Peptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophages
The specific function of putative cut2 protein (or CFP25), encoded by the Rv2301 gene from Mycobacterium tuberculosis H37Rv, has not been identified yet. The aim of this study was to assess some of CFP25 characteristics and its possible biological role in Mycobacterium tuberculosis H37Rv invasion pr...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2012
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/24240
- Acceso en línea:
- https://doi.org/10.1007/s00726-011-0938-7
https://repository.urosario.edu.co/handle/10336/24240
- Palabra clave:
- Bacterial protein
Culture filtrate protein 25
Cytochalasin d
Rv2301 protein
Unclassified drug
Amino acid sequence
Article
Bacterial strain
Binding affinity
Cell invasion
Cell surface
Controlled study
Dissociation constant
Human
Human cell
Immunoelectron microscopy
Internalization
Lung alveolus epithelium
Macrophage
Mycobacterium tuberculosis
Nonhuman
Nucleotide sequence
Priority journal
Protein binding
Western blotting
Amino acid sequence
Bacterial proteins
Binding sites
Cytochalasins
Epithelial cells
Humans
Kinetics
Macrophages
Molecular sequence data
Mycobacterium tuberculosis
Organ specificity
Peptides
Protein binding
Bacilli (class)
Capra hircus
Mycobacterium tuberculosis
Cutinase
High activity binding peptides
Mycobacterium tuberculosis
Rv2301
pulmonary
tumor
western
bacterial
immunoelectron
Antigens
Blotting
Cell line
Microscopy
Tuberculosis
- Rights
- License
- Abierto (Texto Completo)
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dc.title.spa.fl_str_mv |
Peptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophages |
title |
Peptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophages |
spellingShingle |
Peptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophages Bacterial protein Culture filtrate protein 25 Cytochalasin d Rv2301 protein Unclassified drug Amino acid sequence Article Bacterial strain Binding affinity Cell invasion Cell surface Controlled study Dissociation constant Human Human cell Immunoelectron microscopy Internalization Lung alveolus epithelium Macrophage Mycobacterium tuberculosis Nonhuman Nucleotide sequence Priority journal Protein binding Western blotting Amino acid sequence Bacterial proteins Binding sites Cytochalasins Epithelial cells Humans Kinetics Macrophages Molecular sequence data Mycobacterium tuberculosis Organ specificity Peptides Protein binding Bacilli (class) Capra hircus Mycobacterium tuberculosis Cutinase High activity binding peptides Mycobacterium tuberculosis Rv2301 pulmonary tumor western bacterial immunoelectron Antigens Blotting Cell line Microscopy Tuberculosis |
title_short |
Peptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophages |
title_full |
Peptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophages |
title_fullStr |
Peptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophages |
title_full_unstemmed |
Peptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophages |
title_sort |
Peptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophages |
dc.subject.keyword.spa.fl_str_mv |
Bacterial protein Culture filtrate protein 25 Cytochalasin d Rv2301 protein Unclassified drug Amino acid sequence Article Bacterial strain Binding affinity Cell invasion Cell surface Controlled study Dissociation constant Human Human cell Immunoelectron microscopy Internalization Lung alveolus epithelium Macrophage Mycobacterium tuberculosis Nonhuman Nucleotide sequence Priority journal Protein binding Western blotting Amino acid sequence Bacterial proteins Binding sites Cytochalasins Epithelial cells Humans Kinetics Macrophages Molecular sequence data Mycobacterium tuberculosis Organ specificity Peptides Protein binding Bacilli (class) Capra hircus Mycobacterium tuberculosis Cutinase High activity binding peptides Mycobacterium tuberculosis Rv2301 |
topic |
