2017
DOI: 10.1007/978-3-319-73377-7_15
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Heat Shock Proteins in Vector-pathogen Interactions: The Anaplasma phagocytophilum Model

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Cited by 5 publications
(4 citation statements)
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“…). Among the three types of HSP70‐2, the protein showed the greatest identify with HSP70‐2A (Espinosa et al ., ). The gene was thus named HSPA2A .…”
Section: Resultsmentioning
confidence: 97%
“…). Among the three types of HSP70‐2, the protein showed the greatest identify with HSP70‐2A (Espinosa et al ., ). The gene was thus named HSPA2A .…”
Section: Resultsmentioning
confidence: 97%
“…Other tick molecules facilitating pathogen acquisition include Kunitz-type protease inhibitors, Bm86, subolesin, crt, and serum amyloid A [34]. However, when ticks are infected by a pathogen, they activate an immune or stress response to combat against pathogen infection including heat shock protein (HSP) [34][35][36]. HSP response might help to increase tick survival by protecting from stress and preventing desiccation at high temperatures.…”
Section: Discussionmentioning
confidence: 99%
“…This can be explained by increased metabolic costs of the infection and related cellular stress, or activated immune response in the vector. For example, the regulatory role of RPL40 in stress response has been described in model organisms such as Drosophila fruit flies, or arginine kinase has been shown to contribute to the resistance of Bombyx mori to nucleopolyhedrovirus (Kang et al, 2011;Espinosa et al, 2017). Hence, the presence of these peptides does not appear to be unique to the tick infection with B. duttonii but the exact functions of functionally similar proteins in the tick-pathogen interactions remain to be elucidated.…”
Section: Feedingsmentioning
confidence: 99%