By Karim E. Hechemy (auth.), Rudolf Toman, Robert A. Heinzen, James E. Samuel, Jean-Louis Mege (eds.)
Coxiella burnetii is the etiological agent of Q fever, a zoonotic affliction chanced on around the world. The bacterium is an engaging instance of intracellular parasitism that has uniquely developed to thrive within the so much inhospitable of mobile compartments-the phagolysosome. figuring out how C. burnetii resists the degradative services of this vacuole, and the host cellphone features coopted for profitable parasitism, are imperative to figuring out Q fever pathogenesis. fresh achievements in glycomics and proteomics are guiding improvement of more desirable detection schemes for the bacterium as well as laying off mild at the host immune reaction to the pathogen. a number of chapters survey immune capabilities that keep watch over or probably exacerbate Coxiella an infection and delve into correlates of protecting immunity elicited by way of vaccination. Comparative genomics can also be the root of chapters discussing diagnostic antigen discovery and molecular typing of the bacterium, with importance for improvement of recent medical, epidemiologic, and forensic tools.
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Additional info for Coxiella burnetii: Recent Advances and New Perspectives in Research of the Q Fever Bacterium
Burnetii invasion and the establishment of the PV. The SCV forms of the phase I and phase II variants both interact with a3bv integrin and CR3 or TLR4 respectively. Adherence of phase I variants induces membrane ruffling through the activation of Rho GTPase. Subsequent internalization of both phase I and phase II into tight fitting phagosomes that interact with endosomal and autophagic vesicles result in recruitment of Rab5 and LC3 to the phagosomal membrane. Protein production by C. burnetii is required for interaction with the autophagy pathway and for stalling the interaction with lysosomal compartments.
1; Beron et al. 2002). In addition, activation of the autophagic pathway favors C. burnetii infection and bacterial replication (Gutierrez et al. 2005). L3C is recruited to the C. burnetii vacuole as early as 5 min after infection and this localization is dependent on protein production by C. burnetii as chloramphenicol prevents co-localization (Fig. 1; Romano et al. 2007). Another autophagic protein, Beclin 1, also localizes to the C. burnetii PV and knockdown of this protein through siRNA reduces the number and size of the generated PVs.
Burnetii both end up in PV compartments containing the lysosomal enzyme acid phosphatase, however, the kinetics of acquisition are different. The PV containing metabolically active C. burnetii is stalled in its maturation as the acquisition of acid phosphatase may be delayed by up to ~2 h (Howe et al. 2003). This suggests that C. burnetii actively modifies this compartment and is not just simply a passive bystander in the events that occur after phagocytosis. The mechanisms that mediate these events are clearly examples of virulence mechanisms but specific proteins are only beginning to be identified.