The Atomic Structure of the Virally Encoded Antifungal Protein, KP6

Allen, Aron; Chatt, Elizabeth C.; Smith, Thomas J.

doi:10.1016/j.jmb.2012.11.033

Cited by 18 publications

(25 citation statements)

References 32 publications

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“…Four SSPs (Ecp4, Ecp7, Ecp29 [CTR], and Ecp30) were consistently predicted to have structural homology to proteins with a b/g-crystallin fold, including the plant antimicrobial protein MiAMP1 from Macadamia integrifolia (1C01) (McManus et al 1999) and the yeast killer toxin WmKT from Williopsis mrakii (1WKT) (Antuch et al 1996). Three other SSPs (Ecp28-1, Ecp28-2, and Ecp28-3) were consistently predicted to have structural homology to one or both the a and b subunits of KP6 (1KP6 and 4GVB), a virus-encoded antifungal killer toxin with an a/b-sandwich fold secreted by the fungal corn smut pathogen Ustilago maydis (Allen et al 2013a;Li et al 1999). Notably, the NTR of Ecp29 was found to share sequence homology with Ecp28-1, Ecp28-2, and Ecp28-3, suggesting that it, too, adopts a KP6-like fold.…”

Section: Resultsmentioning

confidence: 99%

“…In KP6b, these six Cys residues are known to form three intramolecular disulphide bonds (Cys9-Cys74, Cys11-Cys64, and Cys29-Cys46) (Allen et al 2013a). The predicted Ecp28-3 structure, which was modeled using KP6b as a template, suggests that the three conserved Cys pairs (Cys7/Cys76, Cys9/Cys66, and Cys26/Cys47) form intramolecular disulphide bonds.…”

Section: Resultsmentioning

confidence: 99%

“…KP6 is translated as a single polypeptide but is processed into two subunits, KP6a and KP6b, by a kexin protease during passage through the ER-Golgi secretory pathway. Both subunits adopt a core a/b-sandwich fold (Allen et al 2013a;Li et al 1999). KP6 functions only as a heterodimer, with both subunits required for cytotoxic activity (Peery et al 1987).…”

Section: Discussionmentioning

confidence: 99%

“…Assays in which sensitive U. maydis cells were treated with KP6a or KP6b alone or with one subunit after another, but with a washing step in between, strongly suggest that KP6a is responsible for targeting the cell, while KP6b is cytotoxic (Peery et al 1987). The specific mode of action for KP6, however, remains unclear, although it is thought that KP6a forms strong interactions with cell-wall carbohydrates or membrane-associated proteins of the target cell, with KP6b subsequently recruited to the plasma membrane or imported to an intracellular target to cause cell lysis (Allen et al 2013a;Steinlauf et al 1988). Interestingly, limited amino-acid sequence homology was identified between Ecp29 (NTR) and members of the Ecp28 family, suggesting that Ecp29 (NTR) also adopts a KP6-like fold.…”

Section: Discussionmentioning

confidence: 99%

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Specific Hypersensitive Response–Associated Recognition of New Apoplastic Effectors from Cladosporium fulvum in Wild Tomato

