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  • Structure-Activity Relationship for the Development of a Self-Adjuvanting Mucosally Active Lipopeptide Vaccine against Streptococcus pyogenes

    Author(s)
    Zaman, Mehfuz
    Abdel-Aal, Abu-Baker M
    Fujita, Yoshio
    Ziora, Zyta M
    Batzloff, Michael R
    Good, Michael F
    Toth, Istvan
    Griffith University Author(s)
    Batzloff, Michael R.
    Good, Michael F.
    Year published
    2012
    Metadata
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    Abstract
    Infection with group A streptococcus (GAS) can result in a number of diseases, some of which are potentially life-threatening. The oral-nasal mucosa is a primary site of GAS infection, and a mucosally active vaccine candidate could form the basis of an antidisease and transmission-blocking GAS vaccine. In the present study, a peptide from the GAS M protein (J14) representing a B cell epitope was incorporated alongside a universal T cell helper epitope and a Toll-like receptor 2 targeting lipid moiety to form lipopeptide constructs. Through structure activity studies, we identified a vaccine candidate that induces J14-specific ...
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    Infection with group A streptococcus (GAS) can result in a number of diseases, some of which are potentially life-threatening. The oral-nasal mucosa is a primary site of GAS infection, and a mucosally active vaccine candidate could form the basis of an antidisease and transmission-blocking GAS vaccine. In the present study, a peptide from the GAS M protein (J14) representing a B cell epitope was incorporated alongside a universal T cell helper epitope and a Toll-like receptor 2 targeting lipid moiety to form lipopeptide constructs. Through structure activity studies, we identified a vaccine candidate that induces J14-specific mucosal and systemic antibody responses when administered intranasally without additional adjuvants. The systemic antibodies elicited were capable of inhibiting the growth of GAS. In addition, J14-specific mucosal antibodies corresponded with reduced throat colonization after respiratory GAS challenge. These preclinical experiments show that this lipopeptide could form the basis of an optimal needle-free mucosal GAS vaccine.
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    Journal Title
    Journal of Medicinal Chemistry
    Volume
    55
    Issue
    19
    DOI
    https://doi.org/10.1021/jm301074n
    Copyright Statement
    Self-archiving of the author-manuscript version is not yet supported by this journal. Please refer to the journal link for access to the definitive, published version or contact the authors for more information.
    Subject
    Medicinal and biomolecular chemistry
    Organic chemistry
    Bacteriology
    Pharmacology and pharmaceutical sciences
    Publication URI
    http://hdl.handle.net/10072/48798
    Collection
    • Journal articles

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