Abstract
Concanavalin is a highly revered plant lectin with wide biological significance. Canavalia lectins of the Diocleinae subtribe possess increased structural similarity, but vary in their biological roles and applications. The lectin gene sequences of C. cathartica (ConC), C. ensiformis (ConA), C. gladiata (ConG) and C. rosea (ConM) were sequenced, PCR amplified, collated and compared with members of Phaseoleae tribe. Comparison of nucleotide sequences reveals changes in few bases. All Canavalia spp. diverged from C. bonariensis in the phylogenetic trees constructed according to the nucleotide sequences and the corresponding protein sequence of the legume lectins. The fluctuations in root mean square deviation derived by superimposition of monomers and tetramers substantiate variability in sugar specificity and biological activities.
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Abbreviations
- ConA:
-
Concanavalin A
- ConBr:
-
Concanavalin Br
- CaBo:
-
Concanavalin Bo
- ConC:
-
Concanavalin C
- ConG:
-
Concanavalin G
- ConM:
-
Concanavalin M
- PCR:
-
Polymerase chain reaction
- PDB:
-
Protein data bank
- rmsd:
-
root mean square deviation value
- TM-score:
-
Template modelling score
- CRD:
-
Carbohydrate recognition domain
- ETS:
-
External transcribed spacer
- ITS:
-
Internal transcribed spacer
- trnK:
-
TRNALys(UUU) gene
- matK:
-
MaturaseK gene
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Acknowledgements
Authors profusely thank Prof. K. R. Sridhar, Adjunct Professor, Dept. of Biosciences, Mangalore University for comments and constructive suggestions for improvement of the manuscript.
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42485_2020_41_MOESM1_ESM.jpg
Supplementary 1: Structural homology of concanavalins. Superimposed structures of concanavalins. ●CaBo; ●ConA; ●ConBr; ●ConC; ●ConG; ●ConM; ●Ca2+; ●Mn2+; Sugar binding domain is shown in red circle (JPG 136 kb)
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Suvarna, G., Sharma, B.B. An analogy of Canavalia lectins by molecular phylogenetic characterization. J Proteins Proteom 11, 193–203 (2020). https://doi.org/10.1007/s42485-020-00041-y
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DOI: https://doi.org/10.1007/s42485-020-00041-y