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Legume Nodule Biochemistry and Function
Published in Peter M. Gresshoff, Molecular Biology of Symbiotic Nitrogen Fixation, 2018
Robert B. Mellor, Dietrich Werner
In the early stages of cell colonization, ER vesicles become visibly more numerous throughout the host cell. During this time the ER-located enzymes choline phosphotransferase and GDP-DMP-mannosyltransferase are stimulated by 200 and 300%, respectively.71 Direct connections between the ER and PBM as reported by Kijne and Planqué74 are probably not significant, but a direct transfer of components by vesicle shuttle from the ER matrix to the PBS still cannot be ruled out. The case of alpha-mannosidase is an example. The PBS-located isoenzyme II is made on bound ribosomes of the rough ER,75 remains in the plant vacuome,56 but has not been found in the Golgi.
GlycoVHH: optimal sites for introducing N-glycans on the camelid VHH antibody scaffold and use for macrophage delivery
Published in mAbs, 2023
Loes van Schie, Wander Van Breedam, Charlotte Roels, Bert Schepens, Martin Frank, Ahmad Reza Mehdipour, Bram Laukens, Wim Nerinckx, Francis Santens, Simon Devos, Iebe Rossey, Karel Thooft, Sandrine Vanmarcke, Annelies Van Hecke, Xavier Saelens, Nico Callewaert
N-glycan profiling of glycovariants Q14N-P15A-G16T, G27N-P30T and P48N-K50T through capillary electrophoresis on a DNA sequencer confirmed that in addition to the main Man5GlcNAc2, higher molecular weight glycans were present in small quantities (Supplementary F and G). These additional N-glycans (with a main peak of Hex8GlcNAc2) were recalcitrant to α-1,2-mannosidase and were only partially hydrolyzed by Jack Bean α-1,2/3/6-mannosidase. This behavior is identical to that of glycans observed earlier on other P. pastoris GlycoSwitchM5-produced proteins, where we identified the Hex8GlcNAc2 species as Man5GlcNAc2 with a substituent consisting of Manβ-1,2-Manβ-1,3-Glcα-1,3-R.22 It is known that the β-mannosyltransferase gene family is responsible for the addition of β-mannose residues in P. pastoris. 23 Blocking the synthesis of these apparently also allows for the underlying α-Glc residue to be hydrolyzed by the secretory system α-glucosidase. Indeed, disruption of the BMT2 gene by inducing a double-guide CRISPR-Cpf1-mediated deletion resulted in a more homogeneous N-glycosylation profile of GBP-Q14N-P14A-G16T (Figure 2e), consistent with a previous report that Bmt2p is the key β-mannosyltransferase in the synthesis of these off-target N-glycans.24
Ocular abnormalities in a patient with congenital disorder of glycosylation type Ig
Published in Ophthalmic Genetics, 2019
Hamed Esfandiari, Marilyn B. Mets, Katherine H. Kim, Sudhi P. Kurup
The asparagine-linked glycoylation 12 gene (ALG12, cytogenetic location: 22q13.33) codes for the enzyme, dolichyl-P-mannose:Man-7-GlcNAc-2-PP-dolichyl-⍺-6-mannosyltransferase, which adds the eighth mannose residue onto lipid-linked oligosaccharide precursors and leads to CDG type Ig (11). CDG type Ig (MIM: 607143) is a severe multi-system disorder of neonatal onset that is characterized by failure to thrive, hypotonia, psychomotor retardation, facial dysmorphism, microcephaly, recurrent infections, and skeletal abnormalities (1). CDG type Ig, as with the majority of the CDG, is associated with autosomal recessive inheritance, and carrier couples face a 25% risk of an affected child with each pregnancy. Carriers are not predicted to exhibit any features of the disorder. Most of the pathogenic variants affecting ALG12 to date have been missense variants in highly conserved regions of the protein. The c.563G>A/p.C188Y variant has not been previously reported in disease-related databases nor in large population databases of healthy adults. While the p.C188Y is a non-conserved amino acid substitution, it is predicted to impact secondary protein structure due to the residues differing in polarity, charge and size. In silico analyses by PolyPhen and SIFT were inconclusive. While we cannot completely rule out the possibility that this variant is benign, c.563G>A/p.C188Y is a good candidate for a likely pathogenic variant and consistent with the patient’s carbohydrate-deficient transferrin assay results and clinical presentation.
Regulatory network analysis of hypertension and hypotension microarray data from mouse model
Published in Clinical and Experimental Hypertension, 2018
Yanli Zhu, Jingming Zhuo, Chunmei Li, Qian Wang, Xuefei Liu, Lin Ye
Sept6, a member of the septin family of GTPases, has various cellular roles, including cytoskeletal reorganization, exocytosis, and membrane dynamics (18). In neuronal functions regulated by the ERK3/MK5 pathway, Sept7 was identified as an interacting partner of ERK3, forming a ternary complex that regulates Rho GTPases (19). In addition, blood pressure can be regulated by the Rho kinase pathway in the brain stem based on the sympathetic nervous system activity (20). Moreover, Sept6 was shown to regulate the cytoarchitecture of neurons (21), and arterial blood pressure was modulated by brain serotonin owing to the influence of the serotonergic neuronal system (22). Pigx was also identified as a BPH-related DEG in the regulatory network of the 4 tissues. This gene encodes a type 1 transmembrane protein, which is an essential component of glycosylphosphatidylinositol mannosyltransferase I, for transferring of mannoses (23). Combined with PIG-M, Pigx can form GPI-MTI (α1–4 mannosyltransferase), which serves various functions such as receptor signaling, complement activation, signal transduction, and adhesion (24), and pathways such as apelin receptor signaling play a crucial role in maintaining arterial blood pressure (25). Therefore, Sept6 and Pigx are genes that are potentially involved in the pathogenesis of BPH by participating in pathways such as “lipid biosynthetic process”.