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MUB40 Binds to Lactoferrin and Stands as a Specific Neutrophil Marker

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Anderson, Mark, C. | Chaze, Thibault | Coïc, Yves-Marie | Injarabian, Louise | Jönsson, Friederike | Lombion, Naelle | Selimoglu-Buet, Dorothée | Souphron, Judith | Ridley, Caroline | Vonaesch, Pascale | Baron, Bruno | Arena, Ellen, T | Tinevez, Jean-Yves | Nigro, Giulia | Nothelfer, Katharina | Solary, Eric | Lapierre, Valérie | Lazure, Thierry | Matondo, Mariette | Thornton, David | Sansonetti, Philippe | Baleux, Françoise | Marteyn, Benoit

Edité par CCSD ; Cell Press -

International audience. 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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