Mycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasion

PE/PPE proteins are involved in several processes during Mycobacterium tuberculosis (Mtb) infection of target cells; studying them is extremely interesting as they are the only ones from the Mycobacterium genus, they abound in pathogenic species such as Mtb and their function remains yet unknown. Th...

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Autores:
Tipo de recurso:
Fecha de publicación:
2016
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/24335
Acceso en línea:
https://doi.org/10.1016/j.ijbiomac.2015.12.081
https://repository.urosario.edu.co/handle/10336/24335
Palabra clave:
Bacterial protein
Pe9 protein
Unclassified drug
Bacterial protein
Peptide
Protein binding
Article
Bacterial strain
Cell invasion
Circular dichroism
Controlled study
Crystal structure
Mycobacterium tuberculosis
Nonhuman
Protein binding
Protein expression
Protein localization
Protein secondary structure
Protein targeting
Surface property
A-549 cell line
Amino acid sequence
Biology
Chemistry
Enzyme specificity
Epithelium cell
Genetic transcription
Genetics
Human
Macrophage
Metabolism
Microbiology
Molecular model
Mycobacterium tuberculosis
Physiology
Protein conformation
Protein transport
A549 cells
Amino acid sequence
Bacterial proteins
Computational biology
Epithelial cells
Humans
Macrophages
Mycobacterium tuberculosis
Peptides
Protein binding
Protein conformation
Protein transport
Substrate specificity
Pe9 protein
Synthetic peptide
Tuberculosis
molecular
genetic
Models
Transcription
Rights
License
Abierto (Texto Completo)
id EDOCUR2_36b64eb93c48de3d00d5c3456dc15666
oai_identifier_str oai:repository.urosario.edu.co:10336/24335
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 6923d587-d8a4-4ecc-ab12-ef2c94ef0fd9-129ed545e-1ec1-4586-800c-4a2758cab090-13ec909b1-d14b-4a5a-bbc4-61bd89d7ff48-165bfeebf-fb15-477e-8234-8055cf05e421-19fc64f6d-a903-48f1-ac2e-4e55fd2ed9af-1e7d32914-9338-43b3-9040-27ed6b08a4fb-176e03223-040d-4e46-864f-3bdecc8d2790-12020-05-26T00:11:49Z2020-05-26T00:11:49Z2016PE/PPE proteins are involved in several processes during Mycobacterium tuberculosis (Mtb) infection of target cells; studying them is extremely interesting as they are the only ones from the Mycobacterium genus, they abound in pathogenic species such as Mtb and their function remains yet unknown. The PE9 protein (Rv1088) was characterised, the rv1088 gene was identified by PCR in Mtb complex strains and its expression and localisation on mycobacterial surface was confirmed by Western blot and immunoelectron microscopy. Bioinformatics tools were used for predicting PE9 protein structural aspects and experimental study involved the circular dichroism of synthetic peptides. The peptides were tested in binding assays involving U937 and A549 cells; two high activity binding peptides (HABPs) were found for both cell lines (39226-1MSYMIATPAALTAAATDIDGI21 and 39232-125YQRHFGTGGQPEFRQHSEHRR144), one for U937 (39231-104YAGAGRRQRRRRSGDGQWRLRQ124) and one for A549 (39230-83YGTGVFRRRRGRQTVTAAEHRA103). HABP 39232 inhibited mycobacterial entry to A549 cells (~70%) and U937 cells (~50%), peptides 39226 and 39231 inhibited entry to U937 cells (~60% and 80%, respectively) and peptide 39230 inhibited entry to A549 cells (~60%). This emphasised HABPs' functional importance in recognition between Mtb H37Rv and target cell receptors. These peptide sequences could be involved in invasion and were recognised by the host's immune system, thereby highlighting their use when designing an efficient anti-tuberculosis multiantigenic vaccine. © 2016 Elsevier B.V.application/pdfhttps://doi.org/10.1016/j.ijbiomac.2015.12.0811418130https://repository.urosario.edu.co/handle/10336/24335engElsevier B.V.655646International Journal of Biological MacromoleculesVol. 