Breaking-Down Barriers: Proposal of Using Cellulose Biosynthesis Inhibitors and Cellulase Enzyme as a Novel Treatment Modality for Vision Threatening Pythium Insidiosum Keratitis

References

• Gurnani B, Kaur K, Venugopal A., et al. Pythium insidiosum keratitis - A review. Indian J Ophthalmol. 2022;70(4):1107–1120. doi:10.4103/ijo.IJO_1534_21
   PubMed Web of Science ®Google Scholar
• Gurnani B, Christy J, Narayana S, Rajkumar P, Kaur K, Gubert J. Retrospective multifactorial analysis of Pythium keratitis and review of literature. Indian J Ophthalmol. 2021;69(5):1095–1101. doi:10.4103/ijo.IJO_1808_20
   PubMed Web of Science ®Google Scholar
• Gurnani B, Kaur K. Predicting prognosis based on regional prevalence, ulcer morphology and treatment strategy in vision-threatening Pythium insidiosum keratitis. Clin Ophthalmol. 2023;17:1307–1314. doi:10.2147/OPTH.S412274
   PubMed Web of Science ®Google Scholar
• Hasika R, Lalitha P, Radhakrishnan N, Rameshkumar G, Prajna NV, Srinivasan M. Pythium keratitis in South India: incidence, clinical profile, management, and treatment recommendation. Indian J Ophthalmol. 2019;67(1):42–47. doi:10.4103/ijo.IJO_445_18
   PubMed Web of Science ®Google Scholar
• Sahoo S, Mitra S, Mittal R, Behera HS, Das S. Use of different stains for microscopic evaluation for the diagnosis of Pythium keratitis. Indian J Med Microbiol. 2022;40(4):521–524. doi:10.1016/j.ijmmb.2022.08.003
   PubMed Web of Science ®Google Scholar
• Gurnani B, Kaur K, Agarwal S, et al. Pythium insidiosum Keratitis: past, Present, and Future. Ophthalmol Ther. 2022;11(5):1629–1653. doi:10.1007/s40123-022-00542-7
   PubMedGoogle Scholar
• Bagga B, Sharma S, Madhuri Guda SJ, et al. Leap forward in the treatment of Pythium insidiosum keratitis. Br J Ophthalmol. 2018;102(12):1629–1633. doi:10.1136/bjophthalmol-2017-311360
   PubMed Web of Science ®Google Scholar
• Vishwakarma P, Mohanty A, Kaur A, et al. Pythium keratitis: clinical profile, laboratory diagnosis, treatment, and histopathology features post-treatment at a tertiary eye care center in Eastern India. Indian J Ophthalmol. 2021;69(6):1544–1552. doi:10.4103/ijo.IJO_2356_20
   PubMed Web of Science ®Google Scholar
• Gurnani B, Kaur K, Kumar T. Commentary: current concepts, recent updates, and future treatment options for Pythium insidiosum keratitis. Indian J Ophthalmol. 2023;71(5):1874–1876. doi:10.4103/IJO.IJO_80_23
   PubMed Web of Science ®Google Scholar
• Popper ZA, Ralet M-C, Domozych DS. Plant and algal cell walls: diversity and functionality. Ann Bot. 2014;114(6):1043–1048. doi:10.1093/aob/mcu214
   PubMed Web of Science ®Google Scholar
• Picard K, Tirilly Y, Benhamou N. Cytological effects of cellulases in the parasitism of phytophthora parasitica by pythium oligandrum. Appl Environ Microbiol. 2000;66(10):4305–4314. doi:10.1128/AEM.66.10.4305-4314.2000
   PubMed Web of Science ®Google Scholar
• García-Angulo P, Alonso-Simón A, Encina A, Álvarez JM, Acebes JL. Cellulose biosynthesis inhibitors: comparative effect on bean cell cultures. Int J Mol Sci. 2012;13(3):3685–3702. doi:10.3390/ijms13033685
   PubMed Web of Science ®Google Scholar
• Gaastra W, Lipman LJ, De Cock AW, et al. Pythium insidiosum: an overview. Vet Microbiol. 2010;146(1–2):1–16. doi:10.1016/j.vetmic.2010.07.019
   PubMed Web of Science ®Google Scholar
• Lekhanont K, Chuckpaiwong V, Chongtrakool P, Aroonroch R, Vongthongsri A. Pythium insidiosum keratitis in contact lens wear: a case report. Cornea. 2009;28(10):1173–1177. doi:10.1097/ICO.0b013e318199fa41
   PubMed Web of Science ®Google Scholar
• Reinprayoon U, Permpalung N, Kasetsuwan N, Plongla R, Mendoza L, Chindamporn A. Lagenidium sp. ocular infection mimicking ocular pythiosis. J Clin Microbiol. 2013;51(8):2778–2780. doi:10.1128/JCM.00783-13
   PubMed Web of Science ®Google Scholar
• Gurnani B, Kaur K. Pythium Keratitis. In: StatPearls. Treasure Island (FL): StatPearls Publishing; 2023.
