Human GPI peptide

Objective: To evaluate the levels of serum beta-2-glycoprotein I (beta(2)GP1) and clusterin in the duality of Preeclampsia and HIV. Method: Stored serum samples collected from 72 pregnant women were stratified according to the pregnancy type (pre-eclamptic and healthy normotensive groups) and HIV status (positive or negative). A Bio-Plex multiplex immunoassay was used to determine the concentrations of clusterin and beta(2)GP1. Results: Clusterin concentrations differed significantly (p = 0.01) between the HIV positive (+) (mean = 123 800 ng/ml; 95 % CI: 105 400-142 200) vs. HIV negative (-) (mean = 92 190 ng /ml; 95 %CI: 75 840-108 500) groups and across all groups (p = 0.0006). Beta-2-glycoprotein I concentration differed significantly based on HIV status (p < 0.0001); HIV+ (mean = 393 649 ng/ml; 95 %CI: 30 300-467 000) vs HIV(mean = 224 309 ng/ml; 95 %CI: 154 000-294 700) and across all groups (p < 0.0001). No significant difference was observed between normotensive and Pre-eclamptic groups for both clusterin and beta(2)GPI. Conclusion: Serum concentrations of clusterin and beta(2)GPI were significantly increased in HIV positive pregnancies. It is postulated that both clusterin and beta(2)GPI may have a role in HIV disease progression. These findings need to be confirmed in studies having larger sample sizes and detailed information on anti-retroviral therapy. (C) 2020 Published by Elsevier B.V.

Protein O-mannosyltransferases (PMTs) have been identified in fungi but not in plants and nematodes, which makes PMTs become attractive targets for developing a new strategy against phytopathogens. Three PMTs have been identified in Fusarium oxysporum, a fungal pathogen that causes vascular wilt in a broad range of economical crops. By deletion or suppression of the pmt genes, we showed that all mutants displayed retarded growth, reduced conidiation, cell wall defects, ER stress and attenuated virulence in F. oxysporum f.sp. cucumerinum. In addition, the Delta prnt1 exhibited reduced thermotolerance, while the Delta pmt4 and the pmt2 conditional mutant exhibited abnormal polarized growth. Comparative glycoproteome analysis of these pmt mutants revealed that PMTs preferentially modified random coils with flanking regions rich in Ser, Thr, Ala, Glu, Asp and Lys at the stem region of membrane proteins, the N-terminal region close to signal peptide of secreted proteins, or surface of soluble proteins. PMT1 specifically acted on nuclear proteins and proteins that are responsible for protein folding, which might contribute to thermotolerance. PMT4 specifically acted on the membrane and soluble proteins in secretory pathways, especially the GPI anchoring pathway, which might contribute to synthesis and transportation of GPI anchored proteins and thus polarized growth. PMT2 was responsible for modification of proteins that are required for protein folding and cell wall synthesis, which might make PMT2 essential. Our results gave an insight to understanding of the roles of each O-mannosyltransferase in F. oxysporum f.sp. cucumerinum and provide a new perspective to prevent Fusarium wilt.