[1] Quesada-Ocampo L M, Parada-Rojas C H, Hansen Z, et al. Phytophthora capsici: recent progress on fundamental biology and disease management 100 years after its description [J]. Annual Review of Phytopathology, 2023, 61(1): 185−208. https://doi.org/10.1146/annurev-phyto-021622-103801 doi:  10.1146/annurev-phyto-021622-103801
[2] Barchenger D W, Lamour K H, Bosland P W. Challenges and strategies for breeding resistance in Capsicum annuum to the multifarious pathogen, Phytophthora capsici [J]. Frontiers in Plant Science, 2018, 9: 628. https://doi.org/10.3389/fpls.2018.00628 doi:  10.3389/fpls.2018.00628
[3] Lampugnani E R, Khan G A, Somssich M, et al. Building a plant cell wall at a glance [J]. Journal of Cell Science, 2018, 131(2): jcs207373. https://doi.org/10.1242/jcs.207373 doi:  10.1242/jcs.207373
[4] Yang C, Liu R, Pang J H, et al. Poaceae-specific cell wall-derived oligosaccharides activate plant immunity via OsCERK1 during Magnaporthe oryzae infection in rice [J]. Nature Communications, 2021, 12(1): 2178. https://doi.org/10.1038/s41467-021-22456-x doi:  10.1038/s41467-021-22456-x
[5] de Azevedo Souza C, Li S D, Lin A Z, et al. Cellulose-derived oligomers act as damage-associated molecular patterns and trigger defense-like responses [J]. Plant Physiology, 2017, 173(4): 2383−2398. https://doi.org/10.1104/pp.16.01680 doi:  10.1104/pp.16.01680
[6] Wang Y, Tyler B M, Wang Y C. Defense and counterdefense during plant-pathogenic oomycete infection [J]. Annual Review of Microbiology, 2019, 73(1): 667−696. https://doi.org/10.1146/annurev-micro-020518-120022 doi:  10.1146/annurev-micro-020518-120022
[7] Bradley E L, Ökmen B, Doehlemann G, et al. Secreted glycoside hydrolase proteins as effectors and invasion patterns of plant-associated fungi and oomycetes [J]. Frontiers in Plant Science, 2022, 13: 853106. https://doi.org/10.3389/fpls.2022.853106 doi:  10.3389/fpls.2022.853106
[8] Dora S, Terrett O M, Sánchez-Rodríguez C. Plant–microbe interactions in the apoplast: communication at the plant cell wall [J]. The Plant Cell, 2022, 34(5): 1532−1550. https://doi.org/10.1093/plcell/koac040 doi:  10.1093/plcell/koac040
[9] 屈阳, 沈加星, 靳晶豪, 等. 辣椒疫霉果胶裂解酶PcPL23的功能分析[J]. 植物病理学报, 2025, 55(5): 1070−1080. https://doi.org/10.13926/j.cnki.apps.001670 doi:  10.13926/j.cnki.apps.001670
[10]

Drula E, Garron M L, Dogan S, et al. The carbohydrate-active enzyme database: functions and literature [J]. Nucleic Acids Research, 2022, 50(D1): D571−D577. https://doi.org/10.1093/nar/gkab1045 doi:  10.1093/nar/gkab1045
[11]

Koga S Y, Miyahara T, Nishizaki Y, et al. Anthocyanin glucosylation mediated by a glycoside hydrolase family 3 protein in purple carrot [J]. The Plant Journal, 2024, 119(4): 1816−1829. https://doi.org/10.1111/tpj.16886 doi:  10.1111/tpj.16886
[12]

Choknud S, Prawisut A, Gorantla J N, et al. Expression, purification, characterization and glycoside production potential of rice β-d-glucan glucohydrolase I (OsExoI) [J]. Process Biochemistry, 2023, 127: 145−154. https://doi.org/10.1016/j.procbio.2023.02.015 doi:  10.1016/j.procbio.2023.02.015
[13]

Cai L N, Xu S N, Lu T, et al. Directed expression of halophilic and acidophilic β-glucosidases by introducing homologous constitutive expression cassettes in marine Aspergillus niger [J]. Journal of Biotechnology, 2019, 292: 12−22. https://doi.org/10.1016/j.jbiotec.2018.12.015 doi:  10.1016/j.jbiotec.2018.12.015
[14] 周洁. Sphingomonas sp. ATCC 31555家族3糖苷水解酶的功能研究及Fn3_like结构域的功能初探[D]. 南宁: 广西大学, 2022. https://doi.org/10.27034/d.cnki.ggxiu.2022.002151
[15]