   Google Scholar
• Chatterjee S, Agrawal D, Gomase SN. Clinical differentiation of Pythium keratitis from fungal keratitis and development of a scoring system. Indian J Ophthalmol. 2022;70(10):3515–3521. doi:10.4103/ijo.IJO_870_22
   PubMed Web of Science ®Google Scholar
• Kalra P, Bagga B, Garg P. Pythium insidiosum keratitis: histopathology and rapid novel diagnostic staining technique. Cornea. 2018;37(3):e14. doi:10.1097/ICO.0000000000001463
   PubMed Web of Science ®Google Scholar
• Agarwal S, Iyer G, Srinivasan B, et al. Clinical profile, risk factors and outcome of medical, surgical and adjunct interventions in patients with Pythium insidiosum keratitis. Br J Ophthalmol. 2019;103(3):296–300. doi:10.1136/bjophthalmol-2017-311804
   PubMed Web of Science ®Google Scholar
• Cosgrove DJ. Building an extensible cell wall. Plant Physiol. 2022;189(3):1246–1277. doi:10.1093/plphys/kiac184
   PubMed Web of Science ®Google Scholar
• Tateno M, Brabham C, DeBolt S. Cellulose biosynthesis inhibitors - A multifunctional toolbox. J Exp Bot. 2016;67(2):533–542. doi:10.1093/jxb/erv489
   PubMed Web of Science ®Google Scholar
• Latgé JP. The cell wall: a carbohydrate armour for the fungal cell. Mol Microbiol. 2007;66(2):279–290. doi:10.1111/j.1365-2958.2007.05872.x
   PubMed Web of Science ®Google Scholar
• Blaschek W, Käsbauer J, Kraus J, Franz G. Pythium aphanidermatum: culture, cell-wall composition, and isolation and structure of antitumour storage and solubilised cell-wall (1----3),(1----6)-beta-D-glucans. Carbohydr Res. 1992;231:293–307. doi:10.1016/0008-6215(92)84026-o
   PubMed Web of Science ®Google Scholar
• Yamada M, Miyazaki T. Ultrastructure and chemical analysis of the cell wall of Pythium debaryanum. Jpn J Microbiol. 1976;20(2):83–91. doi:10.1111/j.1348-0421.1976.tb00913.x
   PubMedGoogle Scholar
• Natarajan R, Janani MK. Tissue Adhesive to Tackle a Terrible Infection in Vitro Inhibition of Pythium Insidiosum Keratitis Isolates By 1 N-Butyl-2-Cyanoacrylate. Ophthalmic Pathol. 2021;3(3):123.
