Characterisation of hookworm heat shock factor binding protein (HSB-1) during heat shock and larval activation.
Characterisation of hookworm heat shock factor binding protein (HSB-1) during heat shock and larval activation.
复制标题
热休克和幼虫激活过程中钩虫热冲击因子结合蛋白（HSB-1）的表征。
DOI：
10.1016/j.ijpara.2010.12.001
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发表时间：
2011-04
影响因子：
4
通讯作者：
Hawdon JM
中科院分区：
文献类型：
--
作者：
Krepp J;Gelmedin V;Hawdon JM
When hookworm infective L3s infect their mammalian host, they undergo a temperature shift from that of the ambient environment to that of their endothermic host. Additionally, L3s living in the environment can be exposed to temperature extremes associated with weather fluctuations. The heat shock response (HSR) is a conserved response to heat shock and other stress that involves the expression of protective heat shock proteins (HSPs). The HSR is controlled by heat shock factor 1 (HSF-1), a conserved transcription factor that binds to a heat shock element in the promoter of HSPs, causing their expression. HSF-1 is negatively regulated in part by a HSF binding protein (HSB-1) that binds to and removes HSF-1 trimers bound to HSP gene promoters, resulting in attenuation of the HSR. Herein we describe an HSB-1 ortholog, Ac-HSB-1, from the hookworm Ancylostoma caninum. The Ac-hsb-1 cDNA encodes a 79 amino acid protein that is 71% identical to the Caenorhabditis elegans HSB-1, and is predicted to share the characteristic coiled-coil structural motif comprised of two interacting alpha helices. Recombinant Ac-HSB-1 immunoprecipitated Ce-HSF-1 expressed in mammalian cells that had been heat shocked for 1 h at 42°C, but not from cells incubated at 37°C, indicating that HSB-1 only bound to the active DNA binding form of HSF-1. Expression of Ac-hsb-1 transcripts decreased following 1 h of heat shock, but increased when L3s were incubated at 37°C for 1 h. Activation of hookworm L3s induces an five- to six-fold increase in Ac-hsb-1 expression that peaks at 12 h, coincident with L3 feeding, but that subsequently decreases to two- to three-fold above control at 24 h. Recombinant Ac-HSB-1 immunoprecipitates greater amounts of 70 and 40 kDa proteins from extracts of activated L3s than from non-activated L3s. We propose that an increase in Ac-hsb-1 levels early in activation allows feeding to resume, but that a subsequent decrease in expression permits a HSR that protects non-developing L3s at host-like temperatures. Further investigations of the HSR will clarify the role of HSB-1 and HSF-1 in hookworm infection.
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影响因子：
4
作者：
Brand, AM;Varghese, G;Hawdon, JM
通讯作者：
Hawdon, JM
影响因子：
4
作者：
Devaney, Eileen
通讯作者：
Devaney, Eileen
影响因子：
4
作者：
Brand, A;Hawdon, JM
通讯作者：
Hawdon, JM
影响因子：
4
作者：
Gao X;Frank D;Hawdon JM
通讯作者：
Hawdon JM
影响因子：
2.7
作者：
CASSADA, RC;RUSSELL, RL
通讯作者：
RUSSELL, RL