Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines

Julie A. Chapeton-Montes, David F. Plaza, Hernando Curtidor, Martha Forero, Magnolia Vanegas, Manuel E. Patarroyo, Manuel A. Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

12 Citas (Scopus)

Resumen

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.
Idioma originalEnglish (US)
Páginas (desde-hasta)342-351
Número de páginas10
PublicaciónProtein Science
DOI
EstadoPublished - feb 1 2008

Huella dactilar

Mycobacterium tuberculosis
Cells
Cell Line
U937 Cells
Peptides
Proteins
Assays
Polymerase Chain Reaction
Arvicolinae
Gene encoding
Immunoelectron Microscopy
Bacilli
Transcription
Ports and harbors
Leucine
Alanine
Bacillus
Microscopic examination
Membrane Proteins
Vaccines

Citar esto

Chapeton-Montes, Julie A. ; Plaza, David F. ; Curtidor, Hernando ; Forero, Martha ; Vanegas, Magnolia ; Patarroyo, Manuel E. ; Patarroyo, Manuel A. / Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines. En: Protein Science. 2008 ; pp. 342-351.
@article{5edfff6f6fa14414b7e0f7ee05863846,
title = "Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines",
abstract = "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 {\circledC} 2008 The Protein Society.",
author = "Chapeton-Montes, {Julie A.} and Plaza, {David F.} and Hernando Curtidor and Martha Forero and Magnolia Vanegas and Patarroyo, {Manuel E.} and Patarroyo, {Manuel A.}",
year = "2008",
month = "2",
day = "1",
doi = "10.1110/ps.073083308",
language = "English (US)",
pages = "342--351",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Cold Spring Harbor Laboratory Press",

}

Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines. / Chapeton-Montes, Julie A.; Plaza, David F.; Curtidor, Hernando; Forero, Martha; Vanegas, Magnolia; Patarroyo, Manuel E.; Patarroyo, Manuel A.

En: Protein Science, 01.02.2008, p. 342-351.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Characterizing the Mycobacterium tuberculosis Rv2707 protein and determining its sequences which specifically bind to two human cell lines

AU - Chapeton-Montes, Julie A.

AU - Plaza, David F.

AU - Curtidor, Hernando

AU - Forero, Martha

AU - Vanegas, Magnolia

AU - Patarroyo, Manuel E.

AU - Patarroyo, Manuel A.

PY - 2008/2/1

Y1 - 2008/2/1

N2 - 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.

AB - 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.

U2 - 10.1110/ps.073083308

DO - 10.1110/ps.073083308

M3 - Article

SP - 342

EP - 351

JO - Protein Science

JF - Protein Science

SN - 0961-8368

ER -