LHR
| 17:57 Nov 27, 2023 |
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| French to English translations [PRO] Medical - Medical (general) / LHR | |||||||
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| 1 | Long / Large Helicase Related (protein/gene) |
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Answers
5 hrs confidence: 
Long / Large Helicase Related (protein/gene) Explanation: This is way above my pay grade, so I cannot give the slightest assurance that this is even remotely related to what you are dealing with, but LHR does effect bacterial resistance, though I don't see the relevance to humans carrying it since we are hardly likely to throw ourselves on the barbecue for a long heating session to rid ourselves of it. Though I suppose carriers could convey it to foodstuffs where bacterial heat resistance would be a problem. Both long and large are said, but I have no idea if they are the same thing. "The gene (tentatively termed lhr for long helicase related) contains the seven conserved motifs of the DNA and RNA helicase superfamily II" https://pubmed.ncbi.nlm.nih.gov/7559321/ "Lhr (Large helicase-related) protein is an ATP-dependent DNA translocase and helicase that forms a distinct group within Superfamily 2 helicases [1,2]. Lhr was discovered and named in bacteria[2], in which it is present in eight of ∼30 phyla [2,3]. It is widespread in archaea [4], and the archaeal Lhr is a sequence homologue of the DDX-family of uncharacterized putative helicases found in eukaryotes including in humans [5–7]. Archaeal and bacterial Lhr proteins show high amino acid sequence identity (typically ∼30%) between their N-terminal 800–900 amino acids, which is referred to as the ‘Lhr-Core’, that comprises their helicase domains [8]. Bacterial Lhr is extended to 1300–1500 amino acids by a region of unknown function that lacks obvious sequence homologues. Biochemical analysis of the Lhr-Core from the bacteria Mycobacterium smegmatis and Pseudomonas putida identified ATP-dependent ssDNA translocation with 3′ to 5′ directionality [1,9,10]. A crystal structure of bacterial Lhr-Core highlights significant similarities with the archaeal DNA repair helicase Hel308 [9,11], most notably in the orientation and interaction of its winged helix domain (WHD) with RecA-like domains typical of Ski2-like helicases" https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7437997/ "Quinolones mainly inhibit the synthesis of DNA by inhibiting DNA topoisomerase to achieve bacteriostatic effect. The DNA helicase (GyrA2B2) and topoisomerase IV (ParC2E2) of bacteria are the targets of quinolones. After the mutation of their encoding genes, the structure of DNA helicase or topoisomerase change, which results in a decreased affinity between the drug and DNA-enzyme complex, causing drug resistance" https://www.sciencedirect.com/science/article/pii/S136876462... "Heat resistant E. coli isolates included originated from both clinical and environmental sources; three clinical isolates previously identified as 111, 128, and 8354 were from human cases of acute gastroenteritis submitted to Alberta Precision Laboratories—Provincial Laboratory for Public Health (ProvLab) [15]. Environmental isolate AW1.7 originated from a local cattle slaughter plant [16] and isolates 53 and 63 were obtained from a municipal wastewater treatment plant [17]. [ …] In this study, we were able to confirm biofilm formation in heat resistant E. coli isolates from environmental and clinical sources in Alberta using the two-component apparatus and demonstrate that the LHR likely does not contribute to increased biofilm forming potential. The findings obtained in this study provide further evidence that biofilms are not regarded as an essential virulence factor for EHEC survival and pathogenesis [60]. Weaker biofilm forming potential of clinical E. coli strains compared to environmental E. coli strains is likely due to higher adaptation to various stress conditions the latter encounter in their ecological niches. The identification of pathogenic E. coli that possess the LHR and tolerance to multiple environmental stressors illustrates the threat they pose on food safety at various points in the farm-to-fork continuum. Further study on the contribution of heat resistant E. coli in human foodborne infection may potentially identify new sources of contamination and shortcomings in current pathogen inactivation methods used in the food processing industry" https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7919257/ |
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Reference comments
19 hrs |
| Reference: comment Reference information: no findings at all for this phrase |
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