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Last update 08 May 2025

MPI

Last update 08 May 2025

Basic Info

Synonyms

mannose phosphate isomerase, Mannose-6-phosphate isomerase, MPI

+ [4]

Introduction

Isomerase that catalyzes the interconversion of fructose-6-P and mannose-6-P and has a critical role in the supply of D-mannose derivatives required for many eukaryotic glycosylation reactions.

Drugs associated with MPI

Mannose

Target

MPI

Mechanism

MPI modulators [+1]

Active Org.

Avalo Therapeutics, Inc.

Originator Org.

Avalo Therapeutics, Inc.

Active Indication

Congenital Disorder of Glycosylation Type 1B

Inactive Indication

Multiple Sclerosis [+1]

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

AF-15394

Target

MPI

Mechanism

MPI inhibitors

Active Org.-

Originator Org.

Affymax, Inc.

Active Indication-

Inactive Indication

Candidiasis [+1]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with MPI

ChiCTR2500100084

/ SuspendedEarly Phase 1IIT

Mechanism of mannose promoting cholesterol excretion

Start Date07 Apr 2025

Sponsor / Collaborator-

NCT06507735

/ CompletedNot ApplicableIIT

The Effects of Mannose Supplementation on Glycosylation and Protein Levels in Human Sera

The purpose of our study is to investigate the effects of supplemental mannose on sera of humans who are healthy. We will perform proteomics studies to elucidate changes to glycan structure and protein level changes. We hypothesize that we may find that mannose supplies more properly glycosylated protein substrate and helps expedite protein synthesis, that excess mannose leads to alternative glycan structures which confer improved stability, or that there are new sites that become glycosylated after mannose supplementation.

Start Date29 Oct 2024

Sponsor / Collaborator

The University of Texas Southwestern Medical Center

NCT06360055

/ RecruitingNot ApplicableIIT

A Prospective, Single-Center, Open-Label Study of the Effect of Oral D-mannose Tablets on the Pharmacokinetics of Dabigatran Etexilate in Healthy Adults

The aim of this study is to investigate the effects of oral D-mannose tablets for 2 consecutive weeks on the pharmacokinetics of dabigatrun etexilate, a P-glycoprotein probe substrate drug, in healthy adults

Start Date01 Apr 2024

Sponsor / Collaborator

Peking University Third Hospital

100 Clinical Results associated with MPI

100 Translational Medicine associated with MPI

0 Patents (Medical) associated with MPI

934

Literatures (Medical) associated with MPI

01 Jun 2025·Plant Science

Improving the agronomic performance of high-amylose durum wheat

Article

Author: Masci, Stefania ; Sestili, Francesco ; Lafiandra, Domenico ; Metelli, Giulio ; Silvestri, Marco ; Palombieri, Samuela ; Frittelli, Arianna ; Botticella, Ermelinda

High-amylose wheat has garnered significant attention from the food industry for its potential to produce low-glycaemic food products. It is well-established that there is a direct correlation between the amylose content in flour and the amount of resistant starch (RS) in foods. Recently, some research initiatives have successfully produced high-amylose durum wheat by targeting key enzymes in the amylopectin biosynthesis pathway, though this has resulted in a reduction in seed weight. This study aimed to develop durum wheat genotypes with enhanced nutritional and agronomic traits by pyramiding mutations in the SSIIa genes and the GW2-A1 null allele. A cross between Svevo SSIIa^- and Kronos GW2-A1^- was performed, and marker-assisted selection (MAS) strategies were employed to identify ten sister lines (GW2-A1^-/SSIIa^-). Biochemical analyses revealed that the GW2-A1^-/SSIIa^- genotypes exhibited significantly higher amylose and resistant starch (5-10-fold) levels compared to Svevo and GW2-A1^- controls. Phenotypic analyses highlighted that GW2-A1^-/SSIIa^- lines showed a 50 % increase in hundred-grain weight (HGW) and improved grain size parameters compared to Svevo SSIIa^-, though these values remained lower than Svevo and Kronos GW2-A1^-. Yield per plot increased by 67 % compared to Svevo SSIIa^- but was 30-40 % lower than Svevo and Kronos GW2-A1^-. Gene expression analysis revealed upregulation of key starch biosynthesis genes (Susy2, UGPase) in GW2-A1^-/SSIIa^- lines, suggesting compensatory mechanisms for reduced starch content. Downregulation of TPS7 indicated potential limitations in trehalose-6-phosphate biosynthesis, which may influence starch accumulation. This study demonstrates that combining SSIIa and GW2-A1 null mutations can mitigate yield losses associated with high-amylose genotypes while maintaining elevated levels of resistant starch and dietary fiber.

01 May 2025·Fungal Biology

Combined metabolome and transcriptome analyses reveal the pivotal role of mycorrhizal fungi Tulasnella sp. BJ1 in the growth and accumulation of secondary metabolites in Bletilla striata (Thunb.) Reiehb.f.

