Monosaccharides modulate HCV E2 protein-derived peptide biological properties

Adriana Janneth Bermudez Quintero, Javier E García, Ricardo Fierro, Alvaro Puentes, Jimena Cortés, Gladys Cifuentes, Magnolia Vanegas Murcia, Manuel Elkin Patarroyo

Resultado de la investigación: Contribución a una revistaArtículo

2 Citas (Scopus)

Resumen

A hepatitis C virus E(2) protein-derived sequence was selected for studying the effect of N-glycosylation on the peptide chain's conformational structure. The results suggested that the (534)TDVF(537) motif contained in peptide 33402 ((529)WGENDTDVFVLNNTRY(544)) had a type III beta-turn, relevant in antigen recognition of polyclonal antibodies, binding to human cells, and binding to HLA DRB1 *0401 molecules. N-Glycopeptides derived from this sequence contained monosaccharides in Asn(532). N-Glycopeptides presented differences in peptide chain structure compared to non-glycosylated peptides. Peptide 33402 specifically bound to human cells, specificity becoming lost when it was N-glycosylated. N-Glycosylation decreased antigen recognition of mouse polyclonal sera against this sequence. N-Glycopeptide binding to HLA DRB1 *0401 molecules was similar to that presented by non-glycosylated peptide, indicating that N-glycosylation did not affect binding to HLA DRB1 *0401 molecules. N-Glycosylation induced changes at structural and functional level which could be relevant for modulating human cell binding properties and antibody recognition
Idioma originalInglés estadounidense
Páginas (desde-hasta)409-418
Número de páginas10
PublicaciónBiochemical and Biophysical Research Communications
Volumen355
N.º2
DOI
EstadoPublicada - abr 6 2007

Huella dactilar

Monosaccharides
Glycosylation
Peptides
Glycopeptides
Proteins
Cells
Molecules
Antigens
Antibodies
Viruses
Hepacivirus
Serum
HLA-DRB1*04:01 antigen

Citar esto

Bermudez Quintero, A. J., García, J. E., Fierro, R., Puentes, A., Cortés, J., Cifuentes, G., ... Patarroyo, M. E. (2007). Monosaccharides modulate HCV E2 protein-derived peptide biological properties. Biochemical and Biophysical Research Communications, 355(2), 409-418. https://doi.org/10.1016/j.bbrc.2007.01.167
Bermudez Quintero, Adriana Janneth ; García, Javier E ; Fierro, Ricardo ; Puentes, Alvaro ; Cortés, Jimena ; Cifuentes, Gladys ; Vanegas Murcia, Magnolia ; Patarroyo, Manuel Elkin. / Monosaccharides modulate HCV E2 protein-derived peptide biological properties. En: Biochemical and Biophysical Research Communications. 2007 ; Vol. 355, N.º 2. pp. 409-418.
@article{bc0704cf65f2418391a1785155a13c7c,
title = "Monosaccharides modulate HCV E2 protein-derived peptide biological properties",
abstract = "A hepatitis C virus E(2) protein-derived sequence was selected for studying the effect of N-glycosylation on the peptide chain's conformational structure. The results suggested that the (534)TDVF(537) motif contained in peptide 33402 ((529)WGENDTDVFVLNNTRY(544)) had a type III beta-turn, relevant in antigen recognition of polyclonal antibodies, binding to human cells, and binding to HLA DRB1 *0401 molecules. N-Glycopeptides derived from this sequence contained monosaccharides in Asn(532). N-Glycopeptides presented differences in peptide chain structure compared to non-glycosylated peptides. Peptide 33402 specifically bound to human cells, specificity becoming lost when it was N-glycosylated. N-Glycosylation decreased antigen recognition of mouse polyclonal sera against this sequence. N-Glycopeptide binding to HLA DRB1 *0401 molecules was similar to that presented by non-glycosylated peptide, indicating that N-glycosylation did not affect binding to HLA DRB1 *0401 molecules. N-Glycosylation induced changes at structural and functional level which could be relevant for modulating human cell binding properties and antibody recognition",
author = "{Bermudez Quintero}, {Adriana Janneth} and Garc{\'i}a, {Javier E} and Ricardo Fierro and Alvaro Puentes and Jimena Cort{\'e}s and Gladys Cifuentes and {Vanegas Murcia}, Magnolia and Patarroyo, {Manuel Elkin}",
year = "2007",
month = "4",
day = "6",
doi = "10.1016/j.bbrc.2007.01.167",
language = "English (US)",
volume = "355",
pages = "409--418",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

