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MUB40 Binds to Lactoferrin and Stands as a Specific Neutrophil Marker

Abstract : Neutrophils represent the most abundant immune cells recruited to inflamed tissues. A lack of dedicated tools has hampered their detection and study. We show that a synthesized peptide, MUB40, binds to lactoferrin, the most abundant protein stored in neutrophil-specific and tertiary granules. Lactoferrin is specifically produced by neutrophils among other leukocytes, making MUB40 a specific neutrophil marker. Naive mammalian neutrophils (human, guinea pig, mouse, rabbit) were labeled by fluorescent MUB40 conjugates (-Cy5, Dylight405). A peptidase-resistant retro-inverso MUB40 (RI-MUB40) was synthesized and its lactoferrin-binding property validated. Neutrophil lactoferrin secretion during in vitro Shigella infection was assessed with RI-MUB40-Cy5 using live cell microscopy. Systemically administered RI-MUB40-Cy5 accumulated at sites of inflammation in a mouse arthritis inflammation model in vivo and showed usefulness as a potential tool for inflammation detection using non-invasive imaging. Improving neutrophil detection with the universal and specific MUB40 marker will aid the study of broad ranges of inflammatory diseases.
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Submitted on : Thursday, May 14, 2020 - 10:43:46 AM
Last modification on : Monday, November 28, 2022 - 10:38:07 AM

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Mark C. Anderson, Thibault Chaze, Yves-Marie Coïc, Louise Injarabian, Friederike Jönsson, et al.. MUB40 Binds to Lactoferrin and Stands as a Specific Neutrophil Marker. Cell Chemical Biology, 2018, 25 (4), pp.483-493.e9. ⟨10.1016/j.chembiol.2018.01.014⟩. ⟨pasteur-02573125⟩



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