Bacterial protein Culture filtrate protein 25 Cytochalasin d Rv2301 protein Unclassified drug Amino acid sequence Article Bacterial strain Binding affinity Cell invasion Cell surface Controlled study Dissociation constant Human Human cell Immunoelectron microscopy Internalization Lung alveolus epithelium Macrophage Mycobacterium tuberculosis Nonhuman Nucleotide sequence Priority journal Protein binding Western blotting Amino acid sequence Bacterial proteins Binding sites Cytochalasins Epithelial cells Humans Kinetics Macrophages Molecular sequence data Mycobacterium tuberculosis Organ specificity Peptides Protein binding Bacilli (class) Capra hircus Mycobacterium tuberculosis Cutinase High activity binding peptides Mycobacterium tuberculosis Rv2301 pulmonary tumor western bacterial immunoelectron Antigens Blotting Cell line Microscopy Tuberculosis |
dc.subject.keyword.eng.fl_str_mv |
pulmonary tumor western bacterial immunoelectron Antigens Blotting Cell line Microscopy Tuberculosis |
description |
The specific function of putative cut2 protein (or CFP25), encoded by the Rv2301 gene from Mycobacterium tuberculosis H37Rv, has not been identified yet. The aim of this study was to assess some of CFP25 characteristics and its possible biological role in Mycobacterium tuberculosis H37Rv invasion process to target cells. Molecular assays indicated that the gene encoding Rv2301 is present and transcribed in M. tuberculosis complex strains. The presence of Rv2301 protein over the bacilli surface was confirmed by Western blot and immunoelectron microscopy analyses, using goats sera inoculated with synthetic peptides derived from Rv2301 protein. Receptor-ligand binding assays with carcinomic human alveolar basal epithelial cells (A549) and macrophages derived from human histolytic lymphoma monocytes (U937) allowed us to identify five high activity binding peptides (HABPs) in both cell lines, and two additional HABPs only in A549 cells. U937 HABPs binding interactions were characterized by saturation assays, finding dissociation constants (K d) within the nanomolar range and positive cooperativity (n H and gt; 1). Inhibition assays were performed to assess the possible biological role of Rv2301 identified HABPs, finding that some of them were able to inhibit invasion at a 5 ?M concentration, compared with the cytochalasin control. On the other hand, HABPs, and especially HABP 36507 located at the N-terminus of the protein, facilitated the internalization of fluorescent latex beads into A549 cells. These findings are of vital importance for the rational selection of Rv2301 HABPs, to be included as components of an antituberculosis vaccine. © 2011 Springer-Verlag. |
publishDate |
2012 |
dc.date.created.spa.fl_str_mv |
2012 |
dc.date.accessioned.none.fl_str_mv |
2020-05-26T00:10:36Z |
dc.date.available.none.fl_str_mv |
2020-05-26T00:10:36Z |
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/10.1007/s00726-011-0938-7 |
dc.identifier.issn.none.fl_str_mv |
09394451 14382199 |
dc.identifier.uri.none.fl_str_mv |
https://repository.urosario.edu.co/handle/10336/24240 |
url |
https://doi.org/10.1007/s00726-011-0938-7 https://repository.urosario.edu.co/handle/10336/24240 |
identifier_str_mv |
09394451 14382199 |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.citationEndPage.none.fl_str_mv |
2077 |
dc.relation.citationIssue.none.fl_str_mv |
No. 6 |
dc.relation.citationStartPage.none.fl_str_mv |
2067 |
dc.relation.citationTitle.none.fl_str_mv |
Amino Acids |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 42 |
dc.relation.ispartof.spa.fl_str_mv |
Amino Acids, ISSN:09394451, 14382199, Vol.42, No.6 (2012); pp. 2067-2077 |
dc.relation.uri.spa.fl_str_mv |
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Abierto (Texto Completo) |
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Abierto (Texto Completo) http://purl.org/coar/access_right/c_abf2 |
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reponame:Repositorio Institucional EdocUR |
