Fusarium graminearum produces different xylanases causing host cell death that is prevented by the xylanase inhibitors XIP-I and TAXI-III in wheat

Tundo, Silvio; Moscetti, Ilaria; Faoro, Franco; Lafond, Mickaël; Giardina, Thierry; Favaron, Francesco; Sella, Luca; D’Ovidio, R.

doi:10.1016/j.plantsci.2015.09.002

Cited by 30 publications

(38 citation statements)

References 37 publications

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“…Igawa et al (2004) observed over-expression of TAXI-IB/III and TAXI-IIB/IV in wheat leaves after the infection by the fungus Blumeria graminis. Tundo et al (2015) confirmed the dual function of XIs, namely TAXI-III and XIP. These proteins competitively inhibited F. graminearum xylanase activity (GH11) and also prevented host cell death activities caused by xylanases.…”

Section: Triticum Aestivum Xylanase Inhibitor (Taxi)supporting

confidence: 53%

“…It has been assumed that XIP production is involved in plant defence responses via methyl jasmonate signal pathway (Zhan et al, 2017a;Zhan et al, 2017b). Payan et al 2004 (Tundo et al, 2015). Osxip expression in transgenic plants was mainly observed in the shoot and root tissues after the exposure of two-week-old seedlings of rice to Nilaparvata lugens (Sun et al, 2018).…”

Section: Xylanase Inhibitor Protein (Xip)mentioning

confidence: 99%

“…Osxip expression in transgenic plants was mainly observed in the shoot and root tissues after the exposure of two-week-old seedlings of rice to Nilaparvata lugens (Sun et al, 2018). Some researchers suggest that transgenic plants with over-expression of XIP may be more resistant to pathogens than wild-type plants (Hou et al, 2014;Tundo et al, 2015;Zhan et al, 2017a).…”

Section: Xylanase Inhibitor Protein (Xip)mentioning

confidence: 99%

“…TAXI protein consists of two β-barrel domains with several helical segments divided by an extended cleft (Dornez et al, 2010). TAXI inhibitor binds at the active site of xylanase, resulting in competitive inhibition of the enzyme (Tundo et al, 2015). TAXI-I was able to inhibit recombinant xylanase from Penicillium funiculosum (GH11) although it did not inhibit recombinant xylanase from P. occitanis (GH11).…”

Section: Triticum Aestivum Xylanase Inhibitor (Taxi)mentioning

confidence: 99%

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Microbial xylanases and their inhibition by specific proteins in cereals

Chmelová

Škulcová

Ondrejovič

2019

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Arabinoxylans (AXs) belong to the components of plant cells which are mainly degraded by microbial xylanases during colonization of grain by phytopathogens. For the defence, cereals contain proteinaceous xylanase inhibitors (XIs), namely xylanase inhibitor protein (XIP), Triticum aestivum xylanase inhibitor (TAXI) and thaumatin-like xylanase inhibitor (TLXI). Their presence in cereals in high levels can be a serious problem in different industrial applications. XIs regulate AX hydrolysis and participate in plant defence mechanisms. XIs have various specificity against microbial xylanases from the glycoside hydrolase (GH) families of GH10 and GH11. Therefore, this review brings new information about the function of XIs as defence responses to pathogen infection of plants and as a problem in plant material processing in different industrial applications.

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Section: Triticum Aestivum Xylanase Inhibitor (Taxi)supporting

confidence: 53%

Section: Xylanase Inhibitor Protein (Xip)mentioning

confidence: 99%

Section: Xylanase Inhibitor Protein (Xip)mentioning

confidence: 99%

Section: Triticum Aestivum Xylanase Inhibitor (Taxi)mentioning

confidence: 99%

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Microbial xylanases and their inhibition by specific proteins in cereals

Chmelová

Škulcová

Ondrejovič

2019

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“…The interactions between various xylanases and inhibitors are complicated. It was demonstrated that the well‐studied XIP type inhibitor XIP‐I competitively inhibited fungi‐derived xylanases, regardless of GH10 or GH11, yet it could not act on the bacteria‐derived xylanases (Tundo et al ., ). Surprisingly, several xylanases from fungal sources were exceptions, being not inhibited by XIP‐I.…”

Section: Introductionmentioning

confidence: 97%

Characteristics of a XIP‐resistant xylanase from Neocallimastix sp. GMLF1 and its advantage in barley malt saccharification

Zhu

Xie

et al. 2019

Int J of Food Sci Tech

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The well-studied xylanase inhibitor protein (XIP-I) regularly inhibits fungi-derived xylanases, yet some fungal xylanases are not inhibited by XIP-I. Based on the sequence alignment with the known XIP-I resistant NpXyn11A from Neocallimastix patriciarum, a new annotated xylanase from ruminal fungus Neocallimastix sp. GMLF1 was found, noted as Xyn1B, which shared 77.8% of sequence identity with NpXyn11A and was proved to be resistant to XIP-I. To evaluate the performance of a XIP resistant xylanase used in barley malt saccharification, a XIP-I sensitive xylanase ThXyn1 from Trichoderma harzianum was chosen as a control. The barley malt saccharification experiment was carried out on the condition with or without extra XIP-I added. The results showed that Xyn1B displayed only slight difference in presence and absence of added XIP-I, with the difference of xylose released (DX) and the difference of mash clarity (DA) being 0.17 g L À1 (P > 0.05) and 0.007 (P > 0.05), respectively; while those for ThXyn1 group reached 0.96 g L À1 (P < 0.01) and 0.095 (P < 0.05), indicating that XIP-I did not adversely affect Xyn1B's function, but did affect ThXyn1's function. Our work for the first time suggested that a xylanase with resistance to xylanase inhibitor proteins might have an advantage in barley malt saccharification over an inhibitor sensitive xylanase.

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