Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

The growing emergence of resistant bacteria is the current global concern for the humans and animals. Vaccination could be the desirable method to preventing such infectious diseases. Safe and effective vaccines are urgently needed to manage and prevent Salmonella contamination. Subunit vaccines are safe approaches for the protection against Salmonella spp. The bioinformatics methods were performed to determine the gene structure. Gene cassette (rLPSI) was ordered in pET28a (+), and cloned into E.coli BL21 (DE3), and the recombinant protein was expressed using IPTG (1 mM). Mice were immunized by subcutaneous administration of recombinant protein. Then, the mice were challenged by oral administration of 100LD of live S. Typhimurium. The Codon adaptation index of the chimeric gene was multiplied by 0.92. Validation results showed that >90% of residues lie in the desired or extra allowed area of the Ramachandran plot. The recombinant protein (65.9 kDa) was expressed in E.coli. Antibody titers in vaccinated mice were significantly different from those in the control groups. Recombinant protein immunization of the mice provided 90% and 70% protection against 10LD and 100LD of S. Typhimurium, respectively. In general, the results showed the high efficiency of rLPSI chimeric protein as a protective antigen against S. Typhimurium infection. The rLPSI chimeric protein could be an effective recombinant vaccine candidate against S. Typhimurium infection, but more research is needed.

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.micpath.2022.105959DOI Listing

Publication Analysis

Top Keywords

recombinant protein
16
chimeric protein
12
rlpsi chimeric
8
typhimurium infection
8
protein
7
recombinant
6
typhimurium
5
bioinformatics design
4
design recombinant
4
chimeric
4

Similar Publications

Construction of a bacterial surface display system using split green fluorescent protein (GFP) in Escherichia coli.

Biotechnol Lett

September 2025

Department of Chemical Engineering, Hongik University, Sangsu-dong, Mapo-gu, Seoul, 04066, Republic of Korea.

The cell surface display system employs carrier proteins to present target proteins on the outer membrane of cells. This system enables functional proteins to be exposed on the exterior of living cells without cell lysis, allowing direct interaction with the surrounding environment. A major limitation of conventional approaches is the difficulty in displaying large-sized enzymes or antibodies, despite their critical roles in applications requiring functional domains that must remain intact, such as catalytic or antigen-binding sites.

View Article and Find Full Text PDF

Structural biology is fundamental to understanding the molecular basis of biological processes. While machine learning-based protein structure prediction has advanced considerably, experimentally determined structures remain indispensable for guiding structure-function analyses and for improving predictive modeling. However, experimental studies of protein complexes continue to pose challenges, particularly due to the necessity of high protein concentrations and purity for downstream analyses such as cryogenic electron microscopy.

View Article and Find Full Text PDF

Discovery and phylogeny of a ricin-B-like domain from rice.

Carbohydr Res

September 2025

Laboratory for Biochemistry & Glycobiology, Ghent University, Department of Biotechnology, Ghent, Belgium. Electronic address:

Lectins are carbohydrate-binding proteins which play key roles in various biological processes, including cell signaling, pathogen recognition and development. Previous research conducted on ricin-B lectin domains and carbohydrate-binding modules of family 13 (