Abstract
We report a unique phenomenon, the opposite color response of a giant polyoxometalate, (NH4)42[Mo132O372(CHCOO)30] (H2O)72 ([Mo132]), to the existing states of human papillomavirus (HPV) major capsid protein, L1-pentamer (L1-p), and virus-like particles (VLPs). The color responses originate from the different assembly forms between [Mo132] and the capsid protein. The latter were inspected and separated by using CsCl gradient centrifugation, and validated in detail by sodium dodecyl sulfate-polyacrylamide gel-electrophoresis (SDS-PAGE), dynamic light scattering (DLS), and transmission electron microscopy (TEM) imaging. Furthermore, the intrinsic mechanisms were investigated in-depth by using XPS-based semi-quantitative analysis and well-designed peptides, revealing the critical points of L1 that determine the charge–transfer ratio between Mo(V) to Mo(VI), and consequently, the levels of [Mo132] hypochromic in different assemblies. Such a unique phenomenon is significant as it supplies a colorimetry approach to distinguish the existing states of the HPV capsid protein and would be significant in the quality assay of the HPV vaccine and existing states of other viruses in the future.
Highlights
Human papillomavirus (HPVs) causes commonly transmitted infections that occur in humans [1,2]
As a kind of prophylactic vaccine, virus-like particles (VLPs) were shown to be effective for protecting several subtypes of HPV from infections [5,6]
The [Mosolution to the cluster in aqueous (Figure which can be assigned to the band intervalence the (IVCT)
Summary
Human papillomavirus (HPVs) causes commonly transmitted infections that occur in humans [1,2]. The color changes are reversible because the Mo(VI) at the highest oxidized state are reduced while the cluster structure is maintained, just like the oxidation at a reduced state [23,24] These properties of POMs and their charged surface provide an excellent opportunity to detect the existing state of the proteins comprising capsids through the electrostatic interaction with free N-terminals bearing redox features. The states of some proteins that can be oxidized and reduced can be characterized through the color fading of giant POMs after the redox process In this context, we selected a giant brown Keplerate cluster, (NH4 )42 [Mo132 O372 (CHCOO)30 ](H2 O) , abbreviated as [Mo132 ], which contains 72 Mo(VI) and 60 Mo(V), to sensitize the status of L1 proteins and the stability of the capsid [25].
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
