Bioinformatics analysis of Helicobacter pylori metalloprotease gene
To determine the sequence of the metalloprotease gene (mtp) of Helicobacter pylori MEL-Hp27 strain and investigate the structural characters and biological function of the mtp-encoded protein using bioinformatic methods. The H. pylori mtp gene was applified by PCR from H. pylori MEL-Hp27 strain, and the mtp nucleotide sequence was obtained by gene sequencing. The amino acid sequence, physicochemical properties, transmembrane region, signal peptide, glycosylation and phosphorylation sites, secondary and tertiary structure of the mtp-encoded protein (Mtp) were analyzed using bioinformatics software. The coding region of MEL-HP27 mtp gene is 615 bp in length, encoding a protein comprising 204 amino acids. Bioinformatics analysis resulted in that the homology of mtp among various H. pylori strains is 91%-98%, the metalloprotease is an unstable and alkaline hydrophilic protein, without transmembrane region and signal peptide, but contains glycosylation and phosphorylation sites. The secondary structure of metalloprotease includes alpha helix, extended strand, beta turn, and random coil, which account for 52.45%, 16.67%, 4.41% and 26.47% of the whole molecular length, respectively. The conserved structures found in Mtp suggested that this protein might belong to the M48 protein family. Mtp contains B cell-associated antigenic epitopes and CTL cell antigenic epitopes. The results indicate that Mtp is alkaline hydrophilic protein with low molecular mass, located in cytoplasm or the nucleus might play crucial role in cellular signaling, regulation of cellular function, the mechanism of host immune response to H. pylori infection and the pathogenesis. The findings lay novel basis for approaching pathogenic mechanism and immune prevention of H. pylori infection.
In spite of investigation into the healthful prerequisites of Helicobacter pylori, little is known with respect to its utilization of complex substrates, for example, peptides. Examination of genome arrangements uncovered putative ABC-type transporter qualities for dipeptide (dppABCDF) and oligopeptide (oppABCD) transport. Qualities from every framework were PCR intensified, cloned, and disturbed by tape inclusion either independently (dppA, dppB, dppC, oppA, oppB, and oppC) or to make twofold freaks (dppAoppA, dppBoppB, dppBdppC, and oppBoppC). Peptide-using capacities of the strains were evaluated by checking development in an artificially characterized medium where the main wellspring of the fundamental amino corrosive isoleucine was from peptides of different lengths (two to nine amino acids long). The dipeptide framework freaks came up short on the capacity to utilize certain dipeptides, hexapeptides, and nonapeptides. In any case, these freaks held some capacity to develop with different dipeptides, tripeptides, and tetrapeptides. Of the oligopeptide freaks, just the oppB strain contrasted essentially from the wild kind. This strain demonstrated a wild-type phenotype for development with longer peptides (hexa-and nonapeptides) while having a diminished capacity to use di-, tri-, and tetrapeptides. The dppAoppA and dppBoppB freaks demonstrated comparative phenotypes to those of the dppA and dppB freaks, separately. Peptide absorption by metalloproteases was precluded as the reason for leftover peptide transport by developing freak strains within the sight of either EDTA or EGTA. Corruption items related with a fluorescein isothiocyanate-named hexapeptide (in addition to cells) were insignificant. An up 'til now unidentified peptide transport system(s) in H. pylori is proposed to be answerable for the leftover vehicle.
Helicobacter pylori is a gram-negative bacterium that is the causative operator of various stomach-related ailments, including peptic ulcer malady and certain gastric diseases . H. pylori has generally been developed on complex media, for the most part enhanced with either 5 to 10% blood or serum. In the course of the most recent 15 years, be that as it may, steps have been taken to create characterized media so as to contemplate the healthful and metabolic prerequisites of H. pylori . Most as of late, without a doubt the amino corrosive necessities for the development of H. pylori, just as the necessities of different supplements, (for example, follow metals) for H. pylori and other Helicobacter species, were resolved . In spite of the fact that it has been appeared to develop on glucose , H. pylori doesn't have the enzymatic hardware to separate progressively complex sugars and is along these lines constrained in its capacity to use starches as carbon sources. The bacterium can fuse some basic amino acids as a carbon source, yet similar investigations demonstrated that H. pylori requires various amino acids, including methionine, alanine, histidine, isoleucine, leucine, and valine, for protein amalgamation. These discoveries are in concurrence with the genomic data accessible . Then again, there have not been contemplates concerning H. pylori's capacity to process complex peptides as a carbon source. This is astonishing considering the plenitude of peptides in the stomach . An examination of sequenced H. pylori genomes uncovered explained frameworks for both dipeptide (dppABCDF) and oligopeptide (oppABCD) transport. Both of these frameworks are very rationed in H. pylori strains, demonstrating their basic nature . In view of homology, the two frameworks have a place with the ABC-type superfamily of transporters , contained a substrate restricting area (encoded by dppA and oppA) and two transmembranepermease spaces (encoded by dppBC and oppBC). ABC-type transport frameworks additionally usually contain one (oppD) or two (dppDF) ATP-restricting spaces that work as the vitality hotspot for substrate transport . Such transporter frameworks have been very much concentrated in Escherichia coli and Salmonella entericaserovarTyphimurium and in gram-positive life forms because of the high peptide substance of H. pylori's one of a kind specialty and its constrained capacity to use sugars as a carbon source, we wished to survey the jobs of these frameworks in H. pylori. Helicobacter pylori (H. pylori) is one of the most well-known human pathogens, influencing half of the total populace. Around 20% of the contaminated patients create gastric ulcers or neoplastic changes in the gastric stroma. A contamination likewise prompts the movement of epithelial–mesenchymal progress inside gastric tissue, expanding the likelihood of gastric disease advancement. This paper means to survey the job of H. pylori and its harmfulness factors in epithelial–mesenchymal change related with dangerous change inside the gastric stroma. The surveyed factors included: CagA (cytotoxin-related quality An) alongside enlistment of malignant growth foundational microorganism properties and connection with YAP (Yes-related protein pathway), tumor rot factor α-initiating protein, Lpp20 lipoprotein, Afadin protein, penicillin-restricting protein 1A, microRNA-29a-3p, modified cell passing protein 4, lysosomal-related protein transmembrane 4β, disease related fibroblasts, heparin-restricting epidermal development factor (HB-EGF), lattice metalloproteinase-7 (MMP-7), and disease undeveloped cells (CSCs). The survey sums up the latest discoveries, giving knowledge into likely atomic targets and new treatment methodologies for gastric malignant growth. Helicobacter pylori (H. pylori) is a helix-molded, Gram-negative, microaerophilic, flogged bacterium that is fit for biofilm arrangement and changing over from winding to coccoid structure It is an exceptionally obtrusive microorganism answerable for probably the most noteworthy predominance of ceaseless contaminations around the world, despite the fact that over 80% of tainted patients stay asymptomatic .H. pylori pathogenesis is because of a few harmfulness factors including urease, cytotoxin-related quality A (CagA), vacuolatingcytotoxin (VacA), external fiery protein An (OipA), duodenal ulcer advancing quality A (DupA), neutrophil-initiating protein A (NAP), heat stun proteins (Hsp10, Hsp60), and sialic corrosive restricting adhesin (SabA).