Access the full text.
Sign up today, get DeepDyve free for 14 days.
Wenling Zhang, W. Peumans, A. Barre, Corinne Astoul, P. Rovira, P. Rougé, P. Proost, P. Truffa-bachi, A. Jalali, E. Damme (2000)
Isolation and characterization of a jacalin-related mannose-binding lectin from salt-stressed rice (Oryza sativa) plantsPlanta, 210
H. Yang, T. Czapla (1993)
Isolation and characterization of cDNA clones encoding jacalin isolectins.The Journal of biological chemistry, 268 8
W. Maddison, D. Maddison (1992)
Macclade: Analysis of Phylogeny and Character Evolution/Version 3
Els Damme, A. Barre, P. Verhaert, P. Rougé, W. Peumans (1996)
Molecular cloning of the mitogenic mannose/maltose‐specific rhizome lectin from Calystegia sepiumFEBS Letters, 397
V. Koshte, Willem, Van, Dijk, E. tMarleen, V. Der, STELTt (1990)
Isolation and characterization of BanLec-I, a mannoside-binding lectin from Musa paradisiac (banana).The Biochemical journal, 272 3
S. Ewen, A. Pusztai (1999)
Effect of diets containing genetically modified potatoes expressing Galanthus nivalis lectin on rat small intestineThe Lancet, 354
P. Kraulis (1991)
A program to produce both detailed and schematic plots of protein structures
N. Geshi, A. Brandt (1998)
Two jasmonate-inducible myrosinase-binding proteins from Brassica napus L. seedlings with homology to jacalinPlanta, 204
J. Rosa, L. Greene, P. Oliveira, R. Garratt, L. Beltramini, K. Resing, M. Roque-Barreira (2008)
KM+, a mannose‐binding lectin from artocarpus integrifolia: Amino acid sequence, predicted tertiary structure, carbohydrate recognition, and analysis of the β‐prism foldProtein Science, 8
F. Sanger, S. Nicklen, A. Coulson (1977)
DNA sequencing with chain-terminating inhibitors.Proceedings of the National Academy of Sciences of the United States of America, 74 12
G. May, R. Afza, H. Mason, A. Wiecko, F. Novák, C. Arntzen (1995)
Generation of Transgenic Banana (Musa acuminata) Plants via Agrobacterium-Mediated TransformationBio/Technology, 13
G. Heijne (1986)
A new method for predicting signal sequence cleavage sites.Nucleic Acids Research, 14
J. Thompson, D. Higgins, T. Gibson (1994)
CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice.Nucleic acids research, 22 22
V. Koshte, M. Aalbers, P. Calkhoven, R. Aalberse (1992)
The potent IgG4-inducing antigen in banana is a mannose-binding lectin, BanLec-I.International archives of allergy and immunology, 97 1
L. Lemesle-Varloot, B. Henrissat, C. Gaboriaud, C. Gaboriaud, V. Bissery, A. Morgat, A. Morgat, J. Mornon (1990)
Hydrophobic cluster analysis: procedures to derive structural and functional information from 2-D-representation of protein sequences.Biochimie, 72 8
X. Lee, A. Thompson, Zhiming Zhang, H. Ton-that, J. Biesterfeldt, C. Ogata, Lulu Xu, R. Johnston, N. Young (1998)
Structure of the Complex of Maclura pomiferaAgglutinin and the T-antigen Disaccharide, Galβ1,3GalNAc*The Journal of Biological Chemistry, 273
R. Sankaranarayanan, K. Sekar, R. Banerjee, Vivek Sharma, A. Surolia, M. Vijayan (1996)
A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a β-prism foldNature Structural Biology, 3
S. Clendennen, D. (1997)
Differential Gene Expression in Ripening Banana Fruit, 115
N. Young, R. Johnston, D. Watson (1991)
The amino acid sequences of jacalin and the Maclura pomifera agglutininFEBS Letters, 282
C. Gaboriaud, V. Bissery, T. Benchetrit, J. Mornon (1987)
Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequencesFEBS Letters, 224
Y. Bourne, V. Zamboni, A. Barre, W. Peumans, E. Damme, P. Rougé (2000)
CRYSTAL STRUCTURE OF HELIANTHUS TUBEROSUS LECTIN
U. Laemmli (1970)
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 227
M. Dubois, K. Gilles, J. Hamilton, P. Rebers, F. Smith (1956)
Colorimetric Method for Determination of Sugars and Related SubstancesAnalytical Chemistry, 28
N. Young, R. Johnston, A. Szabo, D. Watson (1989)
Homology of the D-galactose-specific lectins from Artocarpus integrifolia and Maclura pomifera and the role of an unusual small polypeptide subunit.Archives of biochemistry and biophysics, 270 2
E. Damme, W. Peumans, A. Barre, P. Rougé (1998)
Plant Lectins: A Composite of Several Distinct Families of Structurally and Evolutionary Related Proteins with Diverse Biological RolesCritical Reviews in Plant Sciences, 17
E. Damme, A. Barre, A. Mazard, P. Verhaert, A. Horman, H. Debray, P. Rougé, W. Peumans (1999)
Characterization and molecular cloning of the lectin from Helianthus tuberosus.European journal of biochemistry, 259 1-2
One of the predominant proteins in the pulp of ripe bananas (Musa acuminata L.) and plantains (Musa spp.) has been identified as a lectin. The banana and plantain agglutinins (called BanLec and PlanLec, respectively) were purified in reasonable quantities using a novel isolation procedure, which prevented adsorption of the lectins onto insoluble endogenous polysaccharides. Both BanLec and PlanLec are dimeric proteins composed of two identical subunits of 15 kDa. They readily agglutinate rabbit erythrocytes and exhibit specificity towards mannose. Molecular cloning revealed that BanLec has sequence similarity to previously described lectins of the family of jacalin-related lectins, and according to molecular modelling studies has the same overall fold and three-dimensional structure. The identification of BanLec and PlanLec demonstrates the occurrence of jacalin-related lectins in monocot species, suggesting that these lectins are more widespread among higher plants than is actually believed. The banana and plantain lectins are also the first documented examples of jacalin-related lectins, which are abundantly present in the pulp of mature fruits but are apparently absent from other tissues. However, after treatment of intact plants with methyl jasmonate, BanLec is also clearly induced in leaves. The banana lectin is a powerful murine T-cell mitogen. The relevance of the mitogenicity of the banana lectin is discussed in terms of both the physiological role of the lectin and the impact on food safety.
Planta – Springer Journals
Published: Sep 15, 2000
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.