Functional characterization of Mycobacterium tuberculosis Rv2969c membrane protein
Autor: | Manuel A. Patarroyo, Manuel E. Patarroyo, Luis E. Rodriguez, Hernando Curtidor, David F. Plaza, Marisol Ocampo, Martha Forero |
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Rok vydání: | 2008 |
Předmět: |
Rv2969c
Rabbit immunoelectron Gene sequence Monocyte Oryctolagus cuniculus Biochemistry Bacterial proteins Membrane proteins Microscopy Immunoelectron Tuberculosis Vaccines Peptide sequence Phenylalanyltyrosylisoleucylvalylthreonylserylarginylaspartyl aspartyllysyllysylaspartylglycylvalylalanylglycylprolylglycylaspartylalanine Priority journal Microscopy biology Isoleucyllysylglutamylisoleucylvalylglycylaspartylvalylprolyl glycylisoleucylaspartylserylalanylalanylalanylthreonylalanyl threonylseryltyrosine Antibodies Bacterial Polymerase chain reaction Peptide Rabbits Tuberculosis vaccines Lung alveolus epithelium Human Tuberculosis Immunoelectron microscopy Protein subunit Molecular Sequence Data Biophysics Article Antibodies Cell Line Amino acid sequence Mycobacterium tuberculosis Gene product Bacterial Proteins Molecular sequence data medicine Animals Humans bacterial Amino Acid Sequence Animal experiment Molecular Biology Antibody Membrane Proteins Cell Biology Nonhuman biology.organism_classification medicine.disease Molecular biology Synthetic peptide Human cell Genes Membrane protein Genes Bacterial High activity binding peptide (habp) Immunization Cell line Peptides Mycobacterium tuberculosis-host cell interaction Controlled study Nucleotide sequence |
Zdroj: | Repositorio EdocUR-U. Rosario Universidad del Rosario instacron:Universidad del Rosario |
ISSN: | 0006-291X |
DOI: | 10.1016/j.bbrc.2008.05.157 |
Popis: | Identifying Mycobacterium tuberculosis membrane proteins involved in binding to and invasion of host cells is important in designing subunit-based anti-tuberculosis vaccines. The Rv2969c gene sequence was identified by PCR in M. tuberculosis complex strains, being transcribed in M. tuberculosis H37Rv, M. tuberculosis H37Ra, and M. bovis BCG. Rabbits immunized with synthetic peptides from highly specific conserved regions of this protein produced antibodies recognizing 27 and 29 kDa bands in M. tuberculosis lysate, which is consistent with the molecular weight of the Rv2969c gene product in M. tuberculosis H37Rv. Immunoelectron microscopy revealed the protein was localized on the bacillus surface. Four and three specific high activity binding peptides (HABPs) to the A549 alveolar epithelial and U937 monocyte cell lines were found, respectively. Two of the HABPs found inhibited M. tuberculosis invasion of A549 cells, suggesting that these peptides might be good candidates to be included in a multiepitopic, subunit-based anti-tuberculosis vaccine. © 2008 Elsevier Inc. All rights reserved. |
Databáze: | OpenAIRE |
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