Vasquez R, Mendoza R M, Cañas V A, et al. Characterization of recombinant GH 43 β-xylosidases and a GH 3 β-glucosidase from Levilactobacillus brevis for the hydrolysis of lignocellulose-derived substrates [J]. Journal of Microbiology and Biotechnology, 2026, 36: e2601031. https://doi.org/10.4014/jmb.2601.01031 doi:  10.4014/jmb.2601.01031
[16]

Ara K Z G, Månberger A, Gabriško M, et al. Characterization and diversity of the complete set of GH family 3 enzymes from Rhodothermus marinus DSM 4253 [J]. Scientific Reports, 2020, 10(1): 1329. https://doi.org/10.1038/s41598-020-58015-5 doi:  10.1038/s41598-020-58015-5
[17]

Thongpoo P, Mckee L S, Araújo A C, et al. Identification of the acid/base catalyst of a glycoside hydrolase family 3 (GH3) β-glucosidase from Aspergillus niger ASKU28 [J]. Biochimica et Biophysica Acta (BBA) - General Subjects, 2013, 1830(3): 2739−2749. https://doi.org/10.1016/j.bbagen.2012.11.014 doi:  10.1016/j.bbagen.2012.11.014
[18]

Kudo K, Watanabe A, Ujiie S, et al. Purification and enzymatic characterization of secretory glycoside hydrolase family 3 (GH3) aryl β-glucosidases screened from Aspergillus oryzae genome [J]. Journal of Bioscience and Bioengineering, 2015, 120(6): 614−623. https://doi.org/10.1016/j.jbiosc.2015.03.019 doi:  10.1016/j.jbiosc.2015.03.019
[19]

Morales-Cruz A, Amrine K C H, Blanco-Ulate B, et al. Distinctive expansion of gene families associated with plant cell wall degradation, secondary metabolism, and nutrient uptake in the genomes of grapevine trunk pathogens [J]. BMC Genomics, 2015, 16(1): 469. https://doi.org/10.1186/s12864-015-1624-z doi:  10.1186/s12864-015-1624-z
[20]

Pérez-Hernández A, González M, González C, et al. BcSUN1, a B. cinerea SUN-family protein, is involved in virulence [J]. Frontiers in Microbiology, 2017, 8: 35. https://doi.org/10.3389/fmicb.2017.00035 doi:  10.3389/fmicb.2017.00035
[21]

Resjö S, Brus M, Ali A, et al. Proteomic analysis of Phytophthora infestans reveals the importance of cell wall proteins in pathogenicity [J]. Molecular & Cellular Proteomics, 2017, 16(11): 1958−1971. https://doi.org/10.1074/mcp.M116.065656 doi:  10.1074/mcp.M116.065656
[22]

Judelson H S, Ah-Fong A M V, Aux G, et al. Gene expression profiling during asexual development of the late blight pathogen Phytophthora infestans reveals a highly dynamic transcriptome [J]. Molecular Plant-Microbe Interactions®, 2008, 21(4): 433−447. https://doi.org/10.1094/mpmi-21-4-0433 doi:  10.1094/mpmi-21-4-0433
[23]

Grenville-Briggs L J, Anderson V L, Fugelstad J, et al. Cellulose synthesis in Phytophthora infestans is required for normal appressorium formation and successful infection of potato [J]. The Plant Cell, 2008, 20(3): 720−738. https://doi.org/10.1105/tpc.107.052043 doi:  10.1105/tpc.107.052043
[24]

Takahashi M, Konishi T, Takeda T. Biochemical characterization of Magnaporthe oryzae β-glucosidases for efficient β-glucan hydrolysis [J]. Applied Microbiology and Biotechnology, 2011, 91(4): 1073−1082. https://doi.org/10.1007/s00253-011-3340-1 doi:  10.1007/s00253-011-3340-1
[25]

Kojima K, Sunagawa N, Mikkelsen N E, et al. Comparison of glycoside hydrolase family 3 β-xylosidases from basidiomycetes and ascomycetes reveals evolutionarily distinct xylan degradation systems [J]. Journal of Biological Chemistry, 2022, 298(3): 101670. https://doi.org/10.1016/j.jbc.2022.101670 doi:  10.1016/j.jbc.2022.101670
[26] 邢翠霞, 夏雨潇, 张伟欣, 等. 里氏木霉纤维素酶基因表达与调控[J]. 微生物学通报, 2024, 51(12): 4884−4898. https://doi.org/10.13344/j.microbiol.china.240519 doi:  10.13344/j.microbiol.china.240519
[27]