   Google Scholar
• Kraehmer H, Laber B, Rosinger C, Schulz A. Herbicides as weed control agents: state of the art: i. Weed control research and safener technology: the path to modern agriculture. Plant Physiol. 2014;166(3):1119–1131. doi:10.1104/pp.114.241901
   PubMed Web of Science ®Google Scholar
• Grossmann K, Tresch S, Plath P. Triaziflam and Diaminotriazine derivatives affect enantioselectively multiple herbicide target sites. Z Naturforsch C J Biosci. 2001;56(7–8):559–569. doi:10.1515/znc-2001-7-814
   PubMedGoogle Scholar
• Brabham C, Lei L, Gu Y, Stork J, Barrett M, DeBolt S. Indaziflam herbicidal action: a potent cellulose biosynthesis inhibitor. Plant Physiol. 2014;166(3):1177–1185. doi:10.1104/pp.114.241950
   PubMed Web of Science ®Google Scholar
• Gu Y, Kaplinsky N, Bringmann M, et al. Identification of a cellulose synthase-associated protein required for cellulose biosynthesis. Proc Natl Acad Sci U S A. 2010;107(29):12866–12871. doi:10.1073/pnas.1007092107
   PubMed Web of Science ®Google Scholar
• Drakakaki G, van de Ven W, Pan S, et al. Isolation and proteomic analysis of the SYP61 compartment reveal its role in exocytic trafficking in Arabidopsis [published correction appears in Cell Res. 2023 Sep 21;:]. Cell Res. 2012;22(2):413–424. doi:10.1038/cr.2011.129
   PubMed Web of Science ®Google Scholar
• Xia Y, Lei L, Brabham C, et al. Acetobixan, an inhibitor of cellulose synthesis identified by microbial bioprospecting. PLoS One. 2014;9(4):e95245. doi:10.1371/journal.pone.0095245
   PubMed Web of Science ®Google Scholar
• Deguchi S, Degaki H, Taniguchi I, Koga T. Deep-sea-inspired chemistry: a hitchhiker’s guide to the bottom of the ocean for chemists. Langmuir. 2023;39(23):7987–7994. doi:10.1021/acs.langmuir.3c00516
   PubMed Web of Science ®Google Scholar
• Kumar R, Singh S, Singh OV. Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J Ind Microbiol Biotechnol. 2008;35(5):377–391. doi:10.1007/s10295-008-0327-8
   PubMed Web of Science ®Google Scholar
• Dhiman TR, Zaman MS, Gimenez RR, Walters JL, Treacher R. Performance of dairy cows fed forage treated with fibrolytic enzymes prior to feeding. Anim Feed Sci Technol. 2002;101(1):115–125.
   Web of Science ®Google Scholar
• Godfrey T, West S. “Textiles”, in Industrial Enzymology. 2nd ed. London, UK: Macmillan Press; 1996:360–371.
   Google Scholar
• Bhat MK. Cellulases and related enzymes in biotechnology. Biotechnol Adv. 2000;18(5):355–383.
   PubMed Web of Science ®Google Scholar
• Sukumaran RK, Singhania RR, Pandey A. Microbial cellulases—production, applications and challenges. J Sci Ind Res. 2005;64(11):832–844.
   Web of Science ®Google Scholar
• Hebeish A, Ibrahim NA. The impact of frontier sciences on textile industry. Colourage. 2007;54:41–55.
   Google Scholar
• Galante YM, DeConti A, Monteverdi R. “Application of Trichoderma enzymes in food and feed industries”, in Tri- choderma and Gliocladium—Enzymes. In: Harman GF, Kubicek CP, editors. Biological Control and Commercial Applications. Vol. 2. London, UK: Taylor & Francis; 1998:311–326.
   Google Scholar
• Balouiri M, Sadiki M, Ibnsouda SK. Methods for in vitro evaluating antimicrobial activity: a review. J Pharm Anal. 2016;6(2):71–79.
   PubMed Web of Science ®Google Scholar
• Dogan C, Aygun G, Bahar-Tokman H, et al. In vitro antifungal effect of acrylic corneal glue (N-Butyl-2-Cyanoacrylate). Cornea. 2019;38(12):1563–1567.
