scholarly journals Generation and Characterization of Transgenic Plum Lines Expressing gafp-1 with the bul409 Promoter

HortScience ◽  
2011 ◽  
Vol 46 (7) ◽  
pp. 975-980 ◽  
Author(s):  
Hetal M. Kalariya ◽  
Guido Schnabel ◽  
Cesar Petri ◽  
Ralph Scorza
Keyword(s):  
Root Rot ◽  
Woody Plants ◽  
Antifungal Protein ◽  
Open Pollination ◽  
Root Knot Nematode ◽  
Phytophthora Root Rot ◽  
Mannose Binding ◽  
Transgenic Lines ◽  
Binding Lectin

The Gastrodia antifungal protein (GAFP-1) is a mannose-binding lectin that can confer increased disease resistance in transgenic tobacco and plum. In all previously generated, transgenic lines, the gene was under the control of the 35SCaMV promoter. In this study, transgenic plum lines were created from seeds derived from open pollination of the cultivar Bluebyrd (BB-OP) with gafp-1 under the control of the polyubiquitin promoter bul409 and evaluated for Phytophthora root rot (PRR) and Root knot nematode (RKN) susceptibility. One of nine transgenic lines synthesizing GAFP-1 exhibited increased tolerance to PRR caused by P. cinnamomi. The same line (BB-OP-1) was also significantly more tolerant to RKN infection caused by Meloidogyne incognita. BB-OP-1 was more resistant to PRR and equally resistant to RKN compared with the cultivar Stanley-derived 4J line, which expresses gafp-1 under the control of the 35SCaMV promoter. GAFP-1 synthesis in BB-OP-1 was not elevated by pathogen infection, suggesting that the bul409 promoter is not inducible in the plum/GAFP-1 system. This study confirms the usefulness of the gafp-1 gene in various cultivars of transgenic plum and establishes that the bul409 promoter is at least equal in effectiveness to the 35SCaMV promoter for gafp-1 expression in transgenic lines of woody plants.

scholarly journals The Gastrodia Antifungal Protein (GAFP-1) and Its Transcript Are Absent from Scions of Chimeric-grafted Plum

HortScience ◽  
2010 ◽  
Vol 45 (2) ◽  
pp. 188-192 ◽  
Author(s):  
Alexis K. Nagel ◽  
Hetal Kalariya ◽  
Guido Schnabel
Keyword(s):  
Phytophthora Cinnamomi ◽  
Antifungal Protein ◽  
Foreign Gene ◽  
Root Knot Nematode ◽  
Mannose Binding ◽  
Transgenic Lines ◽  
Leaf Tissues ◽  
Polymerase Chain ◽  
Root Tissues ◽  
Binding Lectin

The Gastrodia antifungal protein (GAFP-1) is a monocot mannose-binding lectin found in the Asiatic orchid Gastrodia elata. Transgenic plum (Prunus domestica var. ‘Stanley’) lines (4J and 4I) expressing GAFP-1 exhibit enhanced disease resistance to the stramenopile pathogen Phytophthora cinnamomi and the root-knot nematode Meloidogyne incognita. Rootstocks created from such transgenic lines might be more readily accepted by consumers if it can be shown that foreign gene products are not migrating into a grafted, nontransgenic scion on which fruit is produced. In this study, wild-type (WT) plum tissue was budded onto transgenic plum lines 4J and 4I to create chimeric-grafted trees. Tissues from chimeric-grafted trees were analyzed for gafp-1 transcripts (leaf and root) and protein (leaf, soft shoot, and root) by reverse transcription–polymerase chain reaction and immunodetection, respectively. Transcripts of gafp-1 were detected consistently in the root tissues but not within the leaves of the grafted, WT scions. Similarly, the GAFP-1 lectin was identified within the roots, but not in the soft shoot or leaf tissues of the grafted, WT scions. These results suggest that gafp-1 mRNA and protein are not moving into the WT scion tissues of chimeric-grafted plum trees.

scholarly journals Host Status of Three Transgenic Plum Lines to Mesocriconema xenoplax

HortScience ◽  
2009 ◽  
Vol 44 (7) ◽  
pp. 1932-1935 ◽  
Author(s):  
Andrew P. Nyczepir ◽  
Alexis K. Nagel ◽  
Guido Schnabel
Keyword(s):  
Root Rot ◽  
Phytophthora Cinnamomi ◽  
Promoter Sequence ◽  
Antifungal Protein ◽  
35S Promoter ◽  
Control Line ◽  
Root Knot Nematode ◽  
Phytophthora Root Rot ◽  
Host Status ◽  
The Individual

