Chemical mining of heterotrophic Shewanella algae reveals anti-infective potential of macrocyclic polyketides against multidrug-resistant pathogens

Chakraborty, Kajal and Vinaya, K K and Joy, Minju (2021) Chemical mining of heterotrophic Shewanella algae reveals anti-infective potential of macrocyclic polyketides against multidrug-resistant pathogens. Bioorganic Chemistry, 108. pp. 1-12.

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Abstract

Heterotrophic Gamma-proteobacterium Shewanella algae MTCC 12715, associated with an intertidal red algae Hypnea valentiae, presented broad-spectra of antibacterial activities against pathogenic bacteria bringing about nosocomial infection. Bioassay-guided fractionation of the bacterial crude extract resulted in two undescribed macrocyclic polyketide analogs, with anti-infective activities against methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus faecalis (MIC 3.1–5.0 μg/mL). In order to identify the polyketide biosynthetic machinery termed type-I polyketide synthase (pks-I) encoding biologically active secondary me- tabolites in this strain, the ketosynthase-coding regions of DNA with ≈700 bp size, were amplified, and the partial sequence was submitted in the GenBank (accession number MH157093). The titled compounds were classified under macrocyclic polyketides bearing dodecahydropyrano-trioxacyclooctadecine-dione and trioxo- octadecahydro-1H-benzo[o]tetraoxacyclopentacosine-carboxylate functionalities. Structure-activity correlation analysis displayed that hydrophobic descriptor of the studied compounds could play a prominent role in its anti- infective property against the opportunistic pathogens. Further, in silico molecular docking studies were per- formed in the allosteric sites of penicillin-binding protein (PBP2a) coded by mecA genes of MRSA, and the best binding pose for each compound (docking score

Item Type:	Article
Uncontrolled Keywords:	Heterotrophic Shewanella algae; Intertidal red algae ; Hypnea valentiae; Macrocyclic polyketides; Multidrug-resistant pathogens; Type-I polyketide synthase ;Penicillin-binding protein
Subjects:	Biochemistry > Bioprospecting Biochemistry > Bioactive compounds Biochemistry Algae
Divisions:	CMFRI-Kochi > Marine Biotechnology, Fish Nutrition and Health Division Subject Area > CMFRI > CMFRI-Kochi > Marine Biotechnology, Fish Nutrition and Health Division CMFRI-Kochi > Marine Biotechnology, Fish Nutrition and Health Division Subject Area > CMFRI-Kochi > Marine Biotechnology, Fish Nutrition and Health Division
Depositing User:	Arun Surendran
Date Deposited:	25 Feb 2021 06:36
Last Modified:	25 Feb 2021 06:36
URI:	http://eprints.cmfri.org.in/id/eprint/14900

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