Ask about this productRelated genes to: PGRPL antibody
- Gene:
- PGLYRP2 NIH gene
- Name:
- peptidoglycan recognition protein 2
- Previous symbol:
- -
- Synonyms:
- PGRP-L, PGLYRPL, TAGL-like, tagL, tagL-alpha, tagl-beta, PGRPL
- Chromosome:
- 19p13.12
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-17
- Date modifiied:
- 2014-11-19
Related products to: PGRPL antibody
Related articles to: PGRPL antibody
- Alkaptonuria (AKU) is a rare metabolic disorder caused by homogentisic acid accumulation and characterised by ochronosis, oxidative stress, chronic inflammation, and progressive connective tissue damage. This study aimed to define the circulating proteomic alterations associated with AKU and assess their relationship with nitisinone treatment. Plasma samples from 11 patients with AKU and 6 age- and sex-matched healthy controls were analysed by liquid chromatography coupled to tandem mass spectrometry using label-free quantification. Differentially abundant proteins were identified using thresholds of |logFC| ≥ 1 and Benjamini-Hochberg false discovery rate ≤ 0.01, followed by functional enrichment and treatment-stratified analyses. Twenty-two proteins were differentially abundant between AKU patients and controls. Complement components (C1R, C1S, C9, C4BPA, CPN2), fibronectin, clusterin, PGLYRP2, and haemoglobin subunits showed increased abundance, whereas most immunoglobulin chains, kallikrein, apolipoprotein A2, and alpha-1-antitrypsin showed decreased abundance. Functional enrichment highlighted complement activation, B-cell-mediated and humoral immune responses, immunoglobulin-related functions, platelet activation, and erythrocyte gas-exchange pathways. Correlation analysis linked several proteins, particularly CPN2, APOA2, C1R and C1S, to core biochemical parameters of disease activity. Treatment-stratified analysis identified fourteen proteins that remained significantly altered in both treated and untreated patients, forming a treatment-resistant core of the signature, while several complement-, coagulation-, and lipid-related proteins were significant only in one treatment subgroup. These findings define an AKU plasma proteomic signature dominated by complement activation and humoral immune alterations, together with extracellular matrix, erythrocyte-, and coagulation-associated changes. The persistence of most alterations across treatment groups suggests that residual systemic proteomic dysregulation remains despite nitisinone treatment. - Source: PubMed
Publication date: 2026/08/03
Finetti RebeccaVisibelli AnnaRoncaglia BiancaTrezza AlfonsoPeruzzi LuanaMarzocchi BarbaraSpiga OttaviaCicogni MattiaSalvini LauraTinti LauraCicaloni VittoriaCheleschi SaraRossi MarcoTinti CristinaSantucci Annalisa - Severe cytokine release syndrome (CRS) and immune effector cell-associated neurotoxicity syndrome (ICANS) remain frequent, life-threatening complications of CD19 chimeric antigen receptor (CAR) T-cell therapy and constrain its safety, scalability, and outpatient adoption. Existing predictive models lack sufficient external validation for routine clinical use, and pre-infusion biomarkers that capture host susceptibility before infusion are urgently needed. - Source: PubMed
Publication date: 2026/05/02
Irajizad EhsanFahrmann Johannes FKatayama HiroyukiStrati PaoloNair RanjitChihara DaiAhmed SairahIyer Swaminathan PLocke Frederick LDavila MarcoFlowers Christopher RShpall ElizabethJenq RobertNeelapu Sattva SHanash SamirWestin JasonJain Michael DJohn Teny MSaini Neeraj Y - Patients with multidrug-resistant tuberculosis (MDR-TB) who are resistant to at least both rifampicin and isoniazid, lack effective treatment options in clinic. The gold standard for the diagnosis of MDR-TB is drug sensitivity test, which is time-consuming and has a relatively low positive detection rate. Screening early diagnostic biomarker for MDR-TB is urgent need in clinical practice. - Source: PubMed
Publication date: 2025/08/25
