Isolation and Characterization of Cajanus cajan Lectin

Siddiqui, Shama; Hasan, S.K.; Salahuddin, A

doi:10.1006/abbi.1995.1313

Cited by 19 publications

(3 citation statements)

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“…The lesser adherence in the presence of glucose ⁄ mannose and galactosamine specific lectins could be because of the interaction with this protein. The lowest inhibition by CCL could be explained as it shows lower specificity than Con A (Siddiqui et al 1995). The blocking of this protein by TFA lectin could be a probable reason for the inhibition of biofilm formation as revealed by quantitative estimations on microtitre plate and microscopic evaluations.…”

Section: Discussionmentioning

confidence: 94%

Novel effect of plant lectins on the inhibition ofStreptococcus mutansbiofilm formation on saliva-coated surface

Islam

Khan

Naeem

et al. 2009

Journal of Applied Microbiology

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Aims: Dental caries is caused by the disturbance in oral homeostasis, marked by a notable increase in the population of Streptococcus mutans. Lectins are a group of plant proteins that are capable of recognizing the glycoconjugates present on the bacterial surface. The aim of this study was to evaluate the effect of seven plant lectins on the growth and initial adhesion of S. mutans. Methods and Results: Lectins of different carbohydrate specificities were isolated from plant sources by conventional methods of protein purification. The effect on growth of S. mutans was evaluated following CLSI guidelines. None of the lectins used in this study inhibited the bacterial growth and multiplication. The adherence and biofilm formation of bacteria to saliva‐coated polystyrene plates was tested in the presence of plant lectins. All the plant lectins tested, inhibited both the adherence and biofilm in a concentration dependent manner. Confocal microscopy and scanning electron microscopy were employed to assess the biofilm formation in the presence of plant lectin (glucose/mannose‐specific) at sub‐minimal inhibitory concentrations. These evaluations revealed that lectins inhibited the clumping and attachment of S. mutans. Conclusions: Lectins tested here inhibited initial biofilm formation by S. mutans. Glucose/Mannose‐specific lectin altered the adhesion arrangement of the bacteria on the saliva‐coated surfaces. Significance and Impact of the Study: The plant lectins used in this study may offer a novel strategy to reduce development of dental caries by inhibiting the initial adhesion and subsequent biofilm formation of S. mutans.

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Section: Discussionmentioning

confidence: 94%

Novel effect of plant lectins on the inhibition ofStreptococcus mutansbiofilm formation on saliva-coated surface

Islam

Khan

Naeem

et al. 2009

Journal of Applied Microbiology

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“…Cajanus cajan lectin is a dimer composed of identical subunit with N-and C-terminal residues of threonine and alanine respectively. Its amino acid composition is characterized by presence of hign content of acidic amino acids (Siddiqui et al, 1995). The present study was carried out to study the physico-chemical properties, secondary structure attributes and 3D model of CCL protein.…”

Section: Issn: 2319-7706 Volume 7 Number 06 (2018)mentioning

confidence: 99%

In Silico Analysis and Molecular Docking Studies of Cajanus cajan Lectin against Aminopeptidase-N Receptor from Acyrthosiphon pisum

Prajapat¹,

Singh²,

Tiwari³

et al. 2018

Int.J.Curr.Microbiol.App.Sci

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“…A comparable subunit containing threonine and alanine at the N-and C-termini of each subunit make up the dimer of Cajanus cajan lectin. The presence of a significant amount of acidic amino acids serves as the primary indicator of its amino acid composition [12]. The goal of the current work was to characterize the CCL protein and APN's secondary structure, 3D model, and physicochemical properties.…”

Section: Introductionmentioning

confidence: 99%

Computational Analysis to Study the Insecticidal Properties of Lectin Protein Through Docking Studies

Chandra¹,

Yadav²

2023

Int J Pharm Phytopharmacol Res

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Lectins belong to one of those protein families that exist in nature in abundance. Out of these, legume lectins are widely spread and display interesting antimicrobial and insecticidal properties. This is because, they recognize and bind to specific carbohydrate components without making any changes in the covalent assembly of recognized ligands, which makes them a suitable target candidate for useful applications in food and agriculture Moreover, numerous studies have demonstrated that the lectins found in legumes are poisonous to hemipterans. This study aims to elaborate on the insecticidal properties of Cajanus cajan lectin (CCL) with receptor alanyl Aminopeptidase N (APN) from Acyrthosiphon pisum membrane and other insect origins through molecular modeling. The Protparam tool elaborated on the usefulness of physico-chemical parameters such as the aliphatic index, theoretical isoelectric point, and instability index along with the functional domains of the protein. The secondary structure of the CCL and APN was predicted to explain their structural and behavioral properties. Molecular docking was done between CCL as ligand and APN as receptor from different insect origins to obtain the cluster scores. To validate the current knowledge of the CCL protein structure and to demonstrate the prospective candidate gene for developing transgenics for improved aphid or other insect resistance, cluster scores with the lowest energy were evaluated using a variety of bio-computational tools.

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Isolation and Characterization of Cajanus cajan Lectin

Cited by 19 publications

References 0 publications

Novel effect of plant lectins on the inhibition ofStreptococcus mutansbiofilm formation on saliva-coated surface

Novel effect of plant lectins on the inhibition ofStreptococcus mutansbiofilm formation on saliva-coated surface

In Silico Analysis and Molecular Docking Studies of Cajanus cajan Lectin against Aminopeptidase-N Receptor from Acyrthosiphon pisum

Computational Analysis to Study the Insecticidal Properties of Lectin Protein Through Docking Studies

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