Functional characterization of Mycobacterium tuberculosis Rv2969c membrane protein

Identifying Mycobacterium tuberculosis membrane proteins involved in binding to and invasion of host cells is important in designing subunit-based anti-tuberculosis vaccines. The Rv2969c gene sequence was identified by PCR in M. tuberculosis complex strains, being transcribed in M. tuberculosis H37R...

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Autores:
Tipo de recurso:
Fecha de publicación:
2008
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/23489
Acceso en línea:
https://doi.org/10.1016/j.bbrc.2008.05.157
https://repository.urosario.edu.co/handle/10336/23489
Palabra clave:
Antibody
Isoleucyllysylglutamylisoleucylvalylglycylaspartylvalylprolyl glycylisoleucylaspartylserylalanylalanylalanylthreonylalanyl threonylseryltyrosine
Membrane protein
Peptide
Phenylalanyltyrosylisoleucylvalylthreonylserylarginylaspartyl aspartyllysyllysylaspartylglycylvalylalanylglycylprolylglycylaspartylalanine
Synthetic peptide
Animal experiment
Article
Controlled study
Gene sequence
Human
Human cell
Immunization
Immunoelectron microscopy
Lung alveolus epithelium
Monocyte
Mycobacterium tuberculosis
Nonhuman
Nucleotide sequence
Polymerase chain reaction
Priority journal
Rabbit
Amino acid sequence
Animals
Bacterial proteins
Cell line
Humans
Membrane proteins
Molecular sequence data
Mycobacterium tuberculosis
Peptides
Rabbits
Tuberculosis vaccines
Mycobacterium tuberculosis
Oryctolagus cuniculus
High activity binding peptide (habp)
Mycobacterium tuberculosis-host cell interaction
Rv2969c
immunoelectron
bacterial
bacterial
Antibodies
Genes
Microscopy
Rights
License
Abierto (Texto Completo)
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spelling 79653065-14f4f34c8-2d4c-491e-813c-5d61ee2d1048-151848826-191225589-184cece1e-359c-45a6-b251-f8e4b62a84eb-1efeb3f2a-28fa-4c7b-9d5e-cc72aef13437-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-12020-05-26T00:02:28Z2020-05-26T00:02:28Z2008Identifying Mycobacterium tuberculosis membrane proteins involved in binding to and invasion of host cells is important in designing subunit-based anti-tuberculosis vaccines. The Rv2969c gene sequence was identified by PCR in M. tuberculosis complex strains, being transcribed in M. tuberculosis H37Rv, M. tuberculosis H37Ra, and M. bovis BCG. Rabbits immunized with synthetic peptides from highly specific conserved regions of this protein produced antibodies recognizing 27 and 29 kDa bands in M. tuberculosis lysate, which is consistent with the molecular weight of the Rv2969c gene product in M. tuberculosis H37Rv. Immunoelectron microscopy revealed the protein was localized on the bacillus surface. Four and three specific high activity binding peptides (HABPs) to the A549 alveolar epithelial and U937 monocyte cell lines were found, respectively. Two of the HABPs found inhibited M. tuberculosis invasion of A549 cells, suggesting that these peptides might be good candidates to be included in a multiepitopic, subunit-based anti-tuberculosis vaccine. © 2008 Elsevier Inc. All rights reserved.application/pdfhttps://doi.org/10.1016/j.bbrc.2008.05.1570006291X10902104https://repository.urosario.edu.co/handle/10336/23489eng940No. 4935Biochemical and Biophysical Research CommunicationsVol. 372Biochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.372, No.4 (2008); pp. 935-940https://www.scopus.com/inward/record.uri?eid=2-s2.0-45449101647&doi=10.1016%2fj.bbrc.2008.05.157&partnerID=40&md5=046430185fb4c8a85c3c49efdd70b991Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURAntibodyIsoleucyllysylglutamylisoleucylvalylglycylaspartylvalylprolyl glycylisoleucylaspartylserylalanylalanylalanylthreonylalanyl threonylseryltyrosineMembrane proteinPeptidePhenylalanyltyrosylisoleucylvalylthreonylserylarginylaspartyl aspartyllysyllysylaspartylglycylvalylalanylglycylprolylglycylaspartylalanineSynthetic