Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Novel mouse monoclonal antibodies specifically recognizing beta-(1 -> 3)-D-glucan antigen. / Matveev, Andrey L.; Krylov, Vadim B.; Khlusevich, Yana A. и др.
в: PLoS ONE, Том 14, № 4, 0215535, 25.04.2019, стр. e0215535.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Novel mouse monoclonal antibodies specifically recognizing beta-(1 -> 3)-D-glucan antigen
AU - Matveev, Andrey L.
AU - Krylov, Vadim B.
AU - Khlusevich, Yana A.
AU - Baykov, Ivan K.
AU - Yashunsky, Dmitry V.
AU - Emelyanova, Ljudmila A.
AU - Tsvetkov, Yury E.
AU - Karelin, Alexander A.
AU - Bardashova, Alevtina V.
AU - Wong, Sarah S.W.
AU - Aimanianda, Vishukumar
AU - Latgé, Jean Paul
AU - Tikunova, Nina V.
AU - Nifantiev, Nikolay E.
N1 - Publisher Copyright: © 2019 Matveev et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
PY - 2019/4/25
Y1 - 2019/4/25
N2 - β-(1!3)-D-Glucan is an essential component of the fungal cell wall. Mouse monoclonal antibodies (mAbs) against synthetic nona-β-(1!3)-D-glucoside conjugated with bovine serum albumin (BSA) were generated using hybridoma technology. The affinity constants of two selected mAbs, 3G11 and 5H5, measured by a surface plasmon resonance biosensor assay using biotinylated nona-β-(1!3)-D-glucan as the ligand, were approximately 11 nM and 1.9 nM, respectively. The glycoarray, which included a series of synthetic oligosaccharide derivatives representing β-glucans with different lengths of oligo-β-(1!3)-D-glucoside chains, demonstrated that linear tri-, penta- and nonaglucoside, as well as a β-(1!6)-branched octasaccharide, were recognized by mAb 5H5. By contrast, only linear oligo-β-(1!3)-D-glucoside chains that were not shorter than pentaglucosides (but not the branched octaglucoside) were ligands for mAb 3G11. Immunolabelling indicated that 3G11 and 5H5 interact with both yeasts and filamentous fungi, including species from Aspergillus, Candida, Penicillium genera and Saccharomyces cerevisiae, but not bacteria. Both mAbs could inhibit the germination of Aspergillus fumigatus conidia during the initial hours and demonstrated synergy with the antifungal fluconazole in killing C. albicans in vitro. In addition, mAbs 3G11 and 5H5 demonstrated protective activity in in vivo experiments, suggesting that these β-glucan-specific mAbs could be useful in combinatorial antifungal therapy.
AB - β-(1!3)-D-Glucan is an essential component of the fungal cell wall. Mouse monoclonal antibodies (mAbs) against synthetic nona-β-(1!3)-D-glucoside conjugated with bovine serum albumin (BSA) were generated using hybridoma technology. The affinity constants of two selected mAbs, 3G11 and 5H5, measured by a surface plasmon resonance biosensor assay using biotinylated nona-β-(1!3)-D-glucan as the ligand, were approximately 11 nM and 1.9 nM, respectively. The glycoarray, which included a series of synthetic oligosaccharide derivatives representing β-glucans with different lengths of oligo-β-(1!3)-D-glucoside chains, demonstrated that linear tri-, penta- and nonaglucoside, as well as a β-(1!6)-branched octasaccharide, were recognized by mAb 5H5. By contrast, only linear oligo-β-(1!3)-D-glucoside chains that were not shorter than pentaglucosides (but not the branched octaglucoside) were ligands for mAb 3G11. Immunolabelling indicated that 3G11 and 5H5 interact with both yeasts and filamentous fungi, including species from Aspergillus, Candida, Penicillium genera and Saccharomyces cerevisiae, but not bacteria. Both mAbs could inhibit the germination of Aspergillus fumigatus conidia during the initial hours and demonstrated synergy with the antifungal fluconazole in killing C. albicans in vitro. In addition, mAbs 3G11 and 5H5 demonstrated protective activity in in vivo experiments, suggesting that these β-glucan-specific mAbs could be useful in combinatorial antifungal therapy.
KW - CELL-WALL
KW - 3-AMINOPROPYL GLYCOSIDES
KW - IMMUNE-RESPONSE
KW - CANDIDA
KW - DESIGN
UR - http://www.scopus.com/inward/record.url?scp=85064876767&partnerID=8YFLogxK
U2 - 10.1371/journal.pone.0215535
DO - 10.1371/journal.pone.0215535
M3 - Article
C2 - 31022215
AN - SCOPUS:85064876767
VL - 14
SP - e0215535
JO - PLoS ONE
JF - PLoS ONE
SN - 1932-6203
IS - 4
M1 - 0215535
ER -
ID: 19649351