Potential recombinant vaccine against influenza A virus based on M2e displayed on nodaviral capsid nanoparticles.
Identifieur interne : 000665 ( PubMed/Corpus ); précédent : 000664; suivant : 000666Potential recombinant vaccine against influenza A virus based on M2e displayed on nodaviral capsid nanoparticles.
Auteurs : Chean Yeah Yong ; Swee Keong Yeap ; Kok Lian Ho ; Abdul Rahman Omar ; Wen Siang TanSource :
- International journal of nanomedicine [ 1178-2013 ] ; 2015.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Base Sequence, Blotting, Western, Capsid Proteins (chemistry), Capsid Proteins (metabolism), Enzyme-Linked Immunosorbent Assay, Female, Immunophenotyping, Influenza A virus (chemistry), Influenza A virus (metabolism), Influenza Vaccines (immunology), Influenza Vaccines (therapeutic use), Mice, Mice, Inbred BALB C, Microscopy, Electron, Transmission, Molecular Sequence Data, Nanoparticles (chemistry), Nanoparticles (metabolism), Orthomyxoviridae Infections (immunology), Orthomyxoviridae Infections (prevention & control), Orthomyxoviridae Infections (virology), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (immunology), Vaccination, Vaccines, Synthetic (immunology), Vaccines, Synthetic (therapeutic use), Viral Matrix Proteins (chemistry), Viral Matrix Proteins (metabolism).
- MESH :
- chemical , chemistry : Capsid Proteins, Viral Matrix Proteins.
- chemical , genetics : Recombinant Fusion Proteins.
- chemical , immunology : Influenza Vaccines, Recombinant Fusion Proteins, Vaccines, Synthetic.
- chemical , metabolism : Capsid Proteins, Viral Matrix Proteins.
- chemistry : Influenza A virus, Nanoparticles.
- immunology : Orthomyxoviridae Infections.
- metabolism : Influenza A virus, Nanoparticles.
- prevention & control : Orthomyxoviridae Infections.
- chemical , therapeutic use : Influenza Vaccines, Vaccines, Synthetic.
- virology : Orthomyxoviridae Infections.
- Amino Acid Sequence, Animals, Base Sequence, Blotting, Western, Enzyme-Linked Immunosorbent Assay, Female, Immunophenotyping, Mice, Mice, Inbred BALB C, Microscopy, Electron, Transmission, Molecular Sequence Data, Vaccination.
Abstract
Influenza A virus poses a major threat to human health, causing outbreaks from time to time. Currently available vaccines employ inactivated viruses of different strains to provide protection against influenza virus infection. However, high mutation rates of influenza virus hemagglutinin (H) and neuraminidase (N) glycoproteins give rise to vaccine escape mutants. Thus, an effective vaccine providing protection against all strains of influenza virus would be a valuable asset. The ectodomain of matrix 2 protein (M2e) was found to be highly conserved despite mutations of the H and N glycoproteins. Hence, one to five copies of M2e were fused to the carboxyl-terminal end of the recombinant nodavirus capsid protein derived from Macrobrachium rosenbergii. The chimeric proteins harboring up to five copies of M2e formed nanosized virus-like particles approximately 30 nm in diameter, which could be purified easily by immobilized metal affinity chromatography. BALB/c mice immunized subcutaneously with these chimeric proteins developed antibodies specifically against M2e, and the titer was proportional to the copy numbers of M2e displayed on the nodavirus capsid nanoparticles. The fusion proteins also induced a type 1 T helper immune response. Collectively, M2e displayed on the nodavirus capsid nanoparticles could provide an alternative solution to a possible influenza pandemic in the future.