peptideAnimal experimentArticleControlled studyGene sequenceHumanHuman cellImmunizationImmunoelectron microscopyLung alveolus epitheliumMonocyteMycobacterium tuberculosisNonhumanNucleotide sequencePolymerase chain reactionPriority journalRabbitAmino acid sequenceAnimalsBacterial proteinsCell lineHumansMembrane proteinsMolecular sequence dataMycobacterium tuberculosisPeptidesRabbitsTuberculosis vaccinesMycobacterium tuberculosisOryctolagus cuniculusHigh activity binding peptide (habp)Mycobacterium tuberculosis-host cell interactionRv2969cimmunoelectronbacterialbacterialAntibodiesGenesMicroscopyFunctional characterization of Mycobacterium tuberculosis Rv2969c membrane proteinarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Patarroyo, Manuel A.Plaza, David F.Ocampo, MarisolCurtidor, HernandoForero, MarthaRodriguez, Luis E.Patarroyo, Manuel E.ORIGINALFunctional_characterization_of_Mycobacte.pdfapplication/pdf652452https://repository.urosario.edu.co/bitstreams/ccec94f0-a2ed-4ea8-a4ba-8176ac4d4ef1/download6fbb1e9fffe4c9115dc5061710edf8d0MD51TEXTFunctional_characterization_of_Mycobacte.pdf.txtFunctional_characterization_of_Mycobacte.pdf.txtExtracted texttext/plain30031https://repository.urosario.edu.co/bitstreams/314740f1-8306-4f87-b662-b711a51c2cf5/download4afe18846c3c0999f1a791ff6a8c1ba0MD52THUMBNAILFunctional_characterization_of_Mycobacte.pdf.jpgFunctional_characterization_of_Mycobacte.pdf.jpgGenerated Thumbnailimage/jpeg5026https://repository.urosario.edu.co/bitstreams/c79d750c-689a-4580-abc6-81ff332613d4/download6576b19cb9ca04cf522e1684545ad0b6MD5310336/23489oai:repository.urosario.edu.co:10336/234892022-05-02 07:37:21.007048https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Functional characterization of Mycobacterium tuberculosis Rv2969c membrane protein
title Functional characterization of Mycobacterium tuberculosis Rv2969c membrane protein
spellingShingle Functional characterization of Mycobacterium tuberculosis Rv2969c membrane protein
Antibody
Isoleucyllysylglutamylisoleucylvalylglycylaspartylvalylprolyl glycylisoleucylaspartylserylalanylalanylalanylthreonylalanyl threonylseryltyrosine
Membrane protein
Peptide
Phenylalanyltyrosylisoleucylvalylthreonylserylarginylaspartyl aspartyllysyllysylaspartylglycylvalylalanylglycylprolylglycylaspartylalanine
Synthetic peptide
Animal experiment
Article
Controlled study
Gene sequence
Human
Human cell
Immunization
Immunoelectron microscopy
Lung alveolus epithelium
Monocyte
Mycobacterium tuberculosis
Nonhuman
Nucleotide sequence
Polymerase chain reaction
Priority journal
Rabbit
Amino acid sequence
Animals
Bacterial proteins
Cell line
Humans
Membrane proteins
Molecular sequence data
Mycobacterium tuberculosis
Peptides
Rabbits
Tuberculosis vaccines
Mycobacterium tuberculosis
Oryctolagus cuniculus
High activity binding peptide (habp)
Mycobacterium tuberculosis-host cell interaction
Rv2969c
immunoelectron
bacterial
bacterial
Antibodies
Genes
Microscopy
title_short Functional characterization of Mycobacterium tuberculosis Rv2969c membrane protein
title_full Functional characterization of Mycobacterium tuberculosis Rv2969c membrane protein
title_fullStr Functional characterization of Mycobacterium tuberculosis Rv2969c membrane protein
title_full_unstemmed Functional characterization of Mycobacterium tuberculosis Rv2969c membrane protein
title_sort Functional characterization of Mycobacterium tuberculosis Rv2969c membrane protein
dc.subject.keyword.spa.fl_str_mv Antibody
Isoleucyllysylglutamylisoleucylvalylglycylaspartylvalylprolyl glycylisoleucylaspartylserylalanylalanylalanylthreonylalanyl threonylseryltyrosine
Membrane protein
Peptide
Phenylalanyltyrosylisoleucylvalylthreonylserylarginylaspartyl aspartyllysyllysylaspartylglycylvalylalanylglycylprolylglycylaspartylalanine
Synthetic peptide
Animal experiment
Article
Controlled study
Gene sequence
Human
Human cell
Immunization
Immunoelectron microscopy