The expression of gastrodianin antifungal protein (GAFP) in a form of its VNF isoform increases tolerance to Phytophthora root rot (Phytophthora cinnamomi) and the root-knot nematode (Meloidogyne incognita) in transgenic plum lines. However, nothing is known about the potential of the GAFP lectin to confer disease resistance to the ring nematode, Mesocriconema xenoplax, in plum. Three transgenic plum lines (4I, 4J, and 5D) expressing gafp-1 under the control of CaMV 35S promoter sequence were evaluated for their response to M. xenoplax in the greenhouse. All plum lines were rated as hosts of M. xenoplax. Among the individual plum lines tested, the number of M. xenoplax per gram of dry roots was lowest in the rhizosphere of transgenic line 5D, intermediate in that of the nontransformed control line, and greatest in line 4J. The results of this study indicate that the comparisons of the final soil densities (Pf) of adult and juvenile M. xenoplax expressed as nematodes per gram of dry roots provide a better measure of the nematode carrying capacity by the tested lines than Pf values referred to as number of M. xenoplax/100 cm3 soil.

Molecular cloning and characterization of a mannose-binding lectin gene from Crinum asiaticum

2003 ◽  
Vol 160 (8) ◽  
pp. 913-920 ◽  
Author(s):  
Yourong Chai ◽  
Yongzhen Pang ◽  
Zhihua Liao ◽  
L.e.i. Zhang ◽  
Xiaofen Sun ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Mannose Binding Lectin ◽  
Lectin Gene ◽  
Mannose Binding ◽  
Crinum Asiaticum ◽  
Binding Lectin

scholarly journals Crystal Structure and Functional Characterization of the Complement Regulator Mannose-binding Lectin (MBL)/Ficolin-associated Protein-1 (MAP-1)

2012 ◽  
Vol 287 (39) ◽  
pp. 32913-32921 ◽  
Author(s):  
Mikkel-Ole Skjoedt ◽  
Pietro Roversi ◽  
Tina Hummelshøj ◽  
Yaseelan Palarasah ◽  
Anne Rosbjerg ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Functional Characterization ◽  
Mannose Binding Lectin ◽  
Mannose Binding ◽  
Complement Regulator ◽  
Binding Lectin

Susceptibility of Garden Plants to Phytophthora Root Rot

Plant Disease ◽  
2020 ◽  
Author(s):  
Liz Beal ◽  
Ian Waghorn ◽  
Joe Perry ◽  
Gerard R G Clover ◽  
Matthew Cromey
Keyword(s):  
Host Range ◽  
Root Rot ◽  
Woody Plants ◽  
Integrated Management ◽  
Common Species ◽  
Phytophthora Species ◽  
High Index ◽  
Phytophthora Root Rot ◽  
Wide Host Range ◽  
Serious Disease

Phytophthora root rot (PRR) is a serious disease of horticultural, forest and ornamental plant species caused by species of the oomycete genus Phytophthora. Their wide host range makes choice of resistant plants in management of the disease difficult. We used the Royal Horticultural Society diagnostic dataset of PRR records from U.K. gardens to compare the susceptibility of different host genera to the disease. The dataset was compared with existing reports of plants recorded as notably resistant or notably susceptible to PRR. An index-based approach was used to separate 177 genera of woody plants into three categories: 85 were low-index (<0.10: rarely affected), 34 were medium-index (0.10 – 0.20: sometimes affected) and 58 were high-index (>0.20: frequently affected). Similarly, genera of non-woody plants were separated into: 45 low-index (<0.22), 16 medium-index (0.22 – 0.44) and 18 high-index (>0.44). Taxus was the genus with the highest index, while most genera in the Malvales and Ericales were in the high index group. Most genera in the Myrtales, Fabales and Monocotyledons were low index. Whilst 30 Phytophthora species were recorded in our study, the wide host range spp., P. plurivora, P. cryptogea and P. cinnamomi represented 63% of identifications. Phytophthora plurivora was the most common species on woody plants and P. cryptogea on non-woody plants. These results provide confidence in the use of host resistance as part of the integrated management of PRR.

Characterization of a mannose-binding lectin from channel catfish (Ictalurus punctatus)

2012 ◽  
Vol 92 (3) ◽  
pp. 408-413 ◽  
Author(s):  
Hao Zhang ◽  
Eric Peatman ◽  
Hong Liu ◽  
Donghong Niu ◽  
Tingting Feng ◽  
...  
Keyword(s):  
Ictalurus Punctatus ◽  
Channel Catfish ◽  
Mannose Binding Lectin ◽  
Mannose Binding ◽  
Binding Lectin
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