Article

Author: Chen, Man ; Zhang, Chunchun ; Yuan, Qiang ; Yang, Dongfeng ; Li, Shiqing ; Li, Meiya ; Li, Xiaomei ; Jiang, Fusheng ; Chen, Haimin ; Ye, Yueyu

The orchids usually coexist with mycorrhizal fungi during their growth and development. Numerous studies have substantiated the pivotal regulatory role of Tulasnella sp. mycorrhizal fungi in the germination and growth of orchid seeds. However, there remains a dearth of research elucidating the effects and underlying mechanisms of Tulasnella sp. on the growth, development, and metabolite accumulation in Bletilla striata seedlings. In the current study, metabolomics and transcriptomic analysis were used to reveal the key role of the mycorrhizal fungus Tulasnella sp.BJ1 in the growth and accumulation of secondary metabolites in B. striata. The results demonstrated that the application of BJ1 significantly enhanced the growth and development of B. striata seedlings. In September, the plant weight, tuber diameter, and tuber weight in the BJ1 treatment group reached 44.27 ± 6.79 g, 6.13 ± 0.53 cm, and 23.35 ± 3.06 g, respectively, surpassing those in the control group. The polysaccharide content in the BJ1 treatment group and control group peaked in June, reaching 14.91 ± 2.26 % and 14.38 ± 0.25 %, respectively. Total phenol content in both groups decreased in May and June, and the total phenol content in BJ1 treatment group was significantly lower than that in control group. The significant decrease observed in total phenol content during May and June may be attributed to an increase in proportion of polysaccharides promoted by BJ1. The transcriptome results showed that BJ1 upregulated polysaccharide biosynthesis-related genes, such as mannose phosphatase, transferase, mannose 6-phosphate isomerase, hexokinase, fructose kinase, and glucose 6-phosphate isomerase, as well as genes involved in stilbenes biosynthesis, including hydroxycinnamyltransferase and transcinnamate 4-monooxygenase. Metabolomics data indicated that the content of mannose and seven stilbene compounds in the tubers increased significantly after BJ1 treatment. Interestingly, the accumulation of these compounds corresponds to the pathway of upregulated genes. These findings suggest that an upregulation in mannose synthesis may facilitate the accumulation of polysaccharides in B. striata. Therefore, the current study uncovered that the mycorrhizal fungus Tulasnella sp. BJ1 can not only promote the growth and development of B. striata seedlings and increase tuber yield but also promote the accumulation of polysaccharides and stilbenes.

12 Mar 2025·mBio

Borrelial phosphomannose isomerase as a cell surface localized protein that retains enzymatic activity and promotes host-pathogen interaction

Article

Author: Yang, Xiuli ; Lin, Yi-Pin ; Rai, Ganesha ; Araujo-Aris, Sarai ; Yas, Ozlem B. ; Kitsou, Chrysoula ; Rana, Vipin S. ; Pal, Utpal ; Smith, Alexis A. ; Ronzetti, Michael H. ; Shakya, Anil K. ; Backstedt, Brian T. ; Lipman, Rachel M. ; Dutta, Shraboni ; Herzberg, Osnat

ABSTRACT All organisms produce an intracellular Zn 2+ -dependent enzyme, phosphomannose isomerase (PMI) or mannose-6 phosphate isomerase, that catalyzes the reversible conversion of mannose-6-phosphate and fructose-6-phosphate during sugar metabolism and polysaccharide biosynthesis. Unexpectedly, we discovered an additional PMI function in Borrelia burgdorferi , the pathogen of Lyme disease, where the enzyme is localized on the cell surface and binds to collagen IV—a host extracellular matrix component predominantly found in the skin. The AlphaFold 3-based structural model of B. burgdorferi PMI (BbPMI) retains the active site with tetrahedrally-coordinated Zn 2+ seen in other PMIs of known structure, residing in an elongated crevice. Ligand docking shows that the crevice can accommodate the tip trisaccharide moiety of a glycosylated asparagine residue on the collagen IV 7S domain. Low doses of a well-known PMI benzoisothiazolone inhibitor impair the growth of diverse strains of B. burgdorferi in culture, but not other tested Gram-negative or Gram-positive pathogens. Borrelia cells are even more susceptible to several other structurally related benzoisothiazolone analogs. The passive transfer of anti-BbPMI antibodies in ticks can impact spirochete transmission to mice, while the treatment of collagen IV-containing murine skin with PMI inhibitors impairs spirochete infectivity. Taken together, these results highlight a newly discovered role for BbPMI in mediating host-pathogen interactions during the spirochete infectivity process. In turn, this discovery offers an opportunity for the development of a novel therapeutic strategy to combat Lyme disease by preventing the BbPMI interaction with its host receptor, collagen IV. IMPORTANCE All organisms produce an intracellular enzyme, phosphomannose isomerase (PMI), that converts specific sugars during metabolism. Unexpectedly, we discovered an additional PMI function in Borrelia burgdorferi , the Lyme disease pathogen, where the enzyme is localized on the cell surface and binds to collagen IV—a host extracellular molecule mainly found in the skin. Low doses of PMI chemical inhibitors impair the growth of diverse strains of B. burgdorferi in culture, but not other tested bacterial pathogens. The passive transfer of anti-BbPMI antibodies in ticks can impact B. burgdorferi transmission to mice, while the treatment of collagen IV-containing murine skin with PMI inhibitors impairs infectivity. Taken together, these results highlight a newly discovered role for BbPMI in mediating host-pathogen interactions during infection. In turn, this discovery offers an opportunity for the development of a novel therapeutic strategy to combat Lyme disease by preventing BbPMI function and interaction with host collagen IV.

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