86International Journal of Biological Macromolecules, ISSN:1418130, Vol.86,(2016); pp. 646-655https://www.scopus.com/inward/record.uri?eid=2-s2.0-84957990000&doi=10.1016%2fj.ijbiomac.2015.12.081&partnerID=40&md5=c32fb67debabb348643df423c116c4ecAbierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURBacterial proteinPe9 proteinUnclassified drugBacterial proteinPeptideProtein bindingArticleBacterial strainCell invasionCircular dichroismControlled studyCrystal structureMycobacterium tuberculosisNonhumanProtein bindingProtein expressionProtein localizationProtein secondary structureProtein targetingSurface propertyA-549 cell lineAmino acid sequenceBiologyChemistryEnzyme specificityEpithelium cellGenetic transcriptionGeneticsHumanMacrophageMetabolismMicrobiologyMolecular modelMycobacterium tuberculosisPhysiologyProtein conformationProtein transportA549 cellsAmino acid sequenceBacterial proteinsComputational biologyEpithelial cellsHumansMacrophagesMycobacterium tuberculosisPeptidesProtein bindingProtein conformationProtein transportSubstrate specificityPe9 proteinSynthetic peptideTuberculosismoleculargeneticModelsTranscriptionMycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasionarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Díaz D.P.Ocampo M.Pabón L.Herrera C.Patarroyo M.A.Munoz M.Patarroyo M.E.10336/24335oai:repository.urosario.edu.co:10336/243352022-05-02 07:37:14.955748https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Mycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasion
title Mycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasion
spellingShingle Mycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasion
Bacterial protein
Pe9 protein
Unclassified drug
Bacterial protein
Peptide
Protein binding
Article
Bacterial strain
Cell invasion
Circular dichroism
Controlled study
Crystal structure
Mycobacterium tuberculosis
Nonhuman
Protein binding
Protein expression
Protein localization
Protein secondary structure
Protein targeting
Surface property
A-549 cell line
Amino acid sequence
Biology
Chemistry
Enzyme specificity
Epithelium cell
Genetic transcription
Genetics
Human
Macrophage
Metabolism
Microbiology
Molecular model
Mycobacterium tuberculosis
Physiology
Protein conformation
Protein transport
A549 cells
Amino acid sequence
Bacterial proteins
Computational biology
Epithelial cells
Humans
Macrophages
Mycobacterium tuberculosis
Peptides
Protein binding
Protein conformation
Protein transport
Substrate specificity
Pe9 protein
Synthetic peptide
Tuberculosis
molecular
genetic
Models
Transcription
title_short Mycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasion
title_full Mycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasion
title_fullStr Mycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasion
title_full_unstemmed Mycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasion
title_sort Mycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasion
dc.subject.keyword.spa.fl_str_mv Bacterial protein
Pe9 protein
Unclassified drug
Bacterial protein
Peptide
Protein binding
Article
Bacterial strain
Cell invasion
Circular dichroism
Controlled study
Crystal structure
Mycobacterium tuberculosis
Nonhuman
Protein binding
Protein expression
Protein localization
Protein secondary structure
Protein targeting
Surface property
A-549 cell line
Amino acid sequence
Biology
Chemistry
Enzyme specificity
Epithelium cell
Genetic transcription
Genetics
Human
Macrophage
Metabolism
Microbiology
Molecular model
Mycobacterium tuberculosis
Physiology
Protein conformation
Protein transport
A549 cells
Amino acid sequence
Bacterial proteins
Computational biology
Epithelial cells
Humans
Macrophages
Mycobacterium tuberculosis
Peptides
Protein binding
Protein conformation
Protein transport
Substrate specificity
Pe9 protein
Synthetic peptide
Tuberculosis
topic Bacterial protein
Pe9 protein
Unclassified drug
Bacterial protein
Peptide
Protein binding
Article
Bacterial strain
Cell invasion
Circular dichroism
Controlled study
Crystal structure
Mycobacterium tuberculosis
Nonhuman