DOI: 10.2147/IJN.S77405
PubMed: 25897220
Links to Exploration step
pubmed:25897220Le document en format XML
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Department of Veterinary Pathology and Microbiology, Faculty of Veterinary Medicine, Universiti Putra Malaysia, Selangor, Malaysia.</nlm:affiliation></affiliation></author><author><name sortKey="Tan, Wen Siang" sort="Tan, Wen Siang" uniqKey="Tan W" first="Wen Siang" last="Tan">Wen Siang Tan</name><affiliation><nlm:affiliation>Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, Malaysia ; Institute of Bioscience, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, Selangor, Malaysia.</nlm:affiliation></affiliation></author></analytic><series><title level="j">International journal of nanomedicine</title><idno type="eISSN">1178-2013</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Blotting, Western</term><term>Capsid Proteins (chemistry)</term><term>Capsid Proteins (metabolism)</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Female</term><term>Immunophenotyping</term><term>Influenza A virus (chemistry)</term><term>Influenza A virus (metabolism)</term><term>Influenza Vaccines (immunology)</term><term>Influenza Vaccines (therapeutic use)</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Microscopy, Electron, Transmission</term><term>Molecular Sequence Data</term><term>Nanoparticles (chemistry)</term><term>Nanoparticles (metabolism)</term><term>Orthomyxoviridae Infections (immunology)</term><term>Orthomyxoviridae Infections (prevention & control)</term><term>Orthomyxoviridae Infections (virology)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (immunology)</term><term>Vaccination</term><term>Vaccines, Synthetic (immunology)</term><term>Vaccines, Synthetic (therapeutic use)</term><term>Viral Matrix Proteins (chemistry)</term><term>Viral Matrix Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Capsid Proteins</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Influenza Vaccines</term><term>Recombinant Fusion Proteins</term><term>Vaccines, Synthetic</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Capsid Proteins</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Influenza A virus</term><term>Nanoparticles</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Orthomyxoviridae Infections</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Influenza A virus</term><term>Nanoparticles</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Orthomyxoviridae Infections</term></keywords><keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>Influenza Vaccines</term><term>Vaccines, Synthetic</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Orthomyxoviridae Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Blotting, Western</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Female</term><term>Immunophenotyping</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Microscopy, Electron, Transmission</term><term>Molecular Sequence Data</term><term>Vaccination</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Influenza A virus poses a major threat to human health, causing outbreaks from time to time. Currently available vaccines employ inactivated viruses of different strains to provide protection against influenza virus infection. However, high mutation rates of influenza virus hemagglutinin (H) and neuraminidase (N) glycoproteins give rise to vaccine escape mutants. Thus, an effective vaccine providing protection against all strains of influenza virus would be a valuable asset. The ectodomain of matrix 2 protein (M2e) was found to be highly conserved despite mutations of the H and N glycoproteins. Hence, one to five copies of M2e were fused to the carboxyl-terminal end of the recombinant nodavirus capsid protein derived from Macrobrachium rosenbergii. The chimeric proteins harboring up to five copies of M2e formed nanosized virus-like particles approximately 30 nm in diameter, which could be purified easily by immobilized metal affinity chromatography. BALB/c mice immunized subcutaneously with these chimeric proteins developed antibodies specifically against M2e, and the titer was proportional to the copy numbers of M2e displayed on the nodavirus capsid nanoparticles. The fusion proteins also induced a type 1 T helper immune response. Collectively, M2e displayed on the nodavirus capsid nanoparticles could provide an alternative solution to a possible influenza pandemic in the future. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">25897220</PMID><DateCompleted><Year>2016</Year><Month>08</Month><Day>16</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>02</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1178-2013</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><PubDate><Year>2015</Year></PubDate></JournalIssue><Title>International journal of nanomedicine</Title><ISOAbbreviation>Int J Nanomedicine</ISOAbbreviation></Journal><ArticleTitle>Potential recombinant vaccine against influenza A virus based on M2e displayed on nodaviral capsid nanoparticles.</ArticleTitle><Pagination><MedlinePgn>2751-63</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.2147/IJN.S77405</ELocationID><Abstract><AbstractText>Influenza A virus poses a major threat to human health, causing outbreaks from time to time. Currently available vaccines employ inactivated viruses of different strains to provide protection against influenza virus infection. However, high mutation rates of influenza virus hemagglutinin (H) and neuraminidase (N) glycoproteins give rise to vaccine escape mutants. Thus, an effective vaccine providing protection against all strains of influenza virus would be a valuable asset. The ectodomain of matrix 2 protein (M2e) was found to be highly conserved despite mutations of the H and N glycoproteins. Hence, one to five copies of M2e were fused to the carboxyl-terminal end of the recombinant nodavirus capsid protein derived from Macrobrachium rosenbergii. The chimeric proteins harboring up to five copies of M2e formed nanosized virus-like particles approximately 30 nm in diameter, which could be purified easily by immobilized metal affinity chromatography. BALB/c mice immunized subcutaneously with these chimeric proteins developed antibodies specifically against M2e, and the titer was proportional to the copy numbers of M2e displayed on the nodavirus capsid nanoparticles. The fusion proteins also induced a type 1 T helper immune response. Collectively, M2e displayed on the nodavirus capsid nanoparticles could provide an alternative solution to a possible influenza pandemic in the future. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yong</LastName><ForeName>Chean Yeah</ForeName><Initials>CY</Initials><AffiliationInfo><Affiliation>Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, Malaysia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yeap</LastName><ForeName>Swee Keong</ForeName><Initials>SK</Initials><AffiliationInfo><Affiliation>Institute of Bioscience, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, Selangor, Malaysia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ho</LastName><ForeName>Kok Lian</ForeName><Initials>KL</Initials><AffiliationInfo><Affiliation>Department of Pathology, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, Selangor, Malaysia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Omar</LastName><ForeName>Abdul Rahman</ForeName><Initials>AR</Initials><AffiliationInfo><Affiliation>Institute of Bioscience, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, Selangor, Malaysia ; Department of Veterinary Pathology and Microbiology, Faculty of Veterinary Medicine, Universiti Putra Malaysia, Selangor, Malaysia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Wen Siang</ForeName><Initials>WS</Initials><AffiliationInfo><Affiliation>Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, Malaysia ; Institute of Bioscience, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, Selangor, Malaysia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal 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