2013
DOI: 10.1080/17429145.2013.849362
|View full text |Cite
|
Sign up to set email alerts
|

Induction of β-1,3-glucanase and chitinase inVigna aconitifoliainoculated withMacrophomina phaseolina

Abstract: Pathogenesis-related (PR) proteins are induced in response to pathogen attack. In the present study, the induction of PR proteins in response to the fungal pathogen Macrophomina phaseolina was investigated in 15-day-and 1-month-old plants of Vigna aconitifolia with resistant and susceptible cultivars. Inoculation of the fungal pathogen resulted in the enzyme activity gradually increased throughout the experimental period of 168 h compared to control. However, the activation of β-1,3-glucanase and chitinase was… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

0
6
0

Year Published

2016
2016
2024
2024

Publication Types

Select...
6
1

Relationship

0
7

Authors

Journals

citations
Cited by 10 publications
(7 citation statements)
references
References 26 publications
0
6
0
Order By: Relevance
“…However, the connection site supporting closed conformation was reported at alpha-helix 14 and 15 ranged from residues 404 to 408. The enzyme reported in the current investigation has a residual coverage of 401; hence, the structural difference has displaced the second connection at alpha-helix 13. The open conformation was upon the release of phosphoglycerate and ATP, whereas the closed conformation contained phosphoglycerate and ADP [24].…”
Section: Discussionmentioning
confidence: 65%
See 1 more Smart Citation
“…However, the connection site supporting closed conformation was reported at alpha-helix 14 and 15 ranged from residues 404 to 408. The enzyme reported in the current investigation has a residual coverage of 401; hence, the structural difference has displaced the second connection at alpha-helix 13. The open conformation was upon the release of phosphoglycerate and ATP, whereas the closed conformation contained phosphoglycerate and ADP [24].…”
Section: Discussionmentioning
confidence: 65%
“…These enzymes are called hydrolysis, as they cause the hydrolysis of glycosidic bonds [11]. Induction of β-1,3-glucanase in Vigna aconitifolia and its implications in defense responses of moth bean plants against M. phaseolina have been discussed by Gupta et al [12] and Pareek et al [13]. Defense responses of some other isozymes of glucanase have also been reported in genus Vigna [14,15], which indicates the probability of multiple isozymes of glucanase in the cowpea plant.…”
Section: Introductionmentioning
confidence: 98%
“…In pathogenic fungi, the ability to maintain cell wall integrity is critical for establishing diseases in the host (Jeon et al, 2008). The fungal cell wall is a matrix of three main components: chitin, glucans, and proteins (Webster and Weber, 2007;Lenardon et al, 2010;Pareek et al, 2014). The destruction of these components usually leads to changes in morphology and loss of the biological function of fungal hyphae.…”
Section: Discussionmentioning
confidence: 99%
“…Apart from this, interaction of fungal pathogen with plants results into induction of numerous biochemical responses including rapid accumulation of chitinases and β‐ l,3‐glucanase which degrade chitin and β‐ l,3‐glucan, the major component of fungal cell wall, respectively. Chitinases along with β 1, 3‐glucanases act synergistically and strongly inhibit fungal growth by their combined hydrolytic action in comparison to chitinases and β 1, 3‐glucanases alone as reported in chick pea ( Cicer arientum ), moth bean ( Vigna aconitifolia ), bean leaves ( Phsealous vulgaris ) (Abeles, Bosshart, Forrence, & Habig, ; Nehra et al, ; Pareek et al, ) etc. Hence, in optimal functioning of plant defense mechanism a parallel increase in the activity of both chitinase and glucanase is important.…”
Section: Plant Chitinases (Ec 32114)mentioning
confidence: 97%
“…Plant chitinases have been reported from the roots of yam ( Dioscorea opposite ) (Tsukamoto et al., ), tobacco (Kern et al, ), tomato (Pozo, Azcón‐Aguilar, Dumas‐Gaudot, & Barea, ) and carrot, from stem of sweet potato, cabbage (Chen et al, ) and Crocus sativus (López & Gómez, ), from latex of Ipomoa carnea (Patel et al, ) , Morus alba (Kitajima et al, ) , Ficus microcarpa ((Taira, Ohdomari et al, ), Carica papaya, Ficus carica, Euphorbia characias (Span et al, ) and Hevea brasiliensis (Martin, ), from leaves of tobacco, cotton, tea (Nisha, Prabu, Manda, & Arvinth, ), sugar beet, alfa alfa (Zhong & Hiruki, ), pokeweed (Ohta, Yamagami, & Funatsu, ), potato, Pteris ryukyuensis, beans and oat (Sorensen et al, ), from fruits of Diospyros kaki (Zhang, Kopparapu, Yan, Yang, & Jiang, ) , Punica granatum (Kopparapu, Liu, Yan et al, ) , Ananas comosus (Taira, Ohdomari et al, ) , Ficus awkeotsang (Li, ), wheat and barley grain ( Hordeum vulgare ) (Kragh, Jacobsen, & Mikkelsen, ), barley endosperm, maize kernels (Z ea mays ) (Moore, Price, Boston, Weissinger, & Payne, ) and sweet orange, from seeds of Adenanthera pavonina (Santos et al, ), Astragalus membranaceus (Kopparapu, Liu, Yan et al, ) , Arabidopsis thaliana (Verburg & Huynh, ), Cucumus sativus (Majeau, Trudel, & Asselin, ) , Secale cereale (Yamagami & Funatsu, ), Sorghum bicolor (Krishnaveni, Muthukrishnan, Liang, Wilde, & Manickam, ), Pennisitum glaucum (Radhajeyalakshmi et al, ) , Tamarindus indica (Rao & Gowda, ) , Brassica napus and various beans including faba beans ( Vicia faba ) (S. Wang, Ye, Chen, & Rao, ), canadian cranberry beans ( Phaseolus vulgaris ) (Wang, Shao, Fu, & Rao, ), mung bean ( Phaseolus mungo ) (X. Ye & Ng, ), pea ( Pisum sativum ), black soya bean ( Glycine max ) (Chang et al, ), black soybean seed coat ( Glycine soja ) (Hirano, Hayashi, & Okuno, ), rice bean ( Vigna umbellata ) (Ye & Ng, ), cowpea ( Vigna unguiculata) (Gomes, Oliveira, & Xavier‐Filho, ), lima beans ( Phaseolus limensis ) (Wang, Zhou, Shao, Lu, & Rao, ), moth bean ( Vigna aconitifolia ) (Pareek, Ravi, & Sharma, ) red kidney bean ( Phaseolus vulgaris ) (Mauch & Staehelin, ), chickpea ( Cicer arietinum ) (Nehra, Chugh, Dhillon, & Ranbir, <...>…”
Section: Plant Chitinases (Ec 32114)mentioning
confidence: 99%