Ask about this productRelated genes to: ALG11 antibody
- Gene:
- ALG11 NIH gene
- Name:
- ALG11 alpha-1,2-mannosyltransferase
- Previous symbol:
- -
- Synonyms:
- KIAA0266, CDG1P
- Chromosome:
- 13q14.3
- Locus Type:
- gene with protein product
- Date approved:
- 2006-03-24
- Date modifiied:
- 2019-01-18
Related products to: ALG11 antibody
Related articles to: ALG11 antibody
- Pitch canker caused by the fungus is a destructive disease that affects pines in Europe, South Africa, and North America, particularly along the southeastern and western coasts of the United States. This study systematically elucidated the function of the Leucine-rich repeat (LRR) protein FcLRR1 in the pine pitch canker pathogen . A total of 13 LRR proteins were identified via bioinformatic analysis. Using a gene knockout system, we demonstrated that deletion of FcLRR1 significantly impaired vegetative growth, conidiation, and conidium germination; led to a complete loss of macroconidia production; and drastically reduced abiotic stress tolerance and virulence. Transcriptome profiling revealed 612 downregulated genes, which were significantly enriched in pathways such as starch and sucrose metabolism, indicating that modulated energy supply and pathogenicity through carbon source utilization. Through genome-wide protein structure modeling and yeast two-hybrid assays, we identified and validated the interaction between FcLRR1 and ALG-11, among other candidate proteins, further supporting its involvement in carbon metabolism, cell wall integrity, and pathogenesis. This study represents the first functional characterization of an LRR-containing protein in a forest pathogenic fungus and provides a foundational basis for developing targeted disease control strategies. - Source: PubMed
Publication date: 2026/04/16
Dai TingtingChen ChaoJu FangyiZang JiahuiQi ZhongqiangWang HaiwenZhang XiaoruiYang Chun - The opportunistic fungal pathogen Candida albicans forms biofilms with viscoelastic properties and rheological response to flow that can significantly impact its biology and life cycle. The rheological phenotypes of fungal biofilms, however, have been neither quantified extensively nor genetically dissected. We have developed methods to quantify the rheology of fungal biofilms, and, here, we analyzed a panel of C. albicans deletion mutants impaired in cell wall structure or extracellular matrix (ECM) production for rheological phenotypes. Increased elastic moduli, indicative of higher viscoelasticity, were evident in strains singly deleted for ALG11, KRE5, and PMR1, with complementation strains showing wild-type phenotypes. The deletion mutants exhibited a smooth biofilm morphology on agar, with reduced hyphae, decreased ECM, and decreased fluconazole resistance. Transcriptional profiling of these strains identified altered expression of genes affecting cell membrane/cell wall biology, translation, protein catabolism, lipid metabolism, and filamentous development. Collectively, the data present C. albicans biofilm rheology as a distinct phenotype affected by ECM production and cell morphology, while identifying genes for the further investigation of fungal biofilm viscoelasticity. - Source: PubMed
Publication date: 2026/01/20
Abriat ClémenceHuang LinqiSunder ShamBauman Joshua SLandry Grant ALischwe Mueller Hunter RVanEpps J ScottSolomon Michael JKumar Anuj - Congenital disorders of glycosylation (CDG) are a complex and heterogeneous family of rare metabolic diseases that affect protein and lipid glycosylation and glycosylphosphatidylinositol synthesis. These disorders can affect multiple organs, leading to a broad spectrum of symptoms that vary among different CDG subtypes and between individuals with same type of CDG. This study aimed to investigate the genetic variants, molecular etiologies, and clinical features of 20 Chinese patients diagnosed with CDG. - Source: PubMed
Publication date: 2025/12/23
Zhao PeiweiTan LiMeng QingjieZhang LeiHuang YufengZhang XiankaiHu YanqiuZhou ShiqiongHe Xuelian - Gilthead seabream (Sparus aurata) is an important fish in the aquaculture industry frequently suffering from Sparicotylosis caused by infection with the parasite Sparicotyle chrysophrii. The seabream gills are coated by a mucus layer containing a large abundance of O- and N-glycans. The glycan repertoire is important for homeostasis, host-microbiota interactions and infection as it influences microbial growth, quorum sensing, virulence and adhesion. Here, the mucus glycome from gills with and without experimental S. chrysophrii infection was analyzed using liquid chromatography mass spectrometry. Infection did not induce overall shifts in either terminal moieties or core structures among the 57 O-glycans identified. The proportion of the detected glycans (N + O-glycans) that were N-glycans was 54 % (median) in non-infected gill mucus, while it was 28 % in mucus from S. chrysophrii infected gills. Eight N-glycans were detected and the relative abundance of high mannose N-glycans was increased more than threefold in gill mucus from infected fish. By leveraging gill transcriptomic data, nine transcripts were found differentially expressed in S. chrysophrii infected fish. Notably, the expression of asparagine-linked glycosylation protein 11 (alg11), which codes for a mannosyltransferase that transfers mannose in an α1-2 linkage in the dolichol-linked oligosaccharide pathway correlated with the relative abundance of high-mannose N-glycans. The abundance of high mannose N-glycans also correlated with the number of S. chrysophrii parasites and the abundance of the bacterium 2013Ark19i (Candidatus Ichthyocystis sparus), proposed as the causing agent of epitheliocystis. - Source: PubMed
Publication date: 2025/12/22
Benktander JohnEstensoro ItziarSitjà-Bobadilla AriadnaPiazzon M CarlaLindén Sara K - This study investigated the causes of Mitochondrial Dysfunction (MD) in Diabetic Kidney Disease (DKD) progression, and identified genes associated with DKD, especially those with significant genetic causal effects, to provide a theoretical basis for DKD treatment. - Source: PubMed
Publication date: 2025/06/03
Zhang YanWang ZeyuanShang JinDong YijunZhao Zhanzheng