Expression and characterization of two chitinases with synergistic effect and antifungal activity from Xenorhabdus nematophila

Jia Liu1, Ziyan Nangong1, Jie Zhang2, Ping Song1, Yin Tang1, Yuan Gao1, Qinying Wang1
1College of Plant Protection, Hebei Agricultural University, Baoding, 071001, Hebei, China
2Luanping State-Owned Forestry Farm Management of Chengde City, Chengde, 068250, China

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Ajit NS, Verma R, Shanmugam V (2006) Extracellular chitinases of fluorescent pseudomonads antifungal to Fusarium oxysporum f. sp. dianthi causing carnation wilt. Curr Microbiol 52:310–316. https://doi.org/10.1007/s00284-005-4589-3

Arora N, Ahmad T, Rajagopal R, Bhatnagar RK (2003) A constitutively expressed 36 kDa exochitinase from Bacillus thuringiensis HD-1. Biochem Biophys Res Commun 307:620–625. https://doi.org/10.1016/s0006-291x(03)01228-2

Bhattacharya D, Nagpure A, Gupta RK (2007) Bacterial chitinases: properties and potential. Crit Rev Biotechnol 27:21–28. https://doi.org/10.1080/07388550601168223

Bhuvanachandra B, Madhuprakash J, Podile AR (2018) Active-site mutations improved the transglycosylation activity of Stenotrophomonas maltophilia chitinase A. Bba Proteins Proteom 1866:407–414. https://doi.org/10.1016/j.bbapap.2017.12.003

Bravo A, Soberon M (2008) How to cope with insect resistance to Bt toxins? Trends Biotechnol 26:573–579. https://doi.org/10.1016/j.tibtech.2008.06.005

Busby JN, Landsberg MJ, Simpson RM, Jones SA, Hankamer B, Hurst MR, Lott JS (2012) Structural analysis of Chi1 chitinase from Yen-Tc: the multisubunit insecticidal ABC toxin complex of Yersinia entomophaga. J Mol Biol 415:359–371. https://doi.org/10.1016/j.jmb.2011.11.018

Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B (2009) The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res 37:233–238. https://doi.org/10.1093/nar/gkn663

Downing KJ, Thomson JA (2000) Introduction of the Serratia marcescens chiA gene into an endophytic Pseudomonas fluorescens for the biocontrol of phytopathogenic fungi. Can J Microbiol 46:363–369. https://doi.org/10.1139/w99-147

Fu X, Yan Q, Yang S, Yang X, Guo Y, Jiang Z (2014) An acidic, thermostable exochitinase with β-N-acetylglucosaminidase activity from Paenibacillus barengoltzii converting chitin to N-acetylglucosamine. Biotechnol Biofuels 7:174–185. https://doi.org/10.1186/s13068-014-0174-y

Gao L, Sun J, Secundo F, Gao X, Xue C, Mao X (2018) Cloning, characterization and substrate degradation mode of a novel chitinase from Streptomyces albolongus ATCC 27414. Food Chem 261:329–336. https://doi.org/10.1016/j.foodchem.2018.04.068

García-Fraga B, Da Silva Abigail F, López-Seijas J, Sieiro C (2015) A novel family 19 chitinase from the marine-derived Pseudoalteromonas tunicata CCUG 44952T: Heterologous expression, characterization and antifungal activity. Biochem Eng J 93:84–93. https://doi.org/10.1016/j.bej.2014.09.014

Hjort K, Presti I, Elvang A, Marinelli F, Sjoling S (2014) Bacterial chitinase with phytopathogen control capacity from suppressive soil revealed by functional metagenomics. Appl Microbiol Biotechnol 98:2819–2828. https://doi.org/10.1007/s00253-013-5287-x

Hong SH, Song YS, Seo DJ, Kim KY, Jung WJ (2017) Antifungal activity and expression patterns of extracellular chitinase and β-1,3-glucanase in Wickerhamomyces anomalus EG2 treated with chitin and glucan. Microb Pathog 110:159–164. https://doi.org/10.1016/j.micpath.2017.06.038

Itoh T, Hibi T, Fujii Y, Sugimoto I, Fujiwara A, Suzuki F, Iwasaki Y, Kim JK, Taketo A, Kimotoa H (2013) Cooperative degradation of chitin by extracellular and cell surface-expressed chitinases from Paenibacillus sp. strain FPU-7. Appl Environ Microbiol 79:7482–7490. https://doi.org/10.1128/AEM.02483-13

Joshi MC, Sharma A, Kant S, Birah A, Gupta GP, Khan SR, Bhatnagar R, Banerjee N (2008) An insecticidal GroEL protein with chitin binding activity from Xenorhabdus nematophila. J Biol Chem 283:28287–28296. https://doi.org/10.1074/jbc.M804416200

Juárez-Hernández EO, Casados-Vázquez LE, Brieba LG, Torres-Larios A, Jimenez-sandoval P, Barboza-Corona JE (2019) The crystal structure of the chitinase ChiA74 of Bacillus thuringiensis has a multidomain assembly. Sci Rep 9:2591–2601. https://doi.org/10.1038/s41598-019-39464-z

Kirubakaran SI, Sakthivel N (2007) Cloning and overexpression of antifungal barley chitinase gene in Escherichia coli. Protein Expr Purif 52:159–166. https://doi.org/10.1016/j.pep.2006.08.012

Landsberg MJ, Jonesb SA, Rothnagela R, Busbyc JN, Marshallb SDG, Simpsond RM, Lottc JS, Hankamera B, Hurstb MRH (2011) 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proc Natl Acad Sci USA 108:20544–20549. https://doi.org/10.1073/pnas.1111155108

