Journal
JOURNAL OF INFECTIOUS DISEASES
Volume 208, Issue 11, Pages 1830-1840Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/infdis/jit380
Keywords
ticks; Rickettsia; Ehrlichia; insecta; ubiquitin
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Funding
- Centers for Disease Control and Prevention [K01 CK000101]
- National Institutes of Health [R01 AI093653]
- American Association of University Women
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Ubiquitination is a posttranslational modification that regulates protein degradation and signaling in eukaryotes. Although it is acknowledged that pathogens exploit ubiquitination to infect mammalian cells, it remains unknown how microbes interact with the ubiquitination machinery in medically relevant arthropods. Here, we show that the ubiquitination machinery is present in the tick Ixodes scapularis and demonstrate that the E3 ubiquitin ligase named x-linked inhibitor of apoptosis protein (XIAP) restricts bacterial colonization of this arthropod vector. We provide evidence that xiap silencing significantly increases tick colonization by the bacterium Anaplasma phagocytophilum, the causative agent of human granulocytic anaplasmosis. We also demonstrate that (i) XIAP polyubiquitination is dependent on the really interesting new gene (RING) catalytic domain, (ii) XIAP polyubiquitination occurs via lysine (K)-63 but not K-48 residues, and (iii) XIAP-dependent K-63 polyubiquitination requires zinc for catalysis. Taken together, our data define a role for ubiquitination during bacterial colonization of disease vectors.
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