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...
- 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 |
_version_ |
1814167555076521984 |