27 kDa antibacterial protein
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27 kDa antibacterial protein

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27 kDa antibacterial protein is an antimicrobial peptide produced by Cyprinus carpio (common carp). It has antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.

Category
Functional Peptides
Catalog number
BAT-013194
Molecular Formula
C87H132N22O30
Molecular Weight
1966.13
Synonyms
Gly-Ile-Gly-Gly-Lys-Pro-Val-Gln-Thr-Ala-Phe-Val-Asp-Asn-Asp-Gly-Ile-Tyr-Asp
Appearance
Lyophilized Powder
Purity
>95%
Sequence
GIGGKPVQTAFVDNDGIYD
Storage
Store at -20°C
1. Salicylate uniquely induces a 27-kDa protein in tubercle bacillus
Z Sun, S J Cheng, H Zhang, Y Zhang FEMS Microbiol Lett. 2001 Sep 25;203(2):211-6. doi: 10.1111/j.1574-6968.2001.tb10843.x.
Salicylate was found to uniquely induce a 27-kDa protein in Mycobacterium tuberculosis complex organisms but not in Mycobacterium smegmatis or Escherichia coli. The structural analogue antitubercular para-amino-salicylate also induced the 27-kDa protein but to a somewhat lower level than salicylate. Other structural analogues such as benzoic acid and acetyl salicylic acid (aspirin) did not induce the 27-kDa protein. Western blot analysis indicated that the 27-kDa protein was localized mainly in the cytoplasm. The 27-kDa protein was not expressed at different growth phases in the absence of salicylate. The 27-kDa protein was identified as a putative benzoquinone methyltransferase (Rv0560c), which has several homologues in the M. tuberculosis genome. The cloned 27-kDa gene was found to express constitutively in E. coli, M. smegmatis and BCG with or without salicylate.
2. HIF1A and NFAT5 coordinate Na+-boosted antibacterial defense via enhanced autophagy and autolysosomal targeting
Patrick Neubert, et al. Autophagy. 2019 Nov;15(11):1899-1916. doi: 10.1080/15548627.2019.1596483. Epub 2019 Apr 14.
Infection and inflammation are able to induce diet-independent Na+-accumulation without commensurate water retention in afflicted tissues, which favors the pro-inflammatory activation of mouse macrophages and augments their antibacterial and antiparasitic activity. While Na+-boosted host defense against the protozoan parasite Leishmania major is mediated by increased expression of the leishmanicidal NOS2 (nitric oxide synthase 2, inducible), the molecular mechanisms underpinning this enhanced antibacterial defense of mouse macrophages with high Na+ (HS) exposure are unknown. Here, we provide evidence that HS-increased antibacterial activity against E. coli was neither dependent on NOS2 nor on the phagocyte oxidase. In contrast, HS-augmented antibacterial defense hinged on HIF1A (hypoxia inducible factor 1, alpha subunit)-dependent increased autophagy, and NFAT5 (nuclear factor of activated T cells 5)-dependent targeting of intracellular E. coli to acidic autolysosomal compartments. Overall, these findings suggest that the autolysosomal compartment is a novel target of Na+-modulated cell autonomous innate immunity.
3. Identification of a novel antibacterial protein from hemolymph of freshwater zooplankton Mesocyclops leuckarti
Varadhan Praveena, Sournamanickam Venkatalakshmi, Naiyf S Alharbi, Shine Kadaikunnan, Jamal M Khaled, Marimuthu Govindarajan Saudi J Biol Sci. 2020 Sep;27(9):2390-2397. doi: 10.1016/j.sjbs.2020.05.011. Epub 2020 May 11.
Bacterial infections are the most important problem of health care worldwide. The hemolymph antibacterial proteins of Mesocyclops leuckarti was isolated for the first time and its antibacterial efficacy was evaluated against four different human pathogenic microbes viz., Escherichia coli, Staphylococcus aureus, Klebsiella pneumonia and Shigella flexneri. The antibacterial potential of the antimicrobial proteins of hemolymph samples from plankton cultured in water enriched with Cow Urine Distillate (CUD) was compared with normal ones. The results indicated that the hemolymph proteins were more potential against Gram negative bacteria than Gram positive bacteria. Klebsiella pneumonia was more susceptible to the hemolymph proteins exhibiting a zone of inhibition measuring 27 mm. The supplement of CUD to the culture media further enriched the antibacterial activity of the hemolymph proteins (29 mm). The SDS-PAGE analysis indicated two different types of clear bands representing proteins of 53 kDa and 19 kDa. Overall, this investigation signified that the microcrustaceans have a defence mechanism hemolymph of Mesocyclops leuckarti have a potential agent for novel antibiotics.
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