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Keywords = cryo immuno-electron microscopy (IEM)

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17 pages, 2956 KiB  
Article
Multiple Nucleocapsid Structural Forms of Shrimp White Spot Syndrome Virus Suggests a Novel Viral Morphogenetic Pathway
by Hui-Ju Huang, Sen-Lin Tang, Yuan-Chih Chang, Hao-Ching Wang, Tze Hann Ng, Rees F. Garmann, Yu-Wen Chen, Jiun-Yan Huang, Ramya Kumar, Sheng-Hsiung Chang, Shang-Rung Wu, Chih-Yu Chao, Kyoko Matoba, Iwasaki Kenji, William M. Gelbart, Tzu-Ping Ko, Hwei-Jiung (Andrew) Wang, Chu-Fang Lo, Li-Li Chen and Han-Ching Wang
Int. J. Mol. Sci. 2023, 24(8), 7525; https://doi.org/10.3390/ijms24087525 - 19 Apr 2023
Cited by 7 | Viewed by 4797
Abstract
White spot syndrome virus (WSSV) is a very large dsDNA virus. The accepted shape of the WSSV virion has been as ellipsoidal, with a tail-like extension. However, due to the scarcity of reliable references, the pathogenesis and morphogenesis of WSSV are not well [...] Read more.
White spot syndrome virus (WSSV) is a very large dsDNA virus. The accepted shape of the WSSV virion has been as ellipsoidal, with a tail-like extension. However, due to the scarcity of reliable references, the pathogenesis and morphogenesis of WSSV are not well understood. Here, we used transmission electron microscopy (TEM) and cryogenic electron microscopy (Cryo-EM) to address some knowledge gaps. We concluded that mature WSSV virions with a stout oval-like shape do not have tail-like extensions. Furthermore, there were two distinct ends in WSSV nucleocapsids: a portal cap and a closed base. A C14 symmetric structure of the WSSV nucleocapsid was also proposed, according to our Cryo-EM map. Immunoelectron microscopy (IEM) revealed that VP664 proteins, the main components of the 14 assembly units, form a ring-like architecture. Moreover, WSSV nucleocapsids were also observed to undergo unique helical dissociation. Based on these new results, we propose a novel morphogenetic pathway of WSSV. Full article
(This article belongs to the Section Molecular Biology)
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23 pages, 8767 KiB  
Article
Partial Immunoblotting of 2D-Gels: A Novel Method to Identify Post-Translationally Modified Proteins Exemplified for the Myelin Acetylome
by Kathrin Kusch, Marina Uecker, Thomas Liepold, Wiebke Möbius, Christian Hoffmann, Heinz Neumann, Hauke B. Werner and Olaf Jahn
Proteomes 2017, 5(1), 3; https://doi.org/10.3390/proteomes5010003 - 12 Jan 2017
Cited by 16 | Viewed by 7843
Abstract
Post-translational modifications (PTMs) play a key role in regulating protein function, yet their identification is technically demanding. Here, we present a straightforward workflow to systematically identify post-translationally modified proteins based on two-dimensional gel electrophoresis. Upon colloidal Coomassie staining the proteins are partially transferred, [...] Read more.
Post-translational modifications (PTMs) play a key role in regulating protein function, yet their identification is technically demanding. Here, we present a straightforward workflow to systematically identify post-translationally modified proteins based on two-dimensional gel electrophoresis. Upon colloidal Coomassie staining the proteins are partially transferred, and the investigated PTMs are immunodetected. This strategy allows tracking back the immunopositive antigens to the corresponding spots on the original gel, from which they are excised and mass spectrometrically identified. Candidate proteins are validated on the same membrane by immunodetection using a second fluorescence channel. We exemplify the power of partial immunoblotting with the identification of lysine-acetylated proteins in myelin, the oligodendroglial membrane that insulates neuronal axons. The excellent consistency of the detected fluorescence signals at all levels allows the differential comparison of PTMs across multiple conditions. Beyond PTM screening, our multi-level workflow can be readily adapted to clinical applications such as identifying auto-immune antigens or host-pathogen interactions. Full article
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