Lung alveolus epithelium
Monocyte
Mycobacterium tuberculosis
Nonhuman
Nucleotide sequence
Polymerase chain reaction
Priority journal
Rabbit
Amino acid sequence
Animals
Bacterial proteins
Cell line
Humans
Membrane proteins
Molecular sequence data
Mycobacterium tuberculosis
Peptides
Rabbits
Tuberculosis vaccines
Mycobacterium tuberculosis
Oryctolagus cuniculus
High activity binding peptide (habp)
Mycobacterium tuberculosis-host cell interaction
Rv2969c
topic Antibody
Isoleucyllysylglutamylisoleucylvalylglycylaspartylvalylprolyl glycylisoleucylaspartylserylalanylalanylalanylthreonylalanyl threonylseryltyrosine
Membrane protein
Peptide
Phenylalanyltyrosylisoleucylvalylthreonylserylarginylaspartyl aspartyllysyllysylaspartylglycylvalylalanylglycylprolylglycylaspartylalanine
Synthetic peptide
Animal experiment
Article
Controlled study
Gene sequence
Human
Human cell
Immunization
Immunoelectron microscopy
Lung alveolus epithelium
Monocyte
Mycobacterium tuberculosis
Nonhuman
Nucleotide sequence
Polymerase chain reaction
Priority journal
Rabbit
Amino acid sequence
Animals
Bacterial proteins
Cell line
Humans
Membrane proteins
Molecular sequence data
Mycobacterium tuberculosis
Peptides
Rabbits
Tuberculosis vaccines
Mycobacterium tuberculosis
Oryctolagus cuniculus
High activity binding peptide (habp)
Mycobacterium tuberculosis-host cell interaction
Rv2969c
immunoelectron
bacterial
bacterial
Antibodies
Genes
Microscopy
dc.subject.keyword.eng.fl_str_mv immunoelectron
bacterial
bacterial
Antibodies
Genes
Microscopy
description Identifying Mycobacterium tuberculosis membrane proteins involved in binding to and invasion of host cells is important in designing subunit-based anti-tuberculosis vaccines. The Rv2969c gene sequence was identified by PCR in M. tuberculosis complex strains, being transcribed in M. tuberculosis H37Rv, M. tuberculosis H37Ra, and M. bovis BCG. Rabbits immunized with synthetic peptides from highly specific conserved regions of this protein produced antibodies recognizing 27 and 29 kDa bands in M. tuberculosis lysate, which is consistent with the molecular weight of the Rv2969c gene product in M. tuberculosis H37Rv. Immunoelectron microscopy revealed the protein was localized on the bacillus surface. Four and three specific high activity binding peptides (HABPs) to the A549 alveolar epithelial and U937 monocyte cell lines were found, respectively. Two of the HABPs found inhibited M. tuberculosis invasion of A549 cells, suggesting that these peptides might be good candidates to be included in a multiepitopic, subunit-based anti-tuberculosis vaccine. © 2008 Elsevier Inc. All rights reserved.
publishDate 2008
dc.date.created.spa.fl_str_mv 2008
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:02:28Z
dc.date.available.none.fl_str_mv 2020-05-26T00:02:28Z
dc.type.eng.fl_str_mv article
dc.type.coarversion.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_6501
dc.type.spa.spa.fl_str_mv Artículo
dc.identifier.doi.none.fl_str_mv https://doi.org/10.1016/j.bbrc.2008.05.157
dc.identifier.issn.none.fl_str_mv 0006291X
10902104
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/23489
url https://doi.org/10.1016/j.bbrc.2008.05.157
https://repository.urosario.edu.co/handle/10336/23489
identifier_str_mv 0006291X
10902104
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 940
dc.relation.citationIssue.none.fl_str_mv No. 4
dc.relation.citationStartPage.none.fl_str_mv 935
dc.relation.citationTitle.none.fl_str_mv Biochemical and Biophysical Research Communications
dc.relation.citationVolume.none.fl_str_mv Vol. 372
dc.relation.ispartof.spa.fl_str_mv Biochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.372, No.4 (2008); pp. 935-940
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-45449101647&doi=10.1016%2fj.bbrc.2008.05.157&partnerID=40&md5=046430185fb4c8a85c3c49efdd70b991
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