Rv1268c protein peptide inhibiting Mycobacterium tuberculosis H37Rv entry to target cells

Marisol Ocampo, Deisy Carolina Rodríguez, Jorge Rodríguez, Maritza Bermúdez, Claudia Marina Muñoz, Manuel Alfonso Patarroyo, Manuel Elkin Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

5 Citas (Scopus)

Resumen

Tuberculosis (TB) remains one of the most worrying infectious diseases affecting public health around the world; 8.7 million new TB cases were reported in 2011. The search for an Mycobacterium tuberculosis H37Rv protein sequence which is functionally important in host-pathogen interaction has been proposed for developing a new vaccine which will allow efficient and safe control of the spread of this disease. The present study thus reports the results obtained for the Rv1268c protein described in the M. tuberculosis H37Rv genome as a hypothetical unknown, probably secreted, protein based on a highly robust, specific, sensitive and functional approach to the search for potential epitopes to be included in an anti-tuberculosis vaccine. Rv1268c presence was determined by immunoblotting after obtaining polyclonal sera against mycobacterial total sonicate or subcellular fractions. Such sera were used in electron immunomicroscopy (EIM) for confirming protein localisation on the M. tuberculosis envelop by recognising colloidal gold-labelled immunoglobulin. Screening assays revealed the presence of two sequences having high binding activity: one binding A549 alveolar epithelial cells ( 141TGMAALEQYLGSGHAVIVSI160) and other binding U937 monocyte-derived macrophages (21AVALGLASPADAAAGTMYGD40). Such sequences' ability to inhibit mycobacterial entry during in vitro assays was analysed. The structure of synthetic peptides binding to target cells was also determined, bearing in mind the structure-function relationship. These results, together with those obtained for other proteins, have been involved in selecting peptides which might be included in a subunit-based anti-tuberculosis vaccine. © 2013 Elsevier Ltd. All rights reserved.
Idioma originalEnglish (US)
Páginas (desde-hasta)6650-6656
Número de páginas7
PublicaciónBioorganic and Medicinal Chemistry
DOI
EstadoPublished - nov 1 2013

Huella dactilar

Mycobacterium tuberculosis
Tuberculosis Vaccines
Peptides
Assays
Tuberculosis
Proteins
Alveolar Epithelial Cells
Host-Pathogen Interactions
Gold Colloid
Subcellular Fractions
Macrophages
Public health
Pathogens
Serum
Immunoblotting
Communicable Diseases
Immunoglobulins
Epitopes
Screening
Vaccines

Citar esto

Ocampo, Marisol ; Rodríguez, Deisy Carolina ; Rodríguez, Jorge ; Bermúdez, Maritza ; Muñoz, Claudia Marina ; Patarroyo, Manuel Alfonso ; Patarroyo, Manuel Elkin. / Rv1268c protein peptide inhibiting Mycobacterium tuberculosis H37Rv entry to target cells. En: Bioorganic and Medicinal Chemistry. 2013 ; pp. 6650-6656.
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title = "Rv1268c protein peptide inhibiting Mycobacterium tuberculosis H37Rv entry to target cells",
abstract = "Tuberculosis (TB) remains one of the most worrying infectious diseases affecting public health around the world; 8.7 million new TB cases were reported in 2011. The search for an Mycobacterium tuberculosis H37Rv protein sequence which is functionally important in host-pathogen interaction has been proposed for developing a new vaccine which will allow efficient and safe control of the spread of this disease. The present study thus reports the results obtained for the Rv1268c protein described in the M. tuberculosis H37Rv genome as a hypothetical unknown, probably secreted, protein based on a highly robust, specific, sensitive and functional approach to the search for potential epitopes to be included in an anti-tuberculosis vaccine. Rv1268c presence was determined by immunoblotting after obtaining polyclonal sera against mycobacterial total sonicate or subcellular fractions. Such sera were used in electron immunomicroscopy (EIM) for confirming protein localisation on the M. tuberculosis envelop by recognising colloidal gold-labelled immunoglobulin. Screening assays revealed the presence of two sequences having high binding activity: one binding A549 alveolar epithelial cells ( 141TGMAALEQYLGSGHAVIVSI160) and other binding U937 monocyte-derived macrophages (21AVALGLASPADAAAGTMYGD40). Such sequences' ability to inhibit mycobacterial entry during in vitro assays was analysed. The structure of synthetic peptides binding to target cells was also determined, bearing in mind the structure-function relationship. These results, together with those obtained for other proteins, have been involved in selecting peptides which might be included in a subunit-based anti-tuberculosis vaccine. {\circledC} 2013 Elsevier Ltd. All rights reserved.",
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Rv1268c protein peptide inhibiting Mycobacterium tuberculosis H37Rv entry to target cells. / Ocampo, Marisol; Rodríguez, Deisy Carolina; Rodríguez, Jorge; Bermúdez, Maritza; Muñoz, Claudia Marina; Patarroyo, Manuel Alfonso; Patarroyo, Manuel Elkin.