Wang Z W, Tyler B M, Liu X L. Protocol of Phytophthora capsici transformation using the CRISPR-Cas9 system[M]//Ma W B, Wolpert T. Plant pathogenic fungi and oomycetes. New York: Humana Press, 2018: 265-274. doi: 10.1007/978-1-4939-8724-5_17
[28]

Campbell I D, Spitzfaden C. Building proteins with fibronectin type III modules [J]. Structure, 1994, 2(5): 333−337. https://doi.org/10.1016/S0969-2126(00)00034-4 doi:  10.1016/S0969-2126(00)00034-4
[29]

Lin F P, Ma H Y, Lin H J, et al. Biochemical characterization of two truncated forms of amylopullulanase from Thermoanaerobacterium saccharolyticum NTOU1 to identify its enzymatically active region [J]. Applied Biochemistry and Biotechnology, 2011, 165(3/4): 1047−1056. https://doi.org/10.1007/s12010-011-9319-7 doi:  10.1007/s12010-011-9319-7
[30]

Huang X F, Nazarian F, Vincken J P, et al. A tandem CBM25 domain of α-amylase from Microbacterium aurum as potential tool for targeting proteins to starch granules during starch biosynthesis [J]. BMC Biotechnology, 2017, 17(1): 86. https://doi.org/10.1186/s12896-017-0406-x doi:  10.1186/s12896-017-0406-x
[31]

Brito N, Espino J J, González C. The endo-β-1, 4-xylanase Xyn11A is required for virulence in Botrytis cinerea [J]. Molecular Plant-Microbe Interactions®, 2006, 19(1): 25−32. https://doi.org/10.1094/mpmi-19-0025 doi:  10.1094/mpmi-19-0025
[32]

Gámez-Arjona F M, Vitale S, Voxeur A, et al. Impairment of the cellulose degradation machinery enhances Fusarium oxysporum virulence but limits its reproductive fitness [J]. Science Advances, 2022, 8(16): eabl9734. https://doi.org/10.1126/sciadv.abl9734 doi:  10.1126/sciadv.abl9734
[33]

Zhang X J, Duan P L, Shi S Q, et al. Global characterization of GH3 family glycoside hydrolase genes in Fusarium verticillioides and functional analysis of FvGH3-6 [J]. Frontiers in Microbiology, 2025, 16: 1543210. https://doi.org/10.3389/fmicb.2025.1543210 doi:  10.3389/fmicb.2025.1543210
[34]

Gui Y J, Chen J Y, Zhang D D, et al. Verticillium dahliae manipulates plant immunity by glycoside hydrolase 12 proteins in conjunction with carbohydrate-binding module 1 [J]. Environmental Microbiology, 2017, 19(5): 1914−1932. https://doi.org/10.1111/1462-2920.13695 doi:  10.1111/1462-2920.13695
[35]

Qin J X, Li B H, Zhou S Y. A novel glycoside hydrolase 74 xyloglucanase CvGH74A is a virulence factor in Coniella vitis [J]. Journal of Integrative Agriculture, 2020, 19(11): 2725−2735. https://doi.org/10.1016/s2095-3119(20)63254-3 doi:  10.1016/s2095-3119(20)63254-3
[36]

Tan X W, Hu Y Y, Jia Y L, et al. A conserved glycoside hydrolase family 7 cellobiohydrolase PsGH7a of Phytophthora sojae is required for full virulence on soybean [J]. Frontiers in Microbiology, 2020, 11: 1285. https://doi.org/10.3389/fmicb.2020.01285 doi:  10.3389/fmicb.2020.01285
[37]

Rogers L M, Kim Y K, Guo W J, et al. Requirement for either a host- or pectin-induced pectate lyase for infection of Pisum sativum by Nectria hematococca [J]. Proceedings of the National Academy of Sciences of the United States of America, 2000, 97(17): 9813−9818. https://doi.org/10.1073/pnas.160271497 doi:  10.1073/pnas.160271497
[38]

Quoc N B, Chau N N B. The role of cell wall degrading enzymes in pathogenesis of Magnaporthe oryzae [J]. Current Protein & Peptide Science, 2017, 18(10): 1019−1034. https://doi.org/10.2174/1389203717666160813164955 doi:  10.2174/1389203717666160813164955