Abstract
The conformational conversion of pentameric C-reactive protein (pCRP) to monomeric CRP (mCRP) has been shown to play important roles in the action of CRP in inflammation regulation. In vivo studies revealed the origin of mCRP and provided insights into how pCRP dissociation affected its functions. However, the interplay and exact bioactivities of CRP isoforms still remain uncertain due to the rapid conformational conversion and complex milieu in vivo. Herein, we have used surface-immobilization of pCRP to generate a preservable intermediate with dual antigenicity expression of both pCRP and mCRP. The intermediate has been further shown to exhibit modified bioactivities, such as a high affinity with solution-phase pCRP and an enhanced capacity of complement interaction. These results thus not only provide the conformational conversion details of CRP, but also propose a simple way in vitro to study how the functions of CRP are tuned by distinct isoforms.
Highlights
C-reactive protein (CRP) is a pentameric protein playing important roles in inflammation in the human body[1, 2]
Conformational conversion of pentameric CRP (pCRP) to monomer CRP (mCRP) was shown critical to the function of CRP in vivo[6, 9, 10]
In contrast to the activated platelets or membrane-induced conformation conversion of CRP[8, 15], the present study has proposed another circumstance for pCRP dissociation occurring, which agrees well with the previous study and propose a simpler way to generate the CRP intermediate
Summary
C-reactive protein (CRP) is a pentameric protein playing important roles in inflammation in the human body[1, 2]. PCRP undergoes the conversion to mCRP under certain conditions. CRP has two naturally occurring and conformationally distinct isoforms, i.e., pentameric CRP (pCRP) and monomer CRP (mCRP)[3,4,5]. This process mainly involves disassembly of pentamer and epitope remolding of native subunit structure. MCRP is different from native subunit in pentamer. Recent studies revealed that biological function of CRP mainly involves its conformation changes, and mCRP was indicated to be more active in exerting biological effects [6,7,8,9,10]. The inter-subunit disulfide bond of CRP was proved important to its conformation and activities[11, 12]. PCRP is very stable in the presence of calcium [13, 14] and its dissociation occurs mainly in denaturation conditions[1, 3, 13, 14]
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