Zhang YangZhang LinyuShi LiyingWei LiliangGan LinHu YutingHuang HuaiXie KepingJiang TingtingLi Ji-Cheng - The spirochete Borrelia burgdorferi causes Lyme disease. In some patients, an excessive, dysregulated proinflammatory immune response can develop in joints leading to persistent arthritis even after antibiotic therapy. In such patients, persistence of antigenic B. burgdorferi peptidoglycan (PGBb) fragments within joint tissues may contribute to immunopathogenesis pre- and post-antibiotic treatment. In live B. burgdorferi cells, the outer membrane shields the polymeric PGBb sacculus from exposure to the immune system. However, unlike most diderm bacteria, B. burgdorferi releases PGBb turnover products into its environment due to the absence of recycling activity. In this study, we identified the released PGBb fragments using a mass spectrometry-based approach. By characterizing the l,d-carboxypeptidase activity of B. burgdorferi protein BB0605 (renamed DacA), we found that PGBb turnover largely occurs at sites of PGBb synthesis. In parallel, we demonstrated that the lytic transglycosylase activity associated with BB0259 (renamed MltS) releases PGBb fragments with 1,6-anhydro bond on their N-acetylmuramyl residues. Stimulation of human cell lines with various synthetic PGBb fragments revealed that 1,6-anhydromuramyl-containing PGBb fragments are poor inducers of a NOD2-dependent immune response relative to their hydrated counterparts found in the polymeric PGBb isolated from dead bacteria. We also showed that the activity of the human N-acetylmuramyl-l-alanine amidase PGLYRP2, which reduces the immunogenicity of PGBb material, is low in joint (synovial) fluids relative to serum. Altogether, our findings suggest that MltS activity helps B. burgdorferi evade PG-based immune detection by NOD2 during growth despite shedding PGBb fragments and that PGBb-induced immunopathology likely results from host sensing of PGBb material from dead (lysed) spirochetes. Additionally, our results suggest the possibility that natural variation in PGLYRP2 activity may contribute to differences in susceptibility to PG-induced inflammation across tissues and individuals. - Source: PubMed
Publication date: 2025/07/07
McCausland Joshua WKloos Zachary AIrnov IrnovSonnert Nicole DZhou JunhuiPutnik RachelMueller Elizabeth ASteere Allen CPalm Noah WGrimes Catherine LJacobs-Wagner Christine - Pullorum disease caused by Salmonella pullorum can negatively affect growth and egg-laying performance, resulting in significant economic losses in poultry farming. In this study, spleen tissues from SP-infected chickens (group P) and SP-uninfected chickens (group N) were analyzed for functional enrichment using whole-genome bisulfite and RNA sequencing. The function of the key gene MSX2 was verified by quantitative real-time polymerase chain reaction and enzyme-linked immunosorbent assay. Results indicated significant changes in the spleen methylation pattern of group P, primarily characterized by hypomethylation in the promoter, intron, and exon regions. Coanalysis identified six genes (MSX2, C21orf62, PGLYRP2, KCNQ3, SEZ6L, and SLC38A11) with significant alterations in differentially methylated regions and differentially expressed genes. MSX2 gene overexpression markedly enhanced the expression and secretion of immune factors [Interferon (IFN)-α, IFN-β, Interleukin (IL)-2, IL-3, and tumor necrosis factor-α] in chicken macrophages, suggesting that MSX2 may play a role in immune regulation in chickens. This study revealed the effects of Salmonella pullorum infection on DNA methylation and gene expression in chicken spleen tissues and screened several potential therapeutic targets, providing new insights and methods for the prevention and control of Pullorum disease. - Source: PubMed
Publication date: 2025/07/01
Wu JiongwenLiang WeimingLiu AijunWang XiaomengFan ZhexiaMa XuerongChen ShuyaFang ChengZhang XiquanLuo Qingbin