Multivalent fusion protein vaccine for lymphatic filariasis.
Identifieur interne : 001F25 ( PubMed/Curation ); précédent : 001F24; suivant : 001F26Multivalent fusion protein vaccine for lymphatic filariasis.
Auteurs : Gajalakshmi Dakshinamoorthy [États-Unis] ; Abhilash Kumble Samykutty ; Gnanasekar Munirathinam ; Maryada Venkatarami Reddy ; Ramaswamy KalyanasundaramSource :
- Vaccine [ 1873-2518 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux, Anticorps antihelminthe (sang), Antigènes d'helminthe (immunologie), Brugia malayi, Filariose lymphatique (), Humains, Immunité cellulaire, Lymphocytes auxiliaires Th1 (immunologie), Lymphocytes auxiliaires Th2 (immunologie), Production d'anticorps, Protéines de fusion recombinantes (immunologie), Protéines du choc thermique (immunologie), Protéines recombinantes (immunologie), Souris, Souris de lignée BALB C, Tétraspanines (immunologie), Vaccins (immunologie), Vaccins à ADN (immunologie).
- MESH :
- immunologie : Antigènes d'helminthe, Lymphocytes auxiliaires Th1, Lymphocytes auxiliaires Th2, Protéines de fusion recombinantes, Protéines du choc thermique, Protéines recombinantes, Tétraspanines, Vaccins, Vaccins à ADN.
- sang : Anticorps antihelminthe.
- Animaux, Brugia malayi, Filariose lymphatique, Humains, Immunité cellulaire, Production d'anticorps, Souris, Souris de lignée BALB C.
English descriptors
- KwdEn :
- Animals, Antibodies, Helminth (blood), Antibody Formation, Antigens, Helminth (immunology), Brugia malayi, Elephantiasis, Filarial (prevention & control), Heat-Shock Proteins (immunology), Humans, Immunity, Cellular, Mice, Mice, Inbred BALB C, Recombinant Fusion Proteins (immunology), Recombinant Proteins (immunology), Tetraspanins (immunology), Th1 Cells (immunology), Th2 Cells (immunology), Vaccines (immunology), Vaccines, DNA (immunology).
- MESH :
- chemical , blood : Antibodies, Helminth.
- chemical , immunology : Antigens, Helminth, Heat-Shock Proteins, Recombinant Fusion Proteins, Recombinant Proteins, Tetraspanins, Vaccines, Vaccines, DNA.
- immunology : Th1 Cells, Th2 Cells.
- prevention & control : Elephantiasis, Filarial.
- Animals, Antibody Formation, Brugia malayi, Humans, Immunity, Cellular, Mice, Mice, Inbred BALB C.
Abstract
Lymphatic filariasis affects approximately 3% of the whole world population. Mass drug administration is currently the major control strategy to eradicate this infection from endemic regions by year 2020. Combination drug treatments are highly efficient in controlling the infection. However, there are no effective vaccines available for human or animal lymphatic filariasis despite the identification of several subunit vaccines. Lymphatic filariasis parasites are multicellular organisms and potentially use multiple mechanisms to survive in the host. Therefore, there is a need to combine two or more vaccine candidate antigens to achieve the desired effect. In this study we combined three well characterized vaccine antigens of Brugia malayi, heat shock protein 12.6 (HSP12.6), Abundant Larval transcript-2 (ALT-2) and tetraspanin large extra cellular loop (TSP-LEL) as a multivalent fusion vaccine. Putative immune individuals carry circulating antibodies against all three antigens. Depletion of these antigen specific antibodies from the sera samples removed the ability of the sera to participate in the killing of B. malayi L3 in an antibody dependent cellular cytotoxicity (ADCC) mechanism. Vaccination trials in mice with a bivalent [HSP12.6+ALT-2 (HA), HSP12.6+TSP-LEL (HT) or TSP-LEL+ALT-2 (TA)] or trivalent [HSP12.6+ALT-2+TSP-LEL (HAT)] vaccines using DNA, protein or heterologous prime boost regimen showed that trivalent HAT vaccine either as protein alone or as heterologous prime boost vaccine could confer significant protection (95%) against B. malayi L3 challenge. Immune correlates of protection suggest a Th1/Th2 bias. These finding suggests that the trivalent HAT fusion protein is a promising prophylactic vaccine against lymphatic filariasis infection in human.
