scholarly journals Lectins as Plant Defense Proteins

1995 ◽  
Vol 109 (2) ◽  
pp. 347-352 ◽  
Author(s):  
W. J. Peumans ◽  
EJM. Van Damme
2007 ◽  
Vol 143 (4) ◽  
pp. 1954-1967 ◽  
Author(s):  
Hui Chen ◽  
Eliana Gonzales-Vigil ◽  
Curtis G. Wilkerson ◽  
Gregg A. Howe

2006 ◽  
Vol 24 (2) ◽  
pp. 115-118
Author(s):  
M.T. Mmbaga ◽  
F.J. Avila ◽  
E.F. Howard ◽  
E.L. Myles

Abstract This study was conducted to better understand the nature of powdery mildew resistance in flowering dogwood (Cornus florida L.) and in particular to determine if inducible plant defense proteins are associated with powdery mildew resistance. Results from this study showed an accumulation of a new protein in resistant plants, but not in susceptible plants that were challenged with powdery mildew pathogen (Erysiphe (Sect. Microsphaera) pulchra). The protein accumulated in a high level in the resistant selections at 48 hr after inoculation with the pathogen and that was consistent with the production of pathogenesis related (PR) proteins. The protein was characterized as having an isoelectric point of 7.5 ± 0.5 and molecular weight of 18 ± 2 KD. Partial sequence analysis of this protein revealed homology with PR-10 protein associated with drought resistance in potato and was analogous to other proteins related to resistance in other crops. Repeated analysis showed similar results and suggested that a biochemical mode of resistance involving plant defense proteins may be associated with powdery mildew resistance in flowering dogwood.


2021 ◽  
Vol 4 ◽  
Author(s):  
Tetyana Nosenko ◽  
Manuel Hanke-Uhe ◽  
Philip Alexander Heine ◽  
Afsheen Shahid ◽  
Stefan Dübel ◽  
...  

2010 ◽  
Vol 9 (4) ◽  
pp. 558-568 ◽  
Author(s):  
Hyeseung Lee ◽  
Barbara Damsz ◽  
Charles P. Woloshuk ◽  
Ray A. Bressan ◽  
Meena L. Narasimhan

ABSTRACT Fusarium oxysporum is the causative agent of fungal wilt disease in a variety of crops. The capacity of a fungal pathogen such as F. oxysporum f. sp. nicotianae to establish infection on its tobacco (Nicotiana tabacum) host depends in part on its capacity to evade the toxicity of tobacco defense proteins, such as osmotin. Fusarium genes that control resistance to osmotin would therefore reflect coevolutionary pressures and include genes that control mutual recognition, avoidance, and detoxification. We identified FOR ( Fusarium O smotin R esistance) genes on the basis of their ability to confer osmotin resistance to an osmotin-sensitive strain of Saccharomyces cerevisiae. FOR1 encodes a putative cell wall glycoprotein. FOR2 encodes the structural gene for glutamine:fructose-6-phosphate amidotransferase, the first and rate-limiting step in the biosynthesis of hexosamine and cell wall chitin. FOR3 encodes a homolog of SSD1, which controls cell wall composition, longevity, and virulence in S. cerevisiae. A for3 null mutation increased osmotin sensitivity of conidia and hyphae of F. oxysporum f. sp. nicotianae and also reduced cell wall β-1,3-glucan content. Together our findings show that conserved fungal genes that determine cell wall properties play a crucial role in regulating fungal susceptibility to the plant defense protein osmotin.


1998 ◽  
Vol 11 (5) ◽  
pp. 393-403 ◽  
Author(s):  
Pascal Gamas ◽  
Françoise de Billy ◽  
Georges Truchet

Two Medicago truncatula nodulin genes putatively encoding proteins structurally related to two classes of proteins commonly associated with plant defense reactions have been characterized. MtN1 is homologous to two small, cysteine-rich, pathogen-inducible proteins from pea (pI39 and pI230), whereas MtN13 is closely related to the PR10 family of pathogenesis-related proteins. We show that neither MtN1 nor MtN13 is induced in leaves in response to pathogenic bacteria, and that both are exclusively expressed during nodulation. In situ hybridization experiments as well as Northern (RNA) studies of interactions between M. truncatula and either wild-type Rhizobium meliloti or mutants deficient in infection establish that MtN1 is associated with the infection process, while MtN13 represents the first specific marker described for the nodule outer cortex. Possible roles for MtN1 and MtN13 are discussed. We also present the identification of another member of the PR10 family, designated as MtPR10-1, whose regulation is strikingly different from that observed for MtN13, being constitutively expressed in roots and pathogen-inducible in leaves.


2018 ◽  
Author(s):  
Sabyasachi Mandal ◽  
Wangming Ji ◽  
Thomas D. McKnight

ABSTRACTMany plants in the Solanaceae family secrete acylsugars, which are branched-chain and straight-chain fatty acids esterified to glucose or sucrose. These compounds have important roles in plant defense and potential commercial applications. However, several acylsugar metabolic genes remain unidentified, and little is known about regulation of this pathway. We used comparative transcriptomic analysis between low- and high-acylsugar-producing accessions of Solanum pennellii and found that expression levels of most acylsugar metabolic genes, including known acylsucrose biosynthetic genes and novel candidate genes (putatively encoding a ketoacyl-ACP synthase IV/II-like enzyme, peroxisomal acyl-activating enzymes, ABC transporters, and central carbon metabolic enzymes), were positively correlated with acylsugar accumulation, except two acylglucose biosynthetic genes. Genes putatively encoding oxylipin metabolic proteins, subtilisin-like proteases, and other antimicrobial defense proteins were upregulated in low-acylsugar-producing accessions, possibly to compensate for diminished defense activities of acylsugars. Gene co-expression network analysis clustered most differentially expressed genes into two separate modules and identified genetic networks associated with acylsugar production and plant defense. Transcriptome analysis after inhibition of biosynthesis of branched-chain amino acids (precursors to branched-chain fatty acids) further supported the coordinated regulation of most acylsugar candidate genes and identified three putative AP2-family transcription factor genes that form a strong co-expression network with many acylsugar metabolic genes.


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