Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines
The Rv2707 gene encoding a putative alanine- and leucine-rich protein was found to be present in all Mycobacterium tuberculosis complex strains (by PCR) and its transcription was shown by RT-PCR in all but M. bovis and M. microti. Antibodies raised against Rv2707 peptides specifically recognized the...
- 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:10336/22893
- Acceso en línea:
- https://doi.org/10.1110/ps.073083308
https://repository.urosario.edu.co/handle/10336/22893
- Palabra clave:
- Bacterial protein
Protein rv2707
Unclassified drug
Amino acid sequence
Article
Controlled study
Gene location
Gene sequence
Human
Human cell
Mycobacterium tuberculosis
Nonhuman
Priority journal
Reverse transcription polymerase chain reaction
Amino acid sequence
Bacterial proteins
Computational biology
Humans
Molecular sequence data
Mycobacterium tuberculosis
Peptide fragments
Protein binding
U937 cells
Mycobacterium tuberculosis
Mycobacterium tuberculosis complex
A549 cell
High activity binding peptide (habp)
Invasion
Mycobacterium tuberculosis
Rv2707
U937 cell
tumor
immunoelectron
Cell line
Microscopy
- Rights
- License
- Abierto (Texto Completo)
Summary: | The Rv2707 gene encoding a putative alanine- and leucine-rich protein was found to be present in all Mycobacterium tuberculosis complex strains (by PCR) and its transcription was shown by RT-PCR in all but M. bovis and M. microti. Antibodies raised against Rv2707 peptides specifically recognized the native protein by Western blot and were able to locate this protein on the M. tuberculosis membrane by immunoelectron microscopy. A549 and U937 cells lines were used in binding assays involving synthetic peptides covering the whole Rv2707 protein. High A549 cell-binding peptide 16083 ( 281QEEWPAPATHAHRLGNWLKAY300) was identified. Peptides 16072 (61LFGPDTLPAIEKSALSTAHSY80) and 16084 ( 301RIGVGTTTYSSTAQHSAVAA320) presented high specific binding to both A549 and U937 cells. Cross-linking assays revealed that peptide 16084 specifically bound to a 40-kDa and a 50-kDa U937 cell membrane protein. High activity binding peptides (HABPs) 16083 and 16084 were able to inhibit M. tuberculosis invasion of A549 cells. Our results suggest that these sequences could be part of the binding sites used by the bacillus for interacting with target cells, and thus represent good candidates to be tested in a future subunit-based, multiepitope, antituberculosis vaccine. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society. |
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