DOI: 10.1016/j.vaccine.2012.09.055
PubMed: 23036503
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Proteins (immunology)</term><term>Humans</term><term>Immunity, Cellular</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Recombinant Fusion Proteins (immunology)</term><term>Recombinant Proteins (immunology)</term><term>Tetraspanins (immunology)</term><term>Th1 Cells (immunology)</term><term>Th2 Cells (immunology)</term><term>Vaccines (immunology)</term><term>Vaccines, DNA (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Anticorps antihelminthe (sang)</term><term>Antigènes d'helminthe (immunologie)</term><term>Brugia malayi</term><term>Filariose lymphatique ()</term><term>Humains</term><term>Immunité cellulaire</term><term>Lymphocytes auxiliaires Th1 (immunologie)</term><term>Lymphocytes auxiliaires Th2 (immunologie)</term><term>Production d'anticorps</term><term>Protéines de fusion recombinantes (immunologie)</term><term>Protéines du choc thermique (immunologie)</term><term>Protéines recombinantes (immunologie)</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Tétraspanines (immunologie)</term><term>Vaccins (immunologie)</term><term>Vaccins à ADN (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="blood" xml:lang="en"><term>Antibodies, Helminth</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antigens, Helminth</term><term>Heat-Shock Proteins</term><term>Recombinant Fusion Proteins</term><term>Recombinant Proteins</term><term>Tetraspanins</term><term>Vaccines</term><term>Vaccines, DNA</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Antigènes d'helminthe</term><term>Lymphocytes auxiliaires Th1</term><term>Lymphocytes auxiliaires Th2</term><term>Protéines de fusion recombinantes</term><term>Protéines du choc thermique</term><term>Protéines recombinantes</term><term>Tétraspanines</term><term>Vaccins</term><term>Vaccins à ADN</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Th1 Cells</term><term>Th2 Cells</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Elephantiasis, Filarial</term></keywords><keywords scheme="MESH" qualifier="sang" xml:lang="fr"><term>Anticorps antihelminthe</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Antibody Formation</term><term>Brugia malayi</term><term>Humans</term><term>Immunity, Cellular</term><term>Mice</term><term>Mice, Inbred BALB C</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Brugia malayi</term><term>Filariose lymphatique</term><term>Humains</term><term>Immunité cellulaire</term><term>Production d'anticorps</term><term>Souris</term><term>Souris de lignée BALB C</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lymphatic filariasis affects approximately 3% of the whole world population. Mass drug administration is currently the major control strategy to eradicate this infection from endemic regions by year 2020. Combination drug treatments are highly efficient in controlling the infection. However, there are no effective vaccines available for human or animal lymphatic filariasis despite the identification of several subunit vaccines. Lymphatic filariasis parasites are multicellular organisms and potentially use multiple mechanisms to survive in the host. Therefore, there is a need to combine two or more vaccine candidate antigens to achieve the desired effect. In this study we combined three well characterized vaccine antigens of Brugia malayi, heat shock protein 12.6 (HSP12.6), Abundant Larval transcript-2 (ALT-2) and tetraspanin large extra cellular loop (TSP-LEL) as a multivalent fusion vaccine. Putative immune individuals carry circulating antibodies against all three antigens. Depletion of these antigen specific antibodies from the sera samples removed the ability of the sera to participate in the killing of B. malayi L3 in an antibody dependent cellular cytotoxicity (ADCC) mechanism. Vaccination trials in mice with a bivalent [HSP12.6+ALT-2 (HA), HSP12.6+TSP-LEL (HT) or TSP-LEL+ALT-2 (TA)] or trivalent [HSP12.6+ALT-2+TSP-LEL (HAT)] vaccines using DNA, protein or heterologous prime boost regimen showed that trivalent HAT vaccine either as protein alone or as heterologous prime boost vaccine could confer significant protection (95%) against B. malayi L3 challenge. Immune correlates of protection suggest a Th1/Th2 bias. These finding suggests that the trivalent HAT fusion protein is a promising prophylactic vaccine against lymphatic filariasis infection in human.