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29ed545e-1ec1-4586-800c-4a2758cab090-10b670e21-0f97-46af-9182-9a5721f6841d-1b3a27b76-e6bc-42b1-af99-a3b609b32d7d-1887df23c-d081-4aaf-9f1a-cc1a49c80bbd-19fc64f6d-a903-48f1-ac2e-4e55fd2ed9af-176e03223-040d-4e46-864f-3bdecc8d2790-12020-05-26T00:10:36Z2020-05-26T00:10:36Z2012The specific function of putative cut2 protein (or CFP25), encoded by the Rv2301 gene from Mycobacterium tuberculosis H37Rv, has not been identified yet. The aim of this study was to assess some of CFP25 characteristics and its possible biological role in Mycobacterium tuberculosis H37Rv invasion process to target cells. Molecular assays indicated that the gene encoding Rv2301 is present and transcribed in M. tuberculosis complex strains. The presence of Rv2301 protein over the bacilli surface was confirmed by Western blot and immunoelectron microscopy analyses, using goats sera inoculated with synthetic peptides derived from Rv2301 protein. Receptor-ligand binding assays with carcinomic human alveolar basal epithelial cells (A549) and macrophages derived from human histolytic lymphoma monocytes (U937) allowed us to identify five high activity binding peptides (HABPs) in both cell lines, and two additional HABPs only in A549 cells. U937 HABPs binding interactions were characterized by saturation assays, finding dissociation constants (K d) within the nanomolar range and positive cooperativity (n H and gt; 1). Inhibition assays were performed to assess the possible biological role of Rv2301 identified HABPs, finding that some of them were able to inhibit invasion at a 5 ?M concentration, compared with the cytochalasin control. On the other hand, HABPs, and especially HABP 36507 located at the N-terminus of the protein, facilitated the internalization of fluorescent latex beads into A549 cells. These findings are of vital importance for the rational selection of Rv2301 HABPs, to be included as components of an antituberculosis vaccine. © 2011 Springer-Verlag.application/pdfhttps://doi.org/10.1007/s00726-011-0938-70939445114382199https://repository.urosario.edu.co/handle/10336/24240eng2077No. 62067Amino AcidsVol. 42Amino Acids, ISSN:09394451, 14382199, Vol.42, No.6 (2012); pp. 2067-2077https://www.scopus.com/inward/record.uri?eid=2-s2.0-84862760198&doi=10.1007%2fs00726-011-0938-7&partnerID=40&md5=1dc0bf118b60768ae8db7b1b8d2d3886Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURBacterial proteinCulture filtrate protein 25Cytochalasin dRv2301 proteinUnclassified drugAmino acid sequenceArticleBacterial strainBinding affinityCell invasionCell surfaceControlled studyDissociation constantHumanHuman cellImmunoelectron microscopyInternalizationLung alveolus epitheliumMacrophageMycobacterium tuberculosisNonhumanNucleotide sequencePriority journalProtein bindingWestern blottingAmino acid sequenceBacterial proteinsBinding sitesCytochalasinsEpithelial cellsHumansKineticsMacrophagesMolecular sequence dataMycobacterium tuberculosisOrgan specificityPeptidesProtein bindingBacilli (class)Capra hircusMycobacterium tuberculosisCutinaseHigh activity binding peptidesMycobacterium tuberculosisRv2301pulmonarytumorwesternbacterialimmunoelectronAntigensBlottingCell lineMicroscopyTuberculosisPeptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophagesarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Ocampo, M.Rodríguez, D. M.Curtidor, H.Vanegas, M.Patarroyo, M. A.Patarroyo, M. E.ORIGINALPeptides_derived_from_Mycobacterium_tube.pdfapplication/pdf725804https://repository.urosario.edu.co/bitstreams/16810c6a-5ad9-419e-88eb-c392fa42ef37/download6b61bf872cab524f08b92479e692bb9dMD51TEXTPeptides_derived_from_Mycobacterium_tube.pdf.txtPeptides_derived_from_Mycobacterium_tube.pdf.txtExtracted texttext/plain45651https://repository.urosario.edu.co/bitstreams/b0f98978-441c-4730-bacc-7e07a56a926d/downloadb072c117c9632bf60e94c9b2397aa99aMD52THUMBNAILPeptides_derived_from_Mycobacterium_tube.pdf.jpgPeptides_derived_from_Mycobacterium_tube.pdf.jpgGenerated Thumbnailimage/jpeg4777https://repository.urosario.edu.co/bitstreams/e52f83a3-6795-412e-a5da-f583ff3f2e31/downloadb6a1c7cc1f7a5c07d6a69f954fbea7d4MD5310336/24240oai:repository.urosario.edu.co:10336/242402022-05-02 07:37:14.940482https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |