Literature DB >> 24232144

Correlation between infection by Rhizobium leguminosarum and lectin on the surface of Pisum sativum L. roots.

C L Díaz1, P C van Spronsen, R Bakhuizen, G J Logman, E J Lugtenberg, J W Kijne.   

Abstract

The lectin on the surface of 4- and 5-dold pea roots was located by the use of indirect immunofluorescence. Specific antibodies raised in rabbits against pea seed isolectin 2, which crossreact with root lectins, were used as primary immunoglobulins and were visualized with fluorescein- or tetramethylrhodamine-isothiocyanate-labeled goat antirabbit immunoglobulin G. Lectin was observed on the tips of newly formed, growing root hairs and on epidermal cells located just below the young hairs. On both types of cells, lectin was concentrated in dense small patches rather than uniformly distributed. Lectin-positive young hairs were grouped opposite the (proto)xylematic poles. Older but still-elongating root hairs presented only traces of lectin or none at all. A similar pattern of distribution was found in different pea cultivars, as well as in a supernodulating and a non-nodulating pea mutant. Growth in a nitrate concentration which inhibits nodulation did not affect lectin distribution on the surface of pea roots of this age. We tested whether or not the root zones where lectin was observed were susceptible to infection by Rhizobium leguminosarum. When low inoculum doses (consisting of less than 10(6) bacteria·ml(-1)) were placed next to lectin-positive epidermal cells and on newly formed root hairs, nodules on the primary roots were formed in 73% and 90% of the plants, respectively. Only a few plants showed primary root nodulation when the inoculum was placed on the root zone where lectin was scarce or absent. These results show that lectin is present at those sites on the pea root that are susceptible to infection by the bacterial symbiont.

Entities:  

Year:  1986        PMID: 24232144     DOI: 10.1007/BF00392360

Source DB:  PubMed          Journal:  Planta        ISSN: 0032-0935            Impact factor:   4.116


  13 in total

1.  Transient susceptibility of root cells in four common legumes to nodulation by rhizobia.

Authors:  T V Bhuvaneswari; A A Bhagwat; W D Bauer
Journal:  Plant Physiol       Date:  1981-11       Impact factor: 8.340

2.  Studies on phytohemagglutinins. XXIV. Isoelectric point and hybridization of the pea (Pisum sativum L.) isophytohemagglutinins.

Authors:  G Entlicher; J Kocourek
Journal:  Biochim Biophys Acta       Date:  1975-05-30

3.  The role of hormones and gradients in the initiation of cortex proliferation and nodule formation in Pisum sativum L.

Authors:  K R Libbenga; F van Iren; R J Bogers; M F Schraag-Lamers
Journal:  Planta       Date:  1973-03       Impact factor: 4.116

4.  Early Events in the Infection of Soybean (Glycine max L. Merr) by Rhizobium japonicum: I. LOCALIZATION OF INFECTIBLE ROOT CELLS.

Authors:  T V Bhuvaneswari; B G Turgeon; W D Bauer
Journal:  Plant Physiol       Date:  1980-12       Impact factor: 8.340

5.  The biosynthesis and primary structure of pea seed lectin.

Authors:  T J Higgins; P M Chandler; G Zurawski; S C Button; D Spencer
Journal:  J Biol Chem       Date:  1983-08-10       Impact factor: 5.157

6.  Fading of immunofluorescence during microscopy: a study of the phenomenon and its remedy.

Authors:  G D Johnson; R S Davidson; K C McNamee; G Russell; D Goodwin; E J Holborow
Journal:  J Immunol Methods       Date:  1982-12-17       Impact factor: 2.303

7.  Identification of the Sym plasmid of Rhizobium leguminosarum strain 1001 and its transfer to and expression in other rhizobia and Agrobacterium tumefaciens.

Authors:  P J Hooykaas; F G Snijdewint; R A Schilperoort
Journal:  Plasmid       Date:  1982-07       Impact factor: 3.466

8.  Role of Lectins in the Specific Recognition of Rhizobium by Lotononis bainesii.

Authors:  I J Law; B W Strijdom
Journal:  Plant Physiol       Date:  1984-04       Impact factor: 8.340

9.  Cross-reactive antigens and lectin as determinants of symbiotic specificity in the Rhizobium-clover association.

Authors:  F B Dazzo; D H Hubbell
Journal:  Appl Microbiol       Date:  1975-12

10.  Trifolin: a Rhizobium recognition protein from white clover.

Authors:  F B Dazzo; W E Yanke; W J Brill
Journal:  Biochim Biophys Acta       Date:  1978-03-20
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  13 in total

1.  Sugar-binding activity of pea lectin enhances heterologous infection of transgenic alfalfa plants by Rhizobium leguminosarum biovar viciae.

Authors:  P van Rhijn; N A Fujishige; P O Lim; A M Hirsch
Journal:  Plant Physiol       Date:  2001-05       Impact factor: 8.340

Review 2.  Infection and invasion of roots by symbiotic, nitrogen-fixing rhizobia during nodulation of temperate legumes.

Authors:  Daniel J Gage
Journal:  Microbiol Mol Biol Rev       Date:  2004-06       Impact factor: 11.056

3.  Distribution of glucose/mannose-specific isolectins in pea (Pisum sativum L.) seedlings.

Authors:  C L Díaz; M Hosselet; G J Logman; E van Driessche; B J Lugtenberg; J W Kijne
Journal:  Planta       Date:  1990-07       Impact factor: 4.116

4.  Surface Properties and Motility of Rhizobium and Azospirillum in Relation to Plant Root Attachment

Authors: 
Journal:  Microb Ecol       Date:  1996-07       Impact factor: 4.552

5.  Insertion of pea lectin into a phospholipid monolayer.

Authors:  P Booij; R A Demel; B S de Pater; J W Kijne
Journal:  Plant Mol Biol       Date:  1996-04       Impact factor: 4.076

6.  Mutational analysis of the sugar-binding site of pea lectin.

Authors:  R R Van Eijsden; B S De Pater; J W Kijne
Journal:  Glycoconj J       Date:  1994-08       Impact factor: 2.916

7.  Destabilization of pea lectin by substitution of a single amino acid in a surface loop.

Authors:  F J Hoedemaeker; R R van Eijsden; C L Díaz; B S de Pater; J W Kijne
Journal:  Plant Mol Biol       Date:  1993-09       Impact factor: 4.076

8.  Carbohydrate binding and resistance to proteolysis control insecticidal activity of Griffonia simplicifolia lectin II.

Authors:  K Zhu-Salzman; R E Shade; H Koiwa; R A Salzman; M Narasimhan; R A Bressan; P M Hasegawa; L L Murdock
Journal:  Proc Natl Acad Sci U S A       Date:  1998-12-08       Impact factor: 11.205

9.  Mutational analysis of pea lectin. Substitution of Asn125 for Asp in the monosaccharide-binding site eliminates mannose/glucose-binding activity.

Authors:  R R van Eijsden; F J Hoedemaeker; C L Díaz; B J Lugtenberg; B S de Pater; J W Kijne
Journal:  Plant Mol Biol       Date:  1992-12       Impact factor: 4.076

10.  Pea lectin is correctly processed, stable and active in leaves of transgenic potato plants.

Authors:  G A Edwards; A Hepher; S P Clerk; D Boulter
Journal:  Plant Mol Biol       Date:  1991-07       Impact factor: 4.076

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