Novel mouse monoclonal antibodies specifically recognizing β-(1→3)-D-glucan antigen

Novel mouse monoclonal antibodies specifically recognizing β-(1→3)-D-glucan antigen Full article

Journal

PLOS ONE
ISSN: 1932-6203

Output data

Year: 2019, Volume: 14, Number: 4, Article number : e0215535, Pages count : DOI: 10.1371/journal.pone.0215535

Authors

Matveev Andrey L. ¹ , Krylov Vadim B. ² , Khlusevich Yana A. ¹ , Baykov Ivan K. ¹ , Yashunsky Dmitry V. ² , Emelyanova Ljudmila A. ^1,3 , Tsvetkov Yury E. ² , Karelin Alexander A. ² , Bardashova Alevtina V. ¹ , Wong Sarah S.W. ^4,5 , Aimanianda Vishukumar ^4,5 , Latgé Jean Paul ⁴ , Tikunova Nina V. ^1,3 , Nifantiev Nikolay E. ²

Affiliations

1	Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, Novosibirsk, Russia
2	N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia
3	Novosibirsk State University, Novosibirsk, Russia
4	Aspergillus Unit, Institut Pasteur, Paris, France
5	Molecular Mycology Unit, Institut Pasteur, Paris, France

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.

Matveev A.L. , Krylov V.B. , Khlusevich Y.A. , Baykov I.K. , Yashunsky D.V. , Emelyanova L.A. , Tsvetkov Y.E. , Karelin A.A. , Bardashova A.V. , Wong S.S.W. , Aimanianda V. , Latgé J.P. , Tikunova N.V. , Nifantiev N.E.
Novel mouse monoclonal antibodies specifically recognizing β-(1→3)-D-glucan antigen
PLOS ONE. 2019. V.14. N4. e0215535 . DOI: 10.1371/journal.pone.0215535 WOS Scopus OpenAlex

≡ Web of science:	WOS:000465519100030
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