TLR2
- Known as:
- TLR2
- Catalog number:
- 000136A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- TLR2
Related genes to: TLR2
- Gene:
- TLR2 NIH gene
- Name:
- toll like receptor 2
- Previous symbol:
- -
- Synonyms:
- TIL4, CD282
- Chromosome:
- 4q31.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-06-25
- Date modifiied:
- 2016-10-25
Related products to: TLR2
Related articles to: TLR2
- Aberrant activation of Toll-like receptors 1/2 (TLR1/2) is critically implicated in the pathogenesis of numerous inflammatory and immune-mediated disorders, positioning this receptor complex as a high-value therapeutic target. CU-CPT22, a well-established small-molecule TLR1/2 inhibitor, exhibits potent and selective inhibition of TLR1/2 signaling. However, the atomistic details governing its molecular recognition and allosteric modulation remain elusive. Herein, we present an integrated computational framework that synergistically combines enhanced-sampling molecular dynamics (MD) simulations, rigorous binding free energy calculations, and quantum chemical analyses to decipher the mechanistic basis of CU-CPT22 action. Our MD simulations, complemented by principal component analysis (PCA) and free energy landscape (FEL) mapping, reveal that ligand binding induces an initial conformational selection and subsequently restricts the intrinsic large-scale collective motions of the protein, effectively stabilizing the complex in a distinct, low-entropy conformational state. Per-residue energy decomposition within the MM/PBSA framework identifies a non-polar driving force that overcomes a substantial polar desolvation penalty, with hotspot residues Ile319, Phe322, Tyr323, and Phe349 contributing decisively to the binding affinity. Complementary density functional theory (DFT) calculations and interaction region indicator (IRI) analyses elucidate the frontier molecular orbital profile (ΔE = 5.419 eV) and map the electrophilic and nucleophilic regions on the polycyclic core that orchestrate specific noncovalent contacts. Collectively, these findings provide a comprehensive, multi-scale portrait of the CU-CPT22 binding mechanism and establish a robust conceptual and computational framework for the rational design of next-generation, high-affinity TLR1/2 antagonists. - Source: PubMed
Publication date: 2026/09/24
Jiao PengNi ChengliangJin HaonianZhang XiaokunYan Hong - Musk has traditionally been used for cardiovascular disorders, but its active constituents and mechanisms of action in acute myocardial infarction (AMI) remain unclear. - Source: PubMed
Lu FengWang QinyuWang DanDuan HuxinyueHe YacongWu Chunjie - Aluminum-adjuvanted hepatitis B vaccines effectively prevent primary HBV infection but predominantly favor humoral immunity and have limited capacity to induce strong cellular responses. To improve immune-response quality, we developed a polysaccharide-modified hybrid nanoparticle adjuvant (GHNP) for hepatitis B surface antigen (HBsAg) vaccination. - Source: PubMed
Publication date: 2026/09/06
Zhai ZheYou JiansongLiu Xuhan - is an important zoonotic pathogen responsible for severe infections in animals and humans, and the emergence of diverse strains has reduced the effectiveness of conventional antimicrobial therapies. Since there is no broadly protective vaccine, there is a need for new vaccination strategies that focus on conserved antigens from a variety of strains. This study aimed to design and evaluate a multi-epitope vaccine candidate against diverse strains using an integrated pangenome-guided reverse vaccinology approach. To design a multi-epitope vaccine (MEV) candidate against diverse , an integrated computational framework was employed, incorporating pangenome analysis, subtractive proteomics, reverse vaccinology, immunoinformatics, structural modeling, molecular docking, molecular dynamics simulation, immune simulation, and cloning. The conserved core proteins were systematically screened for essential, non-homologous, antigenic, non-allergenic and non-toxic vaccine candidates for epitope prediction. A total of 7421 gene families, including 1169 conserved core genes, were identified through pangenome analysis of 24 complete genomes. Three computationally prioritized candidate proteins were identified through sequential subtractive proteomics: sucrose phosphorylase, peptidoglycan hydrolase PcsB and an RND transporter-associated adaptor protein, annotated in the source database as an RND efflux transporter periplasmic adaptor subunit. We selected eight cytotoxic T-lymphocyte (CTL) epitopes, five helper T-lymphocyte (HTL) epitopes, and three linear B-cell epitopes with favorable predicted immunological properties to develop a 397-amino acid multi-epitope vaccine construct that contains the 50S ribosomal protein L7/L12 adjuvant with rationally designed peptide linkers. The vaccine construct exhibited favorable physicochemical properties, predicted structural stability, and high antigenicity scores. The predicted combined HLA population coverage of the selected CTL and HTL epitopes was 90.77% across the populations included in the analysis. Immune simulation predicted patterns consistent with humoral and cellular immune activation, including sustained IgG production, elevated IFN-γ and IL-2 secretion, efficient antigen clearance, and generation of immunological memory, whereas molecular docking and molecular dynamics simulations characterized the predicted interaction and conformational behavior of the MEV-TLR1/TLR2 complex. Codon optimization (CAI = 0.996) and cloning into the pET-30a(+) expression vector supported the potential feasibility of recombinant expression in . In this study, a rationally designed multi-epitope vaccine candidate against diverse strains was developed using an integrated pangenome-guided reverse vaccinology approach. Based on these computational analyses, the proposed vaccine candidate showed favorable predicted immunogenicity, predicted structural quality, predicted HLA population coverage, and expression feasibility, providing a foundation for future experimental validation and development of a vaccine against diverse . - Source: PubMed
Publication date: 2026/09/12
Alhaggass Nada SalehAljohani Waad AAlromaihi ReemAlnuwaysir Sarah NasserAlmohimid Razan AbdalrahmanAlmatroudi AhmadAllemailem Khaled S - Usutu virus is an emerging mosquito-borne flavivirus with an expanding geographic distribution and increasing public health relevance, yet no licensed vaccine is currently available. This study used an integrated reverse vaccinology strategy to identify conserved immunogenic regions from the Envelope protein and NS5 protein, and construct a multi-epitope vaccine. Following sequential computational screening, the retained T-cell and B-cell epitopes satisfied the predefined selection criteria, while selected T-cell epitopes achieved an estimated 96.41% global population coverage. The final vaccine consisted of 240 amino acids and incorporated an adjuvant together with peptide linkers. Computational characterization indicated favorable physicochemical features and a refined three-dimensional model with improved stereochemical characteristics. Receptor-binding analyses predicted favorable interactions with TLR2 and TLR4, producing weighted docking scores of -1326.1 and -1230.2, respectively. Molecular dynamics simulation further characterized the temporal behavior of the vaccine-TLR2 complex, while MM-GBSA analysis yielded an estimated binding energy of -74.78 kcal/mol. C-ImmSim predicted enhanced humoral and cellular immune-response patterns following repeated antigen administration, including increased simulated antibody levels and changes in immune-cell populations. All findings in this study are based on in silico analyses and represent computational predictions rather than experimentally confirmed results. Further experimental validation is required to verify the predicted properties, immunogenicity, and protective potential of the proposed vaccine candidate. - Source: PubMed
Publication date: 2026/09/11
Alromaihi ReemAlharbi Hajed ObaidAlmerdasi Suleman AbdullahAhmed Mawahib AAljohani Waad AAlromaihi MonaAlhussain LailaKarkashan AlaaRashad Mohamad Riham MohamadAllemailem Khaled S