| Congresso Brasileiro de Microbiologia 2023 | Resumo: 654-2 | ||||
Resumo:Helicobacter pylori and Campylobacter jejuni are Gram-negative, flagellated, microaerophile, spirally shaped, bacteria. While H. pylori infections are characterized by gastritis, and duodenal ulcers and are a risk factor for gastric cancer; C. jejuni infects several niches in the mucus layer of the human gastrointestinal tract. C. jejuni infections have also been associated with Guillain-Barré syndrome, a form of neuromuscular paralysis. Antibiotic treatments are effective for treating these infections. Still, the emergence of drug-resistant strains is currently one of the greatest health threats, and the World Health Organization (WHO) categorized these bacteria as an urgent need for new antimicrobial development. Nucleoid-Associated-Proteins (NAPs) are a group of global regulators that have been studied as a target for novel compounds to inhibit the biological activity of pathogenic bacteria. HU is one of the most studied NAPs and has an important influence on metabolic cycles; specifically in H. pylori, some studies show that HU protein could play an important role in bacterial infection by interfering with the host immune defenses. YbaB is not yet well characterized NAP protein and is also a promising drug target. Some studies show that YbaB is an anti-repressor of virulence genes in Borrelia burgdorferi. To better understand and compare the characteristics of both we analyzed the sequence and the in-silico structure of HU and YbaB in H. pylori and C. jejuni. First, to observe the sequence similarities between HU from H. pylori and C. jejuni, we investigated about 669 reviewed sequences of HU across several bacterial strains (IPR0001119) from the InterPro database of protein families and domains. Using the software MetaLogo version 1.1.3 we clustered these sequences into two primary groups of high sequence similarity. We use RoseTTAFold to model the protein structure and the FATCAT software version 2.0 pairwise structural alignment for structure prediction and comparison. We observed that HU is structurally similar in both bacteria species (p-value 1.69e-13 with 93 equivalent positions with an RMSD of 1.88Å). Similarly, we analyze the YbaB from several species and found four primary sequence clusters. After the YbaB protein modeling and pairwise alignment, we establish a significant structural similarity in both bacteria species (p-value 0.00e+00, with 97 equivalent positions with an RMSD of 0.86Å). These data suggest that both proteins in H. pylori and C. jejuni are highly similar in sequence and tridimensional structure and open a possibility to make this protein a target to study new development broad-spectrum NAP inhibitor. Palavras-chave: Campylobacter jejuni, Helicobacter pylori, HU, NAPs, YbaB Agência de fomento:Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) | |||||