Protein binding
Protein expression
Protein localization
Protein secondary structure
Protein targeting
Surface property
A-549 cell line
Amino acid sequence
Biology
Chemistry
Enzyme specificity
Epithelium cell
Genetic transcription
Genetics
Human
Macrophage
Metabolism
Microbiology
Molecular model
Mycobacterium tuberculosis
Physiology
Protein conformation
Protein transport
A549 cells
Amino acid sequence
Bacterial proteins
Computational biology
Epithelial cells
Humans
Macrophages
Mycobacterium tuberculosis
Peptides
Protein binding
Protein conformation
Protein transport
Substrate specificity
Pe9 protein
Synthetic peptide
Tuberculosis
molecular
genetic
Models
Transcription
dc.subject.keyword.eng.fl_str_mv molecular
genetic
Models
Transcription
description PE/PPE proteins are involved in several processes during Mycobacterium tuberculosis (Mtb) infection of target cells; studying them is extremely interesting as they are the only ones from the Mycobacterium genus, they abound in pathogenic species such as Mtb and their function remains yet unknown. The PE9 protein (Rv1088) was characterised, the rv1088 gene was identified by PCR in Mtb complex strains and its expression and localisation on mycobacterial surface was confirmed by Western blot and immunoelectron microscopy. Bioinformatics tools were used for predicting PE9 protein structural aspects and experimental study involved the circular dichroism of synthetic peptides. The peptides were tested in binding assays involving U937 and A549 cells; two high activity binding peptides (HABPs) were found for both cell lines (39226-1MSYMIATPAALTAAATDIDGI21 and 39232-125YQRHFGTGGQPEFRQHSEHRR144), one for U937 (39231-104YAGAGRRQRRRRSGDGQWRLRQ124) and one for A549 (39230-83YGTGVFRRRRGRQTVTAAEHRA103). HABP 39232 inhibited mycobacterial entry to A549 cells (~70%) and U937 cells (~50%), peptides 39226 and 39231 inhibited entry to U937 cells (~60% and 80%, respectively) and peptide 39230 inhibited entry to A549 cells (~60%). This emphasised HABPs' functional importance in recognition between Mtb H37Rv and target cell receptors. These peptide sequences could be involved in invasion and were recognised by the host's immune system, thereby highlighting their use when designing an efficient anti-tuberculosis multiantigenic vaccine. © 2016 Elsevier B.V.
publishDate 2016
dc.date.created.spa.fl_str_mv 2016
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:11:49Z
dc.date.available.none.fl_str_mv 2020-05-26T00:11:49Z
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.ijbiomac.2015.12.081
dc.identifier.issn.none.fl_str_mv 1418130
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/24335
url https://doi.org/10.1016/j.ijbiomac.2015.12.081
https://repository.urosario.edu.co/handle/10336/24335
identifier_str_mv 1418130
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 655
dc.relation.citationStartPage.none.fl_str_mv 646
dc.relation.citationTitle.none.fl_str_mv International Journal of Biological Macromolecules
dc.relation.citationVolume.none.fl_str_mv Vol. 86
dc.relation.ispartof.spa.fl_str_mv International Journal of Biological Macromolecules, ISSN:1418130, Vol.86,(2016); pp. 646-655
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-84957990000&doi=10.1016%2fj.ijbiomac.2015.12.081&partnerID=40&md5=c32fb67debabb348643df423c116c4ec
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.acceso.spa.fl_str_mv Abierto (Texto Completo)
rights_invalid_str_mv Abierto (Texto Completo)
http://purl.org/coar/access_right/c_abf2
dc.format.mimetype.none.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Elsevier B.V.
institution Universidad del Rosario
dc.source.instname.spa.fl_str_mv instname:Universidad del Rosario
dc.source.reponame.spa.fl_str_mv reponame:Repositorio Institucional EdocUR
repository.name.fl_str_mv Repositorio institucional EdocUR
repository.mail.fl_str_mv edocur@urosario.edu.co
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