-6956-0095</orcidid></search><sort><creationdate>20170605</creationdate><title>Natural antibody responses to the capsid protein in sera of Dengue infected patients from Sri Lanka</title><author>Nadugala, Mahesha N ; Jeewandara, Chandima ; Malavige, Gathsaurie N ; Premaratne, Prasad H ; Goonasekara, Charitha L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c758t-5d6f980ba615fca915f3d69af8022c123c0f7284c170b7e4cdb01cf3053b14693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Accessibility</topic><topic>Adolescent</topic><topic>Adult</topic><topic>Aged</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Antibodies</topic><topic>Antibodies, Viral - 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Academic</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>Nadugala, Mahesha N</au><au>Jeewandara, Chandima</au><au>Malavige, Gathsaurie N</au><au>Premaratne, Prasad H</au><au>Goonasekara, Charitha L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Natural antibody responses to the capsid protein in sera of Dengue infected patients from Sri Lanka</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2017-06-05</date><risdate>2017</risdate><volume>12</volume><issue>6</issue><spage>e0178009</spage><epage>e0178009</epage><pages>e0178009-e0178009</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>This study aims to characterize the antigenicity of the Capsid (C) protein and the human antibody responses to C protein from the four dengue virus (DENV) serotypes. Parker hydrophilicity prediction, Emini surface accessibility prediction and Karplus & Schulz flexibility predictions were used to bioinformatically characterize antigenicity. The human antibody response to C protein was assessed by ELISA using immune sera and an array of overlapping DENV2 C peptides. DENV2 C protein peptides P1 (located on C protein at 2-18 a.a), P11 (79-95 a.a) and P12 (86-101 a.a) were recognized by most individuals exposed to infections with only one of the 4 DENV serotypes as well as people exposed to infections with two serotypes. These conserved peptide epitopes are located on the amino (1-40 a.a) and carboxy (70-100 a.a) terminal regions of C protein, which were predicted to be antigenic using different bioinformatic tools. DENV2 C peptide P6 (39-56 a.a) was recognized by all individuals exposed to DENV2 infections, some individuals exposed to DENV4 infections and none of the individuals exposed to DENV1 or 3 infections. Thus, unlike C peptides P1, P11 and P12, which contain epitopes, recognized by DENV serotype cross-reactive antibodies, DENV2 peptide P6 contains an epitope that is preferentially recognized by antibodies in people exposed to this serotype compared to other serotypes. We discuss our results in the context of the known structure of C protein and recent work on the human B-cell response to DENV infection.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>28582388</pmid><doi>10.1371/journal.pone.0178009</doi><orcidid>https://orcid.org/0000-0002-6956-0095</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2017-06, Vol.12 (6), p.e0178009-e0178009 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1906288144 |
| source | Public Library of Science (PLoS) Journals Open Access; MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Accessibility Adolescent Adult Aged Amino Acid Sequence Amino acids Antibodies Antibodies, Viral - biosynthesis Antibodies, Viral - chemistry Antibody response Antigenicity Antigens Antigens, Viral - chemistry Antigens, Viral - genetics Antigens, Viral - immunology Antisera Binding Sites Biology and Life Sciences C protein Capsid protein Capsid Proteins - chemistry Capsid Proteins - genetics Capsid Proteins - immunology Care and treatment Child Dengue Dengue - immunology Dengue - virology Dengue fever Dengue virus Dengue Virus - classification Dengue Virus - genetics Dengue Virus - immunology Dosage and administration Enzyme-linked immunosorbent assay Epitope Mapping Epitopes Epitopes - chemistry Epitopes - genetics Exposure Female Flexibility Genomes Health aspects Humans Hydrophilicity Immune Sera - chemistry Immune serum Immunity, Innate Immunoglobulins Infections Lymphocytes B Male Medicine and Health Sciences Methods Middle Aged Patients Peptides Peptides - chemistry Peptides - genetics Peptides - immunology Phylogenetics Phylogeny Predictions Prevention Protein Binding Protein Interaction Domains and Motifs Protein structure Protein Structure, Secondary Proteins Research and Analysis Methods Serogroup Serotypes Sri Lanka Vector-borne diseases Viral diseases Viral infections Viral proteins Viruses |
| title | Natural antibody responses to the capsid protein in sera of Dengue infected patients from Sri Lanka |
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