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23036503</PMID><DateCreated><Year>2013</Year><Month>03</Month><Day>04</Day></DateCreated><DateCompleted><Year>2013</Year><Month>08</Month><Day>05</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-2518</ISSN><JournalIssue CitedMedium="Internet"><Volume>31</Volume><Issue>12</Issue><PubDate><Year>2013</Year><Month>Mar</Month><Day>15</Day></PubDate></JournalIssue><Title>Vaccine</Title><ISOAbbreviation>Vaccine</ISOAbbreviation></Journal><ArticleTitle>Multivalent fusion protein vaccine for lymphatic filariasis.</ArticleTitle><Pagination><MedlinePgn>1616-22</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.vaccine.2012.09.055</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0264-410X(12)01375-8</ELocationID><Abstract><AbstractText>Lymphatic filariasis affects approximately 3% of the whole world population. Mass drug administration is currently the major control strategy to eradicate this infection from endemic regions by year 2020. Combination drug treatments are highly efficient in controlling the infection. However, there are no effective vaccines available for human or animal lymphatic filariasis despite the identification of several subunit vaccines. Lymphatic filariasis parasites are multicellular organisms and potentially use multiple mechanisms to survive in the host. Therefore, there is a need to combine two or more vaccine candidate antigens to achieve the desired effect. In this study we combined three well characterized vaccine antigens of Brugia malayi, heat shock protein 12.6 (HSP12.6), Abundant Larval transcript-2 (ALT-2) and tetraspanin large extra cellular loop (TSP-LEL) as a multivalent fusion vaccine. Putative immune individuals carry circulating antibodies against all three antigens. Depletion of these antigen specific antibodies from the sera samples removed the ability of the sera to participate in the killing of B. malayi L3 in an antibody dependent cellular cytotoxicity (ADCC) mechanism. Vaccination trials in mice with a bivalent [HSP12.6+ALT-2 (HA), HSP12.6+TSP-LEL (HT) or TSP-LEL+ALT-2 (TA)] or trivalent [HSP12.6+ALT-2+TSP-LEL (HAT)] vaccines using DNA, protein or heterologous prime boost regimen showed that trivalent HAT vaccine either as protein alone or as heterologous prime boost vaccine could confer significant protection (95%) against B. malayi L3 challenge. Immune correlates of protection suggest a Th1/Th2 bias. These finding suggests that the trivalent HAT fusion protein is a promising prophylactic vaccine against lymphatic filariasis infection in human.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dakshinamoorthy</LastName><ForeName>Gajalakshmi</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Biomedical Sciences, University of Illinois, College of Medicine at Rockford, IL 61107, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Samykutty</LastName><ForeName>Abhilash Kumble</ForeName><Initials>AK</Initials></Author><Author ValidYN="Y"><LastName>Munirathinam</LastName><ForeName>Gnanasekar</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Reddy</LastName><ForeName>Maryada Venkatarami</ForeName><Initials>MV</Initials></Author><Author ValidYN="Y"><LastName>Kalyanasundaram</LastName><ForeName>Ramaswamy</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI064745</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R56 AI064745</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI064745</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>10</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Vaccine</MedlineTA><NlmUniqueID>8406899</NlmUniqueID><ISSNLinking>0264-410X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C521555">ALT-2 protein, Brugia malayi</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000909">Antibodies, Helminth</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000947">Antigens, Helminth</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006360">Heat-Shock Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D059470">Tetraspanins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014612">Vaccines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019444">Vaccines, DNA</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections 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Source="NLM">NIHMS410997</OtherID><OtherID Source="NLM">PMC3554871</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>06</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>09</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>09</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>10</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>10</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>8</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23036503</ArticleId><ArticleId IdType="pii">S0264-410X(12)01375-8</ArticleId><ArticleId 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