Leucine-Rich, Potent Anti-Bacterial Protein against Vibrio cholerae, Staphylococcus aureus from Solanum trilobatum Leaves.

Manohar Radhakrishnan,Gunasekaran Krishnasamy,Lakshmanan Govindan,Malathy Palayam,Ammar B Altemimi,Lakshminarayanan Karthik,Francesco Cacciola

doi:10.3390/molecules27041167

Abstract

A 24 kDa leucine-rich protein from ion exchange fractions of Solanum trilobatum, which has anti-bacterial activity against both the Gram-negative Vibrio cholerae and Gram-positive Staphylococcus aureus bacteria has been purified. In this study, mass spectrometry analysis identified the leucine richness and found a luminal binding protein (LBP). Circular dichroism suggests that the protein was predominantly composed of α- helical contents of its secondary structure. Scanning electron microscopy visualized the characteristics and morphological and structural changes in LBP-treated bacterium. Further in vitro studies confirmed that mannose-, trehalose- and raffinose-treated LBP completely inhibited the hemagglutination ability towards rat red blood cells. Altogether, these studies suggest that LBP could bind to sugar moieties which are abundantly distributed on bacterial surface which are essential for maintaining the structural integrity of bacteria. Considering that Solanum triolbatum is a well-known medicinal and edible plant, in order to shed light on its ancient usage in this work, an efficient anti-microbial protein was isolated, characterized and its in vitro functional study against human pathogenic bacteria was evaluated.

Highlights

Thanks to their constant evolution, many pathogenic bacteria have developed resistance against conventional antibiotics, which has led to a search for alternative therapeutics.In recent times, the use of antimicrobial proteins or peptides has emerged as one of the most reliable options for circumventing the effect of antibiotic-resistant pathogens
Plants themselves adopt different types of defense mechanisms to protect against microbes, which includes the production of antimicrobial proteins, secondary metabolites, lytic enzymes and membrane-interacting proteins possessing cell wall reinforcement [3]
The role of luminal binding protein (LBP) is well characterized in plants and animals, in the present study, for the first time, we reported its role as an antibacterial agent against human pathogens

Summary

Introduction

The use of antimicrobial proteins or peptides has emerged as one of the most reliable options for circumventing the effect of antibiotic-resistant pathogens. In nature, these antimicrobial proteins are present in most species such as insects, plants and mammals as a part of their defense mechanism. These antimicrobial proteins are present in most species such as insects, plants and mammals as a part of their defense mechanism They possess diversified functions that range from having actual antimicrobial properties to immunomodulatory effects [1]. Plants themselves adopt different types of defense mechanisms to protect against microbes, which includes the production of antimicrobial proteins, secondary metabolites, lytic enzymes and membrane-interacting proteins possessing cell wall reinforcement [3]

Methods

Results

Conclusion