PLP2

Last update 08 May 2025

Basic Info

Synonyms

A4, A4-LSB, Differentiation-dependent protein A4

+ [4]

Introduction

May play a role in cell differentiation in the intestinal epithelium.

100 Clinical Results associated with PLP2

100 Translational Medicine associated with PLP2

0 Patents (Medical) associated with PLP2

140

Literatures (Medical) associated with PLP2

01 Mar 2025·International Journal of Biological Macromolecules

Diverse strategies utilized by coronaviruses to evade antiviral responses and suppress pyroptosis

Article

Author: Yan, Yuqi ; Shi, Wen ; Yang, Yang ; Shi, Fushan ; Xu, Jinxia ; Li, Xiaoliang ; Shi, Yuhua ; Fu, Xinyu ; Li, Danyue ; Xu, Jidong ; Lv, Qian ; Li, Xinyue ; Chen, Nan ; Xu, Weilv

Viral infections trigger inflammasome-mediated caspase-1 activation. Nevertheless, limited understanding exists regarding how viruses use the active caspase-1 to evade host immune response. Here, we use porcine epidemic diarrhea virus (PEDV) as a model of coronaviruses (CoVs) to illustrate the intricate regulation of CoVs to combat IFN-I signaling and pyroptosis. Our findings demonstrate that PEDV infection stabilizes caspase-1 expression via papain-like protease PLP2's deubiquitinase activity. This stabilization of caspase-1 disrupts IFN-I signaling by cleaving RIG-I at the D189 residue. Furthermore, we demonstrate that 6-thioguanine (6TG), a PLP2 inhibitor, reverses the inhibitory effect on IFN-I signaling mediated by PLP2 and significantly reduces PEDV replication. Additionally, PLP2 degrades GSDMD-p30 by removing its K27-linked ubiquitin chain at K275 to restrain pyroptosis. Papain-like proteases from other genera of CoVs (PDCoV and SARS-CoV-2) have the similar activity to degrade GSDMD-p30. We further demonstrate that SARS-CoV-2 N protein induced NLRP3 inflammasome activation also uses the active caspase-1 to counter IFN-I signaling by cleaving RIG-I. Therefore, our work unravels a novel antagonistic mechanism employed by CoVs to evade host antiviral response.

31 Jan 2025·Recent Advances in Inflammation & Allergy Drug Discovery

Evaluation of Toxoplasma gondii Perforin-like Proteins (PLPs) to Find the Potential Epitopes for Immunization through in silico Approach

Article

Author: Safari, Mohamad Hosein ; Majidiani, Hamidreza ; Basati, Gholam ; Siamian, Davood ; Asghari, Ali ; Hosseini, Seyyed Amir

Background:Toxoplasma gondii (T. gondii) is a widespread apicomplexan parasite that affects approximately one-third of the global population, posing particular risks to pregnant women and individuals with weakened immune systems. Despite its significant impact, there is currently no vaccine available for humans.Objective:This study employs computational methods (in silico) to investigate the physicochemical, antigenic, and structural properties of Perforin-like proteins (PLPs) from T. gondii, as well as to identify immunogenic epitopes within these antigens.Methods:For this aim, amino acid sequences of TgPLP1 and TgPLP2 were retrieved and submitted to the ProtParam (physicochemical), VaxiJen v2.0 (antigenicity), NetSurfP-6.0 (2D structure), Robetta (3D structure) web servers, along with the IEDB server to decipher the immunogenic epitopes. Subcellular characteristics such as signal peptide, transmembrane domain, post-translational modifications (PTMs), and cellular localization were also predicted.Results:Both proteins had a high MW of 125.50 and 92.21, respectively, with an alkaline pI, a 30 hours half-life in mammalian reticulocytes, good thermotolerance (high aliphatic index), and hydrophilicity properties (negative GRAVY). They also showed good antigenicity (0.7021 [PLP1] vs 0.5701 [PLP2]), while they were non-allergenic. Both proteins were extracellular with numerous post-translational modification sites (phosphorylation, glycosylation, and acetylation), and a transmembrane domain was only present in TgPLP1, with no signal peptide in both. Furthermore, numerous immunogenic B- and T-cell epitopes were identified within the TgPLPs sequences, suggesting their potential for inclusion in multi-epitope vaccine designs.Conclusion:Further studies are needed to confirm these findings and assess the efficacy of the proposed vaccine constructs.

01 Jan 2025·Journal of Chromatography B

Purification of plasmid DNA using a novel two stage chromatography process

Article

Author: Yu, Mengran ; Yu, Minglei ; Qian, Feng

The chromatography process of large-scale plasmid purification with high efficiency and low cost has always been a major challenge. We established a two-step plasmid chromatography purification process combining multimodal and thiophilic chromatography with an overall chromatography yield of nearly 70%. Capto Core 700, a multimodal core-shell particle, was firstly used to remove the impurities from the crude lysate. The effects of different experimental conditions on chromatography recovery and impurity removal were screened. Compared to conventional size exclusion chromatography, the sample load and flow rate of this step were enhanced by 40-fold and 5-fold, respectively, while maintaining a 90% yield. For the thiophilic chromatography (Capto PlasmidSelect), the method of Design of Experiments (DoEs) was used to study the influence of parameters on the results. The effects of ammonium sulfate concentration, sodium chloride concentration and flowrate in the elution phase were studied and optimized with a central composite design model consisting of 17 experiments. The versatility of this process was demonstrated by successfully purifying three different lentiviral packaging plasmids (pLP1, pLP2 and pLP/VSVG) and the target plasmid containing green fluorescent protein (GFP). Purified plasmids consistently achieved a supercoiled purity of at least 90% with endotoxin levels below 5 EU/mg. Lentiviral vectors packaged using these plasmids exhibited high infectious titers of 1 × 10⁷ TU/mL, thereby verifying the process applicability for diverse plasmid purification requirements.

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PLP2

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