Abstract
Anaplasma phagocytophilum, the aetiologic agent of human granulocytic anaplasmosis (HGA) is an obligate intracellular Gram-negative bacterium. During intracellular replication, A. phagocytophilum interacts with many host cell components including actin cytoskeleton. However the bacterial factors contributing to the interaction between A. phagocytophilum and actin filaments remain unknown. In this study we identified a novel type IV secretion system substrate of A. phagocytophilum by employing TEM-1 β-lactamase based protein translocation assay, and found it is an actin filament-associated protein. Here, we name this protein as an actin filament-associated Anaplasma phagocytophilumprotein (AFAP). Further analysis showed that the middle region of AFAP harboring four tandem repeats is involved in its interaction with actin filaments. The identification and characterization of an actin filament-associated A. phagocytophilum protein in this study may help understand the interaction between A. phagocytophilum and actin cytoskeleton of its host cells, facilitating the elucidation of HGA pathogenesis.
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