Leucine-Rich, Potent Anti-Bacterial Protein against <i>Vibrio cholerae, Staphylococcus aureus</i> from <i>Solanum trilobatum</i> Leaves
A 24 kDa leucine-rich protein from ion exchange fractions of <i>Solanum trilobatum</i>, which has anti-bacterial activity against both the Gram-negative <i>Vibrio cholerae</i> and Gram-positive <i>Staphylococcus aureus</i> bacteria has been purified. In this study...
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2022-02-01
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author | Manohar Radhakrishnan Malathy Palayam Ammar B. Altemimi Lakshminarayanan Karthik Gunasekaran Krishnasamy Francesco Cacciola Lakshmanan Govindan |
author_facet | Manohar Radhakrishnan Malathy Palayam Ammar B. Altemimi Lakshminarayanan Karthik Gunasekaran Krishnasamy Francesco Cacciola Lakshmanan Govindan |
author_sort | Manohar Radhakrishnan |
collection | DOAJ |
description | A 24 kDa leucine-rich protein from ion exchange fractions of <i>Solanum trilobatum</i>, which has anti-bacterial activity against both the Gram-negative <i>Vibrio cholerae</i> and Gram-positive <i>Staphylococcus aureus</i> 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 <i>Solanum triolbatum</i> 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. |
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spelling | doaj.art-223dd21fc4f840738f8f4ef71b1c833d2023-11-23T21:19:45ZengMDPI AGMolecules1420-30492022-02-01274116710.3390/molecules27041167Leucine-Rich, Potent Anti-Bacterial Protein against <i>Vibrio cholerae, Staphylococcus aureus</i> from <i>Solanum trilobatum</i> LeavesManohar Radhakrishnan0Malathy Palayam1Ammar B. Altemimi2Lakshminarayanan Karthik3Gunasekaran Krishnasamy4Francesco Cacciola5Lakshmanan Govindan6Center of Advanced Study in Crystallography & Biophysics, University of Madras, Chennai 600025, IndiaCenter of Advanced Study in Crystallography & Biophysics, University of Madras, Chennai 600025, IndiaDepartment of Food Science, College of Agriculture, University of Basrah, Basrah 61004, IraqCenter of Advanced Study in Crystallography & Biophysics, University of Madras, Chennai 600025, IndiaCenter of Advanced Study in Crystallography & Biophysics, University of Madras, Chennai 600025, IndiaDepartment of Biomedical, Dental, Morphological and Functional Imaging Sciences, University of Messina, 98125 Messina, ItalySri Lakshmi Narayana Institute of Medical Sciences, Puducherry Affiliated to Bharath Institute of Higher Education and Research, Chennai 605502, IndiaA 24 kDa leucine-rich protein from ion exchange fractions of <i>Solanum trilobatum</i>, which has anti-bacterial activity against both the Gram-negative <i>Vibrio cholerae</i> and Gram-positive <i>Staphylococcus aureus</i> 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 <i>Solanum triolbatum</i> 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.https://www.mdpi.com/1420-3049/27/4/1167<i>Staphylococcus aureus</i><i>Vibrio cholerae</i>antimicrobial function<i>Solanum trilobatum</i> |
spellingShingle | Manohar Radhakrishnan Malathy Palayam Ammar B. Altemimi Lakshminarayanan Karthik Gunasekaran Krishnasamy Francesco Cacciola Lakshmanan Govindan Leucine-Rich, Potent Anti-Bacterial Protein against <i>Vibrio cholerae, Staphylococcus aureus</i> from <i>Solanum trilobatum</i> Leaves Molecules <i>Staphylococcus aureus</i> <i>Vibrio cholerae</i> antimicrobial function <i>Solanum trilobatum</i> |
title | Leucine-Rich, Potent Anti-Bacterial Protein against <i>Vibrio cholerae, Staphylococcus aureus</i> from <i>Solanum trilobatum</i> Leaves |
title_full | Leucine-Rich, Potent Anti-Bacterial Protein against <i>Vibrio cholerae, Staphylococcus aureus</i> from <i>Solanum trilobatum</i> Leaves |
title_fullStr | Leucine-Rich, Potent Anti-Bacterial Protein against <i>Vibrio cholerae, Staphylococcus aureus</i> from <i>Solanum trilobatum</i> Leaves |
title_full_unstemmed | Leucine-Rich, Potent Anti-Bacterial Protein against <i>Vibrio cholerae, Staphylococcus aureus</i> from <i>Solanum trilobatum</i> Leaves |
title_short | Leucine-Rich, Potent Anti-Bacterial Protein against <i>Vibrio cholerae, Staphylococcus aureus</i> from <i>Solanum trilobatum</i> Leaves |
title_sort | leucine rich potent anti bacterial protein against i vibrio cholerae staphylococcus aureus i from i solanum trilobatum i leaves |
topic | <i>Staphylococcus aureus</i> <i>Vibrio cholerae</i> antimicrobial function <i>Solanum trilobatum</i> |
url | https://www.mdpi.com/1420-3049/27/4/1167 |
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