Bermudez Quintero, AJ, García, JE, Fierro, R, Puentes, A, Cortés, J, Cifuentes, G, Vanegas Murcia, M & Patarroyo, ME 2007, 'Monosaccharides modulate HCV E2 protein-derived peptide biological properties', Biochemical and Biophysical Research Communications, vol. 355, n.º 2, pp. 409-418. https://doi.org/10.1016/j.bbrc.2007.01.167

Monosaccharides modulate HCV E2 protein-derived peptide biological properties. / Bermudez Quintero, Adriana Janneth; García, Javier E; Fierro, Ricardo; Puentes, Alvaro; Cortés, Jimena; Cifuentes, Gladys; Vanegas Murcia, Magnolia; Patarroyo, Manuel Elkin.

En: Biochemical and Biophysical Research Communications, Vol. 355, N.º 2, 06.04.2007, p. 409-418.

Resultado de la investigación: Contribución a una revistaArtículo

TY - JOUR

T1 - Monosaccharides modulate HCV E2 protein-derived peptide biological properties

AU - Bermudez Quintero, Adriana Janneth

AU - García, Javier E

AU - Fierro, Ricardo

AU - Puentes, Alvaro

AU - Cortés, Jimena

AU - Cifuentes, Gladys

AU - Vanegas Murcia, Magnolia

AU - Patarroyo, Manuel Elkin

PY - 2007/4/6

Y1 - 2007/4/6

N2 - A hepatitis C virus E(2) protein-derived sequence was selected for studying the effect of N-glycosylation on the peptide chain's conformational structure. The results suggested that the (534)TDVF(537) motif contained in peptide 33402 ((529)WGENDTDVFVLNNTRY(544)) had a type III beta-turn, relevant in antigen recognition of polyclonal antibodies, binding to human cells, and binding to HLA DRB1 *0401 molecules. N-Glycopeptides derived from this sequence contained monosaccharides in Asn(532). N-Glycopeptides presented differences in peptide chain structure compared to non-glycosylated peptides. Peptide 33402 specifically bound to human cells, specificity becoming lost when it was N-glycosylated. N-Glycosylation decreased antigen recognition of mouse polyclonal sera against this sequence. N-Glycopeptide binding to HLA DRB1 *0401 molecules was similar to that presented by non-glycosylated peptide, indicating that N-glycosylation did not affect binding to HLA DRB1 *0401 molecules. N-Glycosylation induced changes at structural and functional level which could be relevant for modulating human cell binding properties and antibody recognition

AB - A hepatitis C virus E(2) protein-derived sequence was selected for studying the effect of N-glycosylation on the peptide chain's conformational structure. The results suggested that the (534)TDVF(537) motif contained in peptide 33402 ((529)WGENDTDVFVLNNTRY(544)) had a type III beta-turn, relevant in antigen recognition of polyclonal antibodies, binding to human cells, and binding to HLA DRB1 *0401 molecules. N-Glycopeptides derived from this sequence contained monosaccharides in Asn(532). N-Glycopeptides presented differences in peptide chain structure compared to non-glycosylated peptides. Peptide 33402 specifically bound to human cells, specificity becoming lost when it was N-glycosylated. N-Glycosylation decreased antigen recognition of mouse polyclonal sera against this sequence. N-Glycopeptide binding to HLA DRB1 *0401 molecules was similar to that presented by non-glycosylated peptide, indicating that N-glycosylation did not affect binding to HLA DRB1 *0401 molecules. N-Glycosylation induced changes at structural and functional level which could be relevant for modulating human cell binding properties and antibody recognition

UR - http://www.sciencedirect.com/science/article/pii/S0006291X07002422?via%3Dihub

U2 - 10.1016/j.bbrc.2007.01.167

DO - 10.1016/j.bbrc.2007.01.167

M3 - Article

VL - 355

SP - 409

EP - 418

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -

Bermudez Quintero AJ, García JE, Fierro R, Puentes A, Cortés J, Cifuentes G y otros. Monosaccharides modulate HCV E2 protein-derived peptide biological properties. Biochemical and Biophysical Research Communications. 2007 abr 6;355(2):409-418. https://doi.org/10.1016/j.bbrc.2007.01.167