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CFP-10 from Mycobacterium tuberculosis Selectively Activates Human Neutrophils through a Pertussis Toxin-Sensitive Chemotactic Receptor.

Artikel i vetenskaplig tidskrift
Författare Amanda Welin
Halla Björnsdottir
Malene Winther
Karin Christenson
Tudor I Oprea
Anna Karlsson
Huamei Forsman
Claes Dahlgren
Johan Bylund
Publicerad i Infection and immunity
Volym 83
Nummer/häfte 1
Sidor 205-213
ISSN 1098-5522
Publiceringsår 2015
Publicerad vid Institutionen för odontologi
Institutionen för medicin, avdelningen för reumatologi och inflammationsforskning
Sidor 205-213
Språk en
Länkar dx.doi.org/10.1128/IAI.02493-14
Ämneskategorier Medicinska grundvetenskaper

Sammanfattning

Upon infection with Mycobacterium tuberculosis, neutrophils are massively recruited to the lungs, but the role of these cells in combating the infection is poorly understood. Through a type VII secretion system, M. tuberculosis releases a heterodimeric protein complex, containing a 6-kDa early secreted antigenic target (ESAT-6) and a 10-kDa culture filtrate protein (CFP-10), that is essential for virulence. Whereas the ESAT-6 component possesses multiple virulence-related activities, no direct biological activity of CFP-10 has been shown, and CFP-10 has been described as a chaperone protein for ESAT-6. We here show that the ESAT-6:CFP-10 complex induces a transient release of Ca(2+) from intracellular stores in human neutrophils. Surprisingly, CFP-10 rather than ESAT-6 was responsible for triggering the Ca(2+) response, in a pertussis toxin-sensitive manner, suggesting the involvement of a G-protein-coupled receptor. In line with this, the response was accompanied by neutrophil chemotaxis and activation of the superoxide-producing NADPH-oxidase. Neutrophils were unique among leukocytes in responding to CFP-10, as monocytes and lymphocytes failed to produce a Ca(2+) signal upon stimulation with the M. tuberculosis protein. Hence, CFP-10 may contribute specifically to neutrophil recruitment and activation during M. tuberculosis infection, representing a novel biological role for CFP-10 in the ESAT-6:CFP-10 complex, beyond the previously described chaperone function.

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