About: G-quadruplex stabilization in the ions and maltose transporters inhibit Salmonella enterica growth and virulence

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About: G-quadruplex stabilization in the ions and maltose transporters inhibit Salmonella enterica growth and virulence Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	G-quadruplex stabilization in the ions and maltose transporters inhibit Salmonella enterica growth and virulence
Creator	Kumar, Amit Jain, Neha Shankar, Uma Jaiswal, Ankit Kodgire, Prashant Kumar Mishra, Subodh Kumar Sharma, Tarun Tawani, Arpita
Source	BioRxiv; MedRxiv
abstract	The G-quadruplex structure forming motifs have recently emerged as a novel therapeutic drug target in various human pathogens. Herein, we report three highly conserved G-quadruplex motifs (SE-PGQ-1, 2, and3) in genome of all the 412 strains of Salmonella enterica. Bioinformatics analysis inferred the presence of SE-PGQ-1 in the regulatory region of mgtA, presence of SE-PGQ-2 in the open reading frame of entA and presence of SE-PGQ-3 in the promoter region of malE and malK genes. The products of mgtA and entA are involved in transport and homeostasis of Mg2+ and Fe3+ ion and thereby required for bacterial survival in the presence of reactive nitrogen/oxygen species produced by the host macrophages, whereas, malK and malE genes are involved in transport of maltose sugar, that is one of the major carbon source in the gastrointestinal tract of human. The formation of stable intramolecular G-quadruplex structures by SE-PGQs was confirmed by employing CD, EMSA and NMR spectroscopy. Cellular studies revealed the inhibitory effect of 9-amino acridine on Salmonella enterica growth. Next, CD melting analysis demonstrated the stabilizing effect of 9-amino acridine on SE-PGQs. Further, polymerase inhibition and RT-qPCR assays emphasize the biological relevance of predicted G-quadruplex in the expression of PGQ possessing genes and demonstrate the G-quadruplexes as a potential drug target for the devolping novel therapeutics for combating Salmonella enterica infection. Author Summary Since last several decades’ scientific community has witnessed a rapid increase in number of such human pathogenic bacterial species that acquired resistant to multiple antibacterial agents. Currently, emergence of multidrug-resistant strains remain a major public health concern for clinical investigators that rings a global alarm to search for novel and highly conserved drug targets. Recently, G-quadruplex structure forming nucleic acid sequences were endorsed as highly conserved Drug target for preventing infection of several human pathogens including viral and protozoan species. Therefore, here we explored the presence G-quadruplex forming motif in genome of Salmonella enterica bacteria that causes food poisoning, and enteric fever in human. The formation of intra molecular G-quadruplex structure in four genes (mgtA, entA, malE and malK) was confirmed by NMR, CD and EMSA. The 9-amino acridine, a known G-quadruplex binder has been shown to stabilize the predicted G-quadruplex motif and decreases the expressioin of G-quadruplex hourbouring genes using RT-PCR and cellular toxicity assay. This study concludes the presence of G-quadruplex motifs in essential genes of Salmonella enterica genome as a novel and conserved drug target and 9-amino acridine as candidate small molecule for preventing the infection of Salmonella enterica using a G4 mediated inhibition mechanism.
has issue date	2018-06-27(xsd:dateTime)
bibo:doi	10.1101/357046
has license	biorxiv
sha1sum (hex)	83cca3779f8aeea47c5426e1d0fa65f1e9567e0c
schema:url	https://doi.org/10.1101/357046
resource representing a document's title	G-quadruplex stabilization in the ions and maltose transporters inhibit Salmonella enterica growth and virulence
schema:publication	bioRxiv
resource representing a document's body	covid:83cca3779f8aeea47c5426e1d0fa65f1e9567e0c#body_text
is schema:about of	named entity 'inferred' named entity 'formation' named entity 'involved' named entity 'EMSA' named entity 'species' named entity 'bacterial' named entity 'presence' named entity 'infection' named entity 'melting' named entity 'IONS' named entity 'REGION' named entity 'OPEN READING FRAME' covid:arg/83cca3779f8aeea47c5426e1d0fa65f1e9567e0c named entity 'POTENTIAL' named entity 'BIOINFORMATICS ANALYSIS' named entity 'INVOLVED' named entity 'MGTA' named entity 'RT-QPCR' named entity 'G-QUADRUPLEXES' named entity 'HOMEOSTASIS' named entity 'HIGHLY' named entity 'ENTA' named entity 'HAVE' named entity 'REPORT' named entity 'ONE OF' named entity 'SURVIVAL' named entity 'STUDIES' named entity 'INHIBITORY EFFECT' named entity 'AMINO' named entity 'STABLE' named entity 'DRUG TARGET' named entity 'RECENTLY' named entity 'STABILIZATION' named entity 'VIRULENCE' named entity 'GROWTH' named entity 'TRANSPORTERS' named entity 'QPCR ASSAYS' named entity 'STABILIZING' named entity 'GENES' named entity 'MALE' named entity 'REQUIRED' named entity 'SALMONELLA ENTERICA' named entity 'G-QUADRUPLEX' named entity 'MALTOSE' named entity 'NOVEL' named entity 'INFERRED' named entity 'CONFIRMED BY' named entity 'EMSA' named entity 'MELTING' named entity 'STRUCTURES' named entity 'REACTIVE' named entity 'GASTROINTESTINAL TRACT' named entity 'INHIBITION' named entity 'VARIOUS' named entity 'FORMATION' named entity 'ACRIDINE' named entity 'CONSERVED' named entity 'REGULATORY REGION ' named entity 'REVEALED' named entity 'HOST' named entity 'G-QUADRUPLEX' named entity 'BIOLOGICAL' named entity 'NMR SPECTROSCOPY' named entity 'DEMONSTRATED' named entity 'PREDICTED' named entity 'THERAPEUTIC' named entity 'GROWTH' named entity 'TRANSPORT' named entity 'POLYMERASE' named entity 'MACROPHAGES' named entity 'GENOME' named entity 'CARBON SOURCE' named entity 'BACTERIAL' named entity 'FORMING' named entity 'SALMONELLA ENTERICA' named entity 'RELEVANCE' named entity 'MALTOSE'

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