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Mycobacterium tuberculosis H37Rv LpqG Protein Peptides Can Inhibit Mycobacterial Entry through Specific Interactions

is the causative agent of tuberculosis, a disease causing major mortality worldwide. As part of a systematic methodology for studying surface proteins which might be involved in host-pathogen interactions, our group found that LpqG surface protein (Rv3623) found in complex strains was located on the...

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Bibliographic Details
Published in:Molecules (Basel, Switzerland) Switzerland), 2018-02, Vol.23 (3), p.526
Main Authors: Sánchez-Barinas, Christian David, Ocampo, Marisol, Vanegas, Magnolia, Castañeda-Ramirez, Jeimmy Johana, Patarroyo, Manuel Alfonso, Patarroyo, Manuel Elkin
Format: Article
Language:English
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Summary:is the causative agent of tuberculosis, a disease causing major mortality worldwide. As part of a systematic methodology for studying surface proteins which might be involved in host-pathogen interactions, our group found that LpqG surface protein (Rv3623) found in complex strains was located on the mycobacterial envelope and that peptide 16661 ( SGCDSHNSGSLGADPRQVTVY ) had high specific binding to U937 monocyte-derived macrophages and inhibited mycobacterial entry to such cells in a concentration-dependent way. A region having high specific binding to A549 alveolar epithelial cells was found which had low mycobacterial entry inhibition. As suggested in previous studies, relevant sequences in the host-pathogen interaction do not induce an immune response and peptides characterised as HABPs are poorly recognised by sera from individuals regardless of whether they have been in contact with . Our approach to designing a synthetic, multi-epitope anti-tuberculosis vaccine has been based on identifying sequences involved in different proteins' mycobacteria-target cell interaction and modifying their sequence to improve their immunogenic characteristics, meaning that peptide 16661 sequence should be considered in such design.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules23030526