En: Bioorganic and Medicinal Chemistry, 01.11.2013, p. 6650-6656.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - Rv1268c protein peptide inhibiting Mycobacterium tuberculosis H37Rv entry to target cells

AU - Ocampo, Marisol

AU - Rodríguez, Deisy Carolina

AU - Rodríguez, Jorge

AU - Bermúdez, Maritza

AU - Muñoz, Claudia Marina

AU - Patarroyo, Manuel Alfonso

AU - Patarroyo, Manuel Elkin

PY - 2013/11/1

Y1 - 2013/11/1

N2 - Tuberculosis (TB) remains one of the most worrying infectious diseases affecting public health around the world; 8.7 million new TB cases were reported in 2011. The search for an Mycobacterium tuberculosis H37Rv protein sequence which is functionally important in host-pathogen interaction has been proposed for developing a new vaccine which will allow efficient and safe control of the spread of this disease. The present study thus reports the results obtained for the Rv1268c protein described in the M. tuberculosis H37Rv genome as a hypothetical unknown, probably secreted, protein based on a highly robust, specific, sensitive and functional approach to the search for potential epitopes to be included in an anti-tuberculosis vaccine. Rv1268c presence was determined by immunoblotting after obtaining polyclonal sera against mycobacterial total sonicate or subcellular fractions. Such sera were used in electron immunomicroscopy (EIM) for confirming protein localisation on the M. tuberculosis envelop by recognising colloidal gold-labelled immunoglobulin. Screening assays revealed the presence of two sequences having high binding activity: one binding A549 alveolar epithelial cells ( 141TGMAALEQYLGSGHAVIVSI160) and other binding U937 monocyte-derived macrophages (21AVALGLASPADAAAGTMYGD40). Such sequences' ability to inhibit mycobacterial entry during in vitro assays was analysed. The structure of synthetic peptides binding to target cells was also determined, bearing in mind the structure-function relationship. These results, together with those obtained for other proteins, have been involved in selecting peptides which might be included in a subunit-based anti-tuberculosis vaccine. © 2013 Elsevier Ltd. All rights reserved.

AB - Tuberculosis (TB) remains one of the most worrying infectious diseases affecting public health around the world; 8.7 million new TB cases were reported in 2011. The search for an Mycobacterium tuberculosis H37Rv protein sequence which is functionally important in host-pathogen interaction has been proposed for developing a new vaccine which will allow efficient and safe control of the spread of this disease. The present study thus reports the results obtained for the Rv1268c protein described in the M. tuberculosis H37Rv genome as a hypothetical unknown, probably secreted, protein based on a highly robust, specific, sensitive and functional approach to the search for potential epitopes to be included in an anti-tuberculosis vaccine. Rv1268c presence was determined by immunoblotting after obtaining polyclonal sera against mycobacterial total sonicate or subcellular fractions. Such sera were used in electron immunomicroscopy (EIM) for confirming protein localisation on the M. tuberculosis envelop by recognising colloidal gold-labelled immunoglobulin. Screening assays revealed the presence of two sequences having high binding activity: one binding A549 alveolar epithelial cells ( 141TGMAALEQYLGSGHAVIVSI160) and other binding U937 monocyte-derived macrophages (21AVALGLASPADAAAGTMYGD40). Such sequences' ability to inhibit mycobacterial entry during in vitro assays was analysed. The structure of synthetic peptides binding to target cells was also determined, bearing in mind the structure-function relationship. These results, together with those obtained for other proteins, have been involved in selecting peptides which might be included in a subunit-based anti-tuberculosis vaccine. © 2013 Elsevier Ltd. All rights reserved.

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DO - 10.1016/j.bmc.2013.08.018

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JO - Bioorganic and Medicinal Chemistry

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SN - 0968-0896

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