   PubMed Web of Science ®Google Scholar
• Petrikkou E, Rodríguez-Tudela JL, Cuenca-Estrella M, Gómez A, Molleja A, Mellado E. Inoculum standardization for antifungal susceptibility testing of filamentous fungi pathogenic for humans. J Clin Microbiol. 2001;39(4):1345–1347. doi:10.1128/JCM.39.4.1345-1347.2001
   PubMed Web of Science ®Google Scholar
• Romero IL, Malta JB, Silva CB, Mimica LM, Soong KH, Hida RY. Antibacterial properties of cyanoacrylate tissue adhesive: does the polymerization reaction play a role? Indian J Ophthalmol. 2009;57(5):341–344. doi:10.4103/0301-4738.55065
   PubMed Web of Science ®Google Scholar
• Henrissat B, Teeri TT, Warren RAJ. A scheme for designating enzymes that hydrolyse the polysaccharides in the cell walls of plants. FEBS Lett. 1998;425(2):352–354.
   PubMed Web of Science ®Google Scholar
• Sang-Mok L, Koo YM. Pilot-scale production of cellulase using Trichoderma reesei Rut C-30 in fed-batch mode. J Microbiol Biotechnol. 2001;11(2):229–233.
   Web of Science ®Google Scholar
• Kuhad RC, Manchanda M, Singh A. Hydrolytic potential of extracellular enzymes from a mutant strain of Fusarium oxysporum. Bioprocess Eng. 1999;20(2):133–135.
   Google Scholar
• Herbert R, Sharp R. Chapman and Hall. Molecular Biology and Biotechnology of Extremophiles; 1992.
   Google Scholar
• Kubicek CP, Penttila ME. Regulation of production of plant polysaccharide degrading enzymes by Trichoderma. In: Harman E, Kubicek CP, editors. In Trichoderma and Gliocladium. London: Taylor & Francis Ltd; 1998:49–72.
   Google Scholar
• Aro N, Ilmen M, Saloheimo A, Penttila M. ACEI is a repressor of cellulase and xylanase genes of Trichoderma reesei. Appl Environ Microbiol. 2002;69:56–65.
   Web of Science ®Google Scholar
• Strauss J, Mach RL, Zeilinger S, et al. Cre1, the carbon catabolites repressor protein from Trichoderma reesei. FEBS Letts. 1995;376:103–107.
   PubMed Web of Science ®Google Scholar
• Narendja FM, Davis MA, Hynes MJ. An CF, the CCAAT binding complex of Aspergillus nidulans, is essential for the formation of a DNAse I-hypersensitive site in the 50 region of the amdS gene. Mol Cell Biol. 1999;19:6523–6531.
   PubMed Web of Science ®Google Scholar
• Suto M, Tomita F. Induction and catabolic repression mechanisms of cellulase in fungi. J Biosci Bioeng. 2001;92:305–311.
   PubMed Web of Science ®Google Scholar
• Inoue T, Moriya S, Ohkuma M, Kudo T. Molecular cloning and characterization of a cellulase gene from a symbiotic protist of the lower termite, Coptotermes formosanus. Gene. 2005;349:67–75.
   PubMed Web of Science ®Google Scholar
• Silano V, Barat Baviera JM, Bolognesi C, et al. EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP). Safety evaluation of the food enzyme cellulase from Trichoderma reesei (strain DP-Nzc36). EFSA J. 2019;17:10.
   Web of Science ®Google Scholar
• Worden N, Wilkop TE, Esteve VE, et al. CESA TRAFFICKING INHIBITOR inhibits cellulose deposition and interferes with the trafficking of cellulose synthase complexes and their associated proteins KORRIGAN1 and POM2/CELLULOSE SYNTHASE INTERACTIVE PROTEIN1. Plant Physiol. 2015;167(2):381–393. doi:10.1104/pp.114.249003
   PubMed Web of Science ®Google Scholar
• Aro N, Saloheimo A, Ilmen M, Penttila M. ACEII, a novel transcriptional activator involved in regulation of cellulase and xylanase genes of Trichoderma reesei. J Biol Chem. 2001;276:24309–24314.
   PubMed Web of Science ®Google Scholar
• Xin X, Lei L, Zheng Y, et al. Cellulose synthase interactive1- and microtubule-dependent cell wall architecture is required for acid growth in Arabidopsis hypocotyls. J Exp Bot. 2020;71(10):2982–2994. doi:10.1093/jxb/eraa063
   PubMed Web of Science ®Google Scholar