Mce4F Mycobacterium tuberculosis protein peptides can inhibit invasion of human cell lines
| Autor: | Manuel A. Patarroyo, Hernando Curtidor, Marisol Ocampo, Manuel E. Patarroyo, Deisy Carolina Rodriguez, Yahson Varela |
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| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Unclassified drug
Protein Conformation Macrophage Physiology Habp Peptide Epithelial cells immunoelectron Epithelium cell Iodine 125 Biological product Bacterial protein Membrane proteins Rv3494c protein Beta sheet Immunology and Allergy Microscopy Immunoelectron Antiinfective agent Alpha helix Priority journal chemistry.chemical_classification Microscopy biology Circular Dichroism Mycobacterium tuberculosis h37rv General Medicine Endocytosis Anti-Bacterial Agents Cell invasion Infectious Diseases Protein conformation A-549 cell line Protein Binding Human Microbiology (medical) Immunoelectron microscopy Circular dichroism Bacterial antigen Microbiology Article Cell Line Mycobacterium tuberculosis Lung alveolus macrophage Mycobacterium tuberculosis antigens Antigen Inhibition and invasion assay Anti-bacterial agents Protein binding Humans Tuberculosis U-937 cell line bacterial Biological products Antigens A549 cell Antigens Bacterial Biological Products Drug effects General Immunology and Microbiology Mce4f protein Macrophages Membrane Proteins Epithelial Cells biology.organism_classification Nonhuman Molecular biology Bacterial virulence Metabolism chemistry Human cell Cell culture Membrane protein Protein expression Cytoplasm protein Cell line Controlled study Internalization |
| Zdroj: | Repositorio EdocUR-U. Rosario Universidad del Rosario instacron:Universidad del Rosario |
| Popis: | This work was aimed at studying the Mycobacterium tuberculosis H37Rv Rv3494c protein, taking into account that it belongs to the mammalian cell entry family (mce) which is thought to have important functions in the disease's pathogenesis. The protein was characterized in silico; its presence on mycobacterial surface was confirmed by immunoelectron microscopy. High-activity binding peptides (HABPs) were identified by binding assays with (125)I; their ability to inhibit mycobacterial entry to two cell lines (U937 alveolar macrophages and A549 epithelial cells) was ascertained and their role in bacterial entry was confirmed by fluorescent microsphere internalization assay. This protein's predicted alpha-helix structure was confirmed by circular dichroism of its peptides. All HABPs inhibited mycobacterial entry to cells and that the 38379 peptide ((201)IDQAGPFLQAQIRAGGDIKSY(220)) had high binding ability and inhibited the mycobacterial entry to both cell lines assayed here. Rv3494c peptides 38370 ((21)LSVMAIFYLRLPATFGIGTY(40)), 38373 ((81)HMRLNSGTAIPSNVTATVRSY(100)) and 38379 ((201)IDQAGPFLQAQIRAGGDIKSY(220)) showed to be HABP and inhibited mycobacterial entry to A549 cells and peptide 38382 ((261)RPSFPALAASLANLGRVGVIY(280)) bind to U937 and inhibited the mycobacterial entry to this cell line; all of these sequences play an important role in cell line recognition and invasion, and may thus be considered in the search for prophylactic candidates against tuberculosis. |
| Databáze: | OpenAIRE |
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