Genomic characterization of plant cell wall degrading enzymes and in silico analysis of xylanases and polygalacturonases of Fusarium virguliforme.
Genomic characterization of plant cell wall degrading enzymes and in silico analysis of xylanases and polygalacturonases of Fusarium virguliforme.
复制标题
DOI：
10.1186/s12866-016-0761-0
复制
发表时间：
2016-07-12
期刊：
影响因子：
4.2
通讯作者：
Hartman GL
中科院分区：
文献类型：
--
作者：
Chang HX;Yendrek CR;Caetano-Anolles G;Hartman GL
植物细胞壁降解酶（PCWDEs）是由植物病原体产生的降解植物细胞壁的碳水化合物活性酶（CAZy）的子集。为了抵消多氯WDE，植物释放多氯WDE抑制蛋白（PIP）以减少其影响。一些转基因植物表达的外源PIP与真菌糖苷水解酶（GH）11型木聚糖酶或GH 28型多聚半乳糖醛酸酶（PG）的相互作用，已被证明可以提高抗病性。然而，据报道，许多植物病原性镰刀菌物种逃避PIP抑制。大豆枯萎病菌是引起大豆猝死综合征（SDS）的一种土传病原菌。虽然F.虽然对玉米豆形黄单胞菌的PCWDEs进行了测序，但对玉米豆形黄单胞菌PCWDEs的研究还很有限。virguliforme。我们的目标是了解F.研究了外源PIP在理论上是否可以用于大豆以增强对F. viguliforme的抗性。virguliforme。F. virguliforme产生不同的CAZy降解纤维素和果胶，类似于其他坏死性和半活体营养植物病原真菌。然而，一些常见的植物病原真菌，如GH 29，GH 30，GH44，GH54，GH 62和GH 67的CAZy催化半纤维素酶在F. virguliforme。虽然这些CAZy家族的缺失可能被其他半纤维素酶补充，但F. virguliforme含有GH 131、多糖裂解酶（PL）9、PL 20和PL 22等在其他植物病原真菌或卵菌中未报道的独特家族。序列分析表明，F. virguliforme，FvXyn 11 A和FvXyn 11B具有允许木聚糖酶抑制剂蛋白I（XIP-1）结合的保守残基。结构模型表明，FvXyn 11 A和FvXyn 11B可以被XIP-I阻断，这是开发转基因大豆的良好候选。相比之下，一个GH 28 PG，FvPG 2，含有一个氨基酸取代，这是潜在的不兼容的豆多聚半乳糖醛酸酶抑制剂蛋白II（PvPGIP 2）。CAZy的鉴定和注释为深入了解F. virguliforme。FvXyn 11 A和FvXyn 11B的序列和结构分析表明，这两种木聚糖酶是保守的残基，允许XIP-I抑制，和表达的木聚糖酶在大豆根感染。我们推测，表达小麦XIP-Ⅰ的转基因大豆可能有助于发展对F. virguliforme。本文的在线版本（doi：10.1186/s12866-016-0761-0）包含补充材料，可供授权用户使用。
Plant cell wall degrading enzymes (PCWDEs) are a subset of carbohydrate-active enzymes (CAZy) produced by plant pathogens to degrade plant cell walls. To counteract PCWDEs, plants release PCWDEs inhibitor proteins (PIPs) to reduce their impact. Several transgenic plants expressing exogenous PIPs that interact with fungal glycoside hydrolase (GH)11-type xylanases or GH28-type polygalacturonase (PG) have been shown to enhance disease resistance. However, many plant pathogenic Fusarium species were reported to escape PIPs inhibition. Fusarium virguliforme is a soilborne pathogen that causes soybean sudden death syndrome (SDS). Although the genome of F. virguliforme was sequenced, there were limited studies focused on the PCWDEs of F. virguliforme. Our goal was to understand the genomic CAZy structure of F. viguliforme, and determine if exogenous PIPs could be theoretically used in soybean to enhance resistance against F. virguliforme. F. virguliforme produces diverse CAZy to degrade cellulose and pectin, similar to other necrotorphic and hemibiotrophic plant pathogenic fungi. However, some common CAZy of plant pathogenic fungi that catalyze hemicellulose, such as GH29, GH30, GH44, GH54, GH62, and GH67, were deficient in F. virguliforme. While the absence of these CAZy families might be complemented by other hemicellulases, F. virguliforme contained unique families including GH131, polysaccharide lyase (PL) 9, PL20, and PL22 that were not reported in other plant pathogenic fungi or oomycetes. Sequence analysis revealed two GH11 xylanases of F. virguliforme, FvXyn11A and FvXyn11B, have conserved residues that allow xylanase inhibitor protein I (XIP-I) binding. Structural modeling suggested that FvXyn11A and FvXyn11B could be blocked by XIP-I that serves as good candidate for developing transgenic soybeans. In contrast, one GH28 PG, FvPG2, contains an amino acid substitution that is potentially incompatible with the bean polygalacturonase-inhibitor protein II (PvPGIP2). Identification and annotation of CAZy provided advanced understanding of genomic composition of PCWDEs in F. virguliforme. Sequence and structural analyses of FvXyn11A and FvXyn11B suggested both xylanases were conserved in residues that allow XIP-I inhibition, and expression of both xylanases were detected during soybean roots infection. We postulate that a transgenic soybean expressing wheat XIP-I may be useful for developing root rot resistance to F. virguliforme. The online version of this article (doi:10.1186/s12866-016-0761-0) contains supplementary material, which is available to authorized users.