A novel enzyme immunoassay for the measurement of plasma (1 → 3)-β-D-glucan levels

Sunamura, Ei-Ichiro; IWASAKI, Manami; Shiina, Shota; Kitahara, Shin-ichiro; Yotani, Takuya; Manabe, Mitsuhisa; Miyazaki, Osamu

doi:10.1016/j.jim.2020.112872

Cited by 7 publications

(4 citation statements)

References 22 publications

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“…Detection of 1, 3-β-D glucan most often indicates fungal infections, 19 but this patient, unexpectedly, tested negative. However, matrix-assisted laser desorption ionization-time of flight mass spectrometry and a rapid microbial identification system revealed C. auris in his blood.…”

Section: Discussionmentioning

confidence: 79%

A Candidemia Case Caused by a Novel Drug-Resistant Candida auris with the Y132F Mutation in Erg11 in Mainland China

Xu¹,

Zhang²,

Han³

et al. 2023

IDR

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Background Candida auris is a pathogen first found in external ear canal, becoming a major threat to global health. Here, we describe a candidemia case caused by a novel drug-resistant Candida auris strain. Case Presentation An 80-year-old patient, with multiple serious medical conditions, was suffered from candidemia caused by Candida auris , died 9 days after admission in our hospital. Phylogenetic analysis indicates that this C. auris isolate (designated BJCA003) belongs to the South Asian clade, carries the Y132F mutation in the protein Erg11. And antibiotic susceptibility test indicated that BJCA003 is resistant to fluconazole and amphotericin B, not susceptible to caspofungin. In addition, this strain has multiple colony and cellular morphologies under different culture conditions. Conclusion Strain BJCA003 is a novel drug resistant C. auris strain in mainland China, the Y132F mutation in Erg11 may attribute to fluconazole-resistance, alarming that we still face more challenges about C. auris.

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Section: Discussionmentioning

confidence: 79%

A Candidemia Case Caused by a Novel Drug-Resistant Candida auris with the Y132F Mutation in Erg11 in Mainland China

Xu¹,

Zhang²,

Han³

et al. 2023

IDR

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“…Analytical methods such as nuclear magnetic resonance (NMR) and chromatography have been used to investigate the detailed structure of β-glucan [19] but often require highly purified and solubilized samples prepared through multiple procedures. Several biochemical methods have been developed to measure β-1,3-glucan, including the limulus amebocyte lysate (LAL) assay and LAL-related methods using the β-1,3-D-glucan recognition molecule (factor G) in horseshoe crabs [20][21][22] as well as those using the β-1,3-glucan recognition proteins in mammals, such as antibodies and dectin-1 (the primary receptor for β-1,3-glucan) [23][24][25]. In addition, to quantify β-1,6-branched β-1,3-glucan, heterosandwich ELISA and the glucan enzymatic method (GEM assay) combining chemical and enzymatic hydrolysis, such as α-glucanase and β-glucanase, have been developed [26][27][28].…”

Section: Discussionmentioning

confidence: 99%

Split Enzyme-Based Biosensors for Structural Characterization of Soluble and Insoluble β-Glucans

Yamanaka¹,

Kurita²,

Hanayama³

et al. 2021

IJMS

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β-Glucan is widely distributed in various plants and microorganisms and is composed of β-1,3-linked d-glucose units. It may have a branched short or long side chain of glucose units with β-1,6- or β-1,4-linkage. Numerous studies have investigated different β-glucans and revealed their bioactivities. To understand the structure-function relationship of β-glucan, we constructed a split-luciferase complementation assay for the structural analysis of long-chain β-1,6-branched β-1,3-glucan. The N- and C-terminal fragments of luciferase from deep-sea shrimp were fused to insect-derived β-1,3-glucan recognition protein and fungal endo-β-1,6-glucanase (Neg1)-derived β-1,6-glucan recognition protein, respectively. In this approach, two β-glucan recognition proteins bound to β-glucan molecules come into close proximity, resulting in the assembly of the full-length reporter enzyme and induction of transient luciferase activity, indicative of the structure of β-glucan. To test the applicability of this assay, β-glucan and two β-glucan recognition proteins were mixed, resulting in an increase in the luminescence intensity in a β-1,3-glucan with a long polymer of β-1,6-glucan in a dose-dependent manner. This simple test also allows the monitoring of real-time changes in the side chain structure and serves as a convenient method to distinguish between β-1,3-glucan and long-chain β-1,6-branched β-1,3-glucan in various soluble and insoluble β-glucans.

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“…Several papers have been published on the detection of BGs by enzyme-linked immunosorbent assay. Using antibodies specific for (1→3)-β-D-glucan, it is possible to detect fungal BGs in the ng/mL range with a monoclonal antibody against laminarin and bovine serum albumin conjugate [ 27 ] and in the pg/mL range with a monoclonal antibody against laminariheptaose-human transferrin-conjugate antigen [ 28 ]. All of these are specific to the linear (1→3)-β-D-glucan structure, and the possibility of cross-reactivity with plant BGs other than fungi cannot be completely excluded [ 29 ].…”

Section: Discussionmentioning

confidence: 99%

Development of a Highly Sensitive β-Glucan Detection System Using Scanning Single-Molecule Counting Method

Adachi

Nakata

Tanabe

et al. 2021

IJMS

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To overcome the limitations of the Limulus amebocyte lysate (LAL) assay method for the diagnosis of invasive fungal infection, we applied a reaction system combining recombinant β-glucan binding proteins and a scanning single-molecule counting (SSMC) method. A novel (1→3)-β-D-glucan recognition protein (S-BGRP) and a (1→6)-β-glucanase mutant protein were prepared and tested for the binding of (1→6)-branched (1→3)-β-D-glucan from fungi. S-BGRP and (1→6)-β-glucanase mutant proteins reacted with β-glucan from Candida and Aspergillus spp. Although LAL cross-reacted with plant-derived β-glucans, the new detection system using the SSMC method showed low sensitivity to plant (1→3)-β-D-glucan, which significantly improved the appearance of false positives, a recognized problem with the LAL method. Measurement of β-glucan levels by the SSMC method using recombinant β-glucan-binding proteins may be useful for the diagnosis of fungal infections. This study shows that this detection system could be a new alternative diagnostic method to the LAL method.

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A novel enzyme immunoassay for the measurement of plasma (1 → 3)-β-D-glucan levels

Cited by 7 publications

References 22 publications

A Candidemia Case Caused by a Novel Drug-Resistant Candida auris with the Y132F Mutation in Erg11 in Mainland China

A Candidemia Case Caused by a Novel Drug-Resistant Candida auris with the Y132F Mutation in Erg11 in Mainland China

Split Enzyme-Based Biosensors for Structural Characterization of Soluble and Insoluble β-Glucans

Development of a Highly Sensitive β-Glucan Detection System Using Scanning Single-Molecule Counting Method

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