Lee SC, Stoilova-Mcphie S, Baxter L, Fülöp V, Henderson J, Rodger A, Roper DI, Scott DJ, Smith CJ, Morgan JAW (2007) Structural characterisation of the insecticidal toxin XptA1, reveals a 1.15 MDa tetramer with a cage-like structure. J Mol Biol 366:1558–1568. https://doi.org/10.1016/j.jmb.2006.12.057

Lertcanawanichakul M, Wiwat C, Bhumiratana A, Dean DH (2004) Expression of chitinase-encoding genes in Bacillus thuringiensis and toxicity of engineered B. thuringiensis subsp. aizawai toward Lymantria dispar larvae. Curr Microbiol 48:175–181. https://doi.org/10.1007/s00284-003-4119-0

Liu D, Cai J, Xie C, Liu C, Chen Y (2010) Purification and partial characterization of a 36-kDa chitinase from Bacillus thuringiensis subsp. colmeri, and its biocontrol potential. Enzyme and Microbial Technology 46:252–256. https://doi.org/10.1016/j.enzmictec.2009.10.007

Liu M, Cai QX, Liu HZ, Zhang BH, Yan JP, Yu ZM (2002) Chitinolytic activities in Bacillus thuringiensis and their synergistic effects on larvicidal activity. J Appl Microbiol 93:374–379. https://doi.org/10.1046/j.1365-2672.2002.01693.x/full

Lu Y, Wang N, He J, Li Y, Gao X, Huang L, Yan X (2018) Expression and characterization of a novel chitinase with antifungal activity from a rare actinomycete, Saccharothrix yanglingensis Hhs. 015. Protein Expr Purif 143:45–51. https://doi.org/10.1016/j.pep.2017.10.013

Mander P, Cho SS, Choi YH, Panthi S, Choi YS, Kim HM, Yoo JC (2016) Purification and characterization of chitinase showing antifungal and biodegradation properties obtained from Streptomyces anulatus CS242. Arch Pharm Res 39:878–886. https://doi.org/10.1007/s12272-016-0747-3

Mehmood MA, Xiao X, Hafeez FY, Gai Y, Wang F (2010) Molecular characterization of an endochitinase from Bacillus thuringiensis subsp. konkukian. World J Microbiol Biotechnol 26:2171–2178. https://doi.org/10.1007/s11274-010-0401-z

Mehmood MA, Xiao X, Hafeez FY, Gai Y, Wang F (2011) Molecular characterization of the modular chitin binding protein Cbp50 from Bacillus thuringiensis serovar konkukian. Anton Leeuw Int J G 100:445–453. https://doi.org/10.1007/s10482-011-9601-2

Miller GL (1959) Use of dinitrosaIicyIic acid reagent for determination of reducing sugar. Anal chem 31:426–428. https://doi.org/10.1021/ac60147a030

Morgan JA, Sergeant M, Ellis D, Ousley M, Jarrett P (2001) Sequence analysis of insecticidal genes from Xenorhabdus nematophilus PMFI296. Appl Environ Microbiol 67:2062–2069. https://doi.org/10.1128/AEM.67.5.2062-2069.2001

Patil RS, Ghormade V, Deshpande MV (2000) Chitinolytic enzymes: an exploration. Enzyme and Microbial Technology 26:473–483. https://doi.org/10.1016/s0141-0229(00)00134-4

Shehataa AN, Aty AAAE, Darwishc DA, Wahabb WAA, Faten AM (2018) Purification, physicochemical and thermodynamic studies of antifungal chitinase with production of bioactive chitosan-oligosaccharide from newly isolated Aspergillus griseoaurantiacus KX010988. Int J Biol Macromol 107:990–999. https://doi.org/10.1016/j.ijbiomac.2017.09.071

Toufiq N, Tabassum B, Bhatti MU, Khan A, Tariq M, Shahid N, Nasir IA, Husnain T (2018) Improved antifungal activity of barley derived chitinase I gene that overexpress a 32 kDa recombinant chitinase in Escherichia coli host. Braz J Microbiol 49:414–421. https://doi.org/10.1016/j.bjm.2017.05.007

Wang SL, Peng JH, Liang TW, Liu KC (2008) Purification and characterization of a chitosanase from Serratia marcescens TKU011. Carbohyd Res 343:1316–1323. https://doi.org/10.1016/j.carres.2008.03.030

Wiwat C, Thaithanun S, Pantuwatana S, Bhumiratana A (2000) Toxicity of chitinase-producing Bacillus thuringiensis ssp kurstaki HD-1 (G) toward Plutella xylostella. J Invertebr Pathol 76:270–277. https://doi.org/10.1006/jipa.2000.4976

Yang S, Fu X, Yan Q, Guo Y, Liu Z, Jiang Z (2016) Cloning, expression, purification and application of a novel chitinase from a thermophilic marine bacterium Paenibacillus barengoltzii. Food Chem 192:1041–1048. https://doi.org/10.1016/j.foodchem.2015.07.092

Yang Q, Zhang J, Li T, Liu S, Song P, Nangong Z, Wang Q (2017) PirAB protein from Xenorhabdus nematophila HB310 exhibits a binary toxin with insecticidal activity and cytotoxicity in Galleria mellonella. J Invertebr Pathol 148:43–50. https://doi.org/10.1016/j.jip.2017.04.007

Zarei M, Aminzadeh S, Zolgharnein H, Safahieh A, Daliri M, Noghabi KA, Ghoroghi A, Motallebi A (2011) Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A. Braz J Microbiol 42:1017–1029