Mesarich

Ökmen

Rövenich

et al. 2018

MPMI

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Tomato leaf mold disease is caused by the biotrophic fungus Cladosporium fulvum. During infection, C. fulvum produces extracellular small secreted protein (SSP) effectors that function to promote colonization of the leaf apoplast. Resistance to the disease is governed by Cf immune receptor genes that encode receptor-like proteins (RLPs). These RLPs recognize specific SSP effectors to initiate a hypersensitive response (HR) that renders the pathogen avirulent. C. fulvum strains capable of overcoming one or more of all cloned Cf genes have now emerged. To combat these strains, new Cf genes are required. An effectoromics approach was employed to identify wild tomato accessions carrying new Cf genes. Proteomics and transcriptome sequencing were first used to identify 70 apoplastic in planta-induced C. fulvum SSPs. Based on sequence homology, 61 of these SSPs were novel or lacked known functional domains. Seven, however, had predicted structural homology to antimicrobial proteins, suggesting a possible role in mediating antagonistic microbe-microbe interactions in planta. Wild tomato accessions were then screened for HR-associated recognition of 41 SSPs, using the Potato virus X-based transient expression system. Nine SSPs were recognized by one or more accessions, suggesting that these plants carry new Cf genes available for incorporation into cultivated tomato.Leaf mold disease of tomato (Solanum lycopersicum) is caused by the biotrophic Dothideomycete fungal pathogen Cladosporium fulvum (syn. Passalora fulva and Fulvia fulva) (Thomma et al. 2005). The fungus likely originated in South America, the center of origin for tomato (Jenkins 1948), with Nucleotide sequence data is available in the GenBank database under the following accession numbers: Ecp6, KX943112; Ecp7, KX943113; Ecp8, KX943038; Ecp9-1, KX943041; Ecp9-2, KX943114; Ecp9-3, KX943115; Ecp9-4, KX943116; Ecp9-5, KX943117; Ecp9-6, KX943118; Ecp9-7, KX943119; Ecp9-8, KX943120; Ecp9-9, KX943081; Ecp10-1, KX943046; Ecp10-2, KX943063; Ecp10-3, KX943121; Ecp11-1, KX943050; Ecp12, KX943058; Ecp13, KX943065; Ecp14-1, KX943087; Ecp14-2, KX943122; Ecp15, KX943091; Ecp16, KX943080; Ecp17, KX943051; Ecp18, KX943035; Ecp19-1, KX943036; Ecp19-2, KX943048; Ecp20-1, KX943037; Ecp20-2, KX943057; Ecp20-3, KX943096; Ecp21-1, KX943039; Ecp22, KX943040; Ecp23, KX943044; Ecp24-1, KX943045; Ecp24-2, KX943094; Ecp25, KX943047; Ecp26, KX943052; Ecp27, KX943054; Ecp28-1, KX943056; Ecp28-2, KX943088; Ecp28-3, KX943090; Ecp29, KX943103; Ecp30, KX943076; Ecp31, KX943059; Ecp32-1, KX943062; Ecp32-2, KX943101; Ecp33, KX943066; Ecp34, KX943067; Ecp35, KX943068; Ecp36-1, KX943069; Ecp37, KX943072; Ecp38, KX943073; Ecp39, KX943074; Ecp40, KX943079; Ecp41, KX943082; Ecp42, KX943083; Ecp43-1, KX943089; Ecp44, KX943092; Ecp45, KX943093; Ecp46, KX943095; Ecp47, KX943097; Ecp48, KX943098; Ecp49-1, KX943099; Ecp50-1, KX943100; Ecp51, KX943102; Ecp52, KX943104; Ecp53-1, KX943105; Ecp54-1, KX943107; Ecp55, KX943108; Ecp56, KX943110; Ecp57-1,

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Specific Hypersensitive Response–Associated Recognition of New Apoplastic Effectors from Cladosporium fulvum in Wild Tomato

Mesarich

Ökmen

Rövenich

et al. 2018

MPMI

View full text Add to dashboard Cite

show abstract

“…Four ipiSSPs (Ecp4, Ecp7, CfCE44 and CfCE72 [CTR]) were consistently predicted to have structural homology to proteins with a β/γ-crystallin fold, including the plant antimicrobial protein MiAMP1 from Macadamia integrifolia (ID: 1C01) (McManus et al, 1999), and the yeast killer toxin WmKT from Williopsis mrakii (ID: 1WKT) (Antuch et al, 1996) (Table S2). A further three ipiSSPs (CfCE24, CfCE56 and CfCE58) were consistently predicted to have structural homology to the α and/or β subunit of KP6 (IDs: 1KP6 and 4GVB), a virus-encoded antifungal killer toxin with an α/β-sandwich fold secreted by the fungal corn smut pathogen Ustilago maydis (Allen et al, 2013a; Li et al, 1999) (Table S2). Notably, the NTR of CfCE72 was found to share sequence homology with CfCE24, CfCE56 and CfCE58 (Fig.…”

Section: Resultsmentioning

confidence: 99%