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Insights into the Antibacterial Activity of Prolactin-Inducible Protein against the Standard and Environmental MDR Bacterial Strains
Background: Prolactin inducible protein (PIP) is a small secretary glycoprotein present in most biological fluids and contributes to various cellular functions, including cell growth, fertility, antitumor, and antifungal activities. Objectives: The present study evaluated the antibacterial activitie...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8950685/ https://www.ncbi.nlm.nih.gov/pubmed/35336169 http://dx.doi.org/10.3390/microorganisms10030597 |
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author | Yousuf, Mohd Ali, Asghar Khan, Parvez Anjum, Farah Elasbali, Abdelbaset Mohamed Islam, Asimul Yadav, Dharmendra Kumar Shafie, Alaa Rizwanul Haque, Qazi Mohd. Hassan, Md. Imtaiyaz |
author_facet | Yousuf, Mohd Ali, Asghar Khan, Parvez Anjum, Farah Elasbali, Abdelbaset Mohamed Islam, Asimul Yadav, Dharmendra Kumar Shafie, Alaa Rizwanul Haque, Qazi Mohd. Hassan, Md. Imtaiyaz |
author_sort | Yousuf, Mohd |
collection | PubMed |
description | Background: Prolactin inducible protein (PIP) is a small secretary glycoprotein present in most biological fluids and contributes to various cellular functions, including cell growth, fertility, antitumor, and antifungal activities. Objectives: The present study evaluated the antibacterial activities of recombinant PIP against multiple broad-spectrum MDR bacterial strains. Methods: The PIP gene was cloned, expressed and purified using affinity chromatography. Disk diffusion, broth microdilution, and growth kinetic assays were used to determine the antibacterial activities of PIP. Results: Disk diffusion assay showed that PIP has a minimum and maximum zone of inhibition against E. coli and P. aeruginosa, respectively, compared to the reference drug ampicillin. Furthermore, growth kinetics studies also suggested that PIP significantly inhibited the growth of E. coli and P. aeruginosa. The minimum inhibitory concentration of PIP was 32 µg/mL for E. coli (443), a standard bacterial strain, and 64 µg/mL for Bacillus sp. (LG1), an environmental multidrug-resistant (MDR) strain. The synergistic studies of PIP with ampicillin showed better efficacies towards selected bacterial strains having MDR properties. Conclusion: Our findings suggest that PIP has a broad range of antibacterial activities with important implications in alleviating MDR problems. |
format | Online Article Text |
id | pubmed-8950685 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-89506852022-03-26 Insights into the Antibacterial Activity of Prolactin-Inducible Protein against the Standard and Environmental MDR Bacterial Strains Yousuf, Mohd Ali, Asghar Khan, Parvez Anjum, Farah Elasbali, Abdelbaset Mohamed Islam, Asimul Yadav, Dharmendra Kumar Shafie, Alaa Rizwanul Haque, Qazi Mohd. Hassan, Md. Imtaiyaz Microorganisms Article Background: Prolactin inducible protein (PIP) is a small secretary glycoprotein present in most biological fluids and contributes to various cellular functions, including cell growth, fertility, antitumor, and antifungal activities. Objectives: The present study evaluated the antibacterial activities of recombinant PIP against multiple broad-spectrum MDR bacterial strains. Methods: The PIP gene was cloned, expressed and purified using affinity chromatography. Disk diffusion, broth microdilution, and growth kinetic assays were used to determine the antibacterial activities of PIP. Results: Disk diffusion assay showed that PIP has a minimum and maximum zone of inhibition against E. coli and P. aeruginosa, respectively, compared to the reference drug ampicillin. Furthermore, growth kinetics studies also suggested that PIP significantly inhibited the growth of E. coli and P. aeruginosa. The minimum inhibitory concentration of PIP was 32 µg/mL for E. coli (443), a standard bacterial strain, and 64 µg/mL for Bacillus sp. (LG1), an environmental multidrug-resistant (MDR) strain. The synergistic studies of PIP with ampicillin showed better efficacies towards selected bacterial strains having MDR properties. Conclusion: Our findings suggest that PIP has a broad range of antibacterial activities with important implications in alleviating MDR problems. MDPI 2022-03-09 /pmc/articles/PMC8950685/ /pubmed/35336169 http://dx.doi.org/10.3390/microorganisms10030597 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Yousuf, Mohd Ali, Asghar Khan, Parvez Anjum, Farah Elasbali, Abdelbaset Mohamed Islam, Asimul Yadav, Dharmendra Kumar Shafie, Alaa Rizwanul Haque, Qazi Mohd. Hassan, Md. Imtaiyaz Insights into the Antibacterial Activity of Prolactin-Inducible Protein against the Standard and Environmental MDR Bacterial Strains |
title | Insights into the Antibacterial Activity of Prolactin-Inducible Protein against the Standard and Environmental MDR Bacterial Strains |
title_full | Insights into the Antibacterial Activity of Prolactin-Inducible Protein against the Standard and Environmental MDR Bacterial Strains |
title_fullStr | Insights into the Antibacterial Activity of Prolactin-Inducible Protein against the Standard and Environmental MDR Bacterial Strains |
title_full_unstemmed | Insights into the Antibacterial Activity of Prolactin-Inducible Protein against the Standard and Environmental MDR Bacterial Strains |
title_short | Insights into the Antibacterial Activity of Prolactin-Inducible Protein against the Standard and Environmental MDR Bacterial Strains |
title_sort | insights into the antibacterial activity of prolactin-inducible protein against the standard and environmental mdr bacterial strains |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8950685/ https://www.ncbi.nlm.nih.gov/pubmed/35336169 http://dx.doi.org/10.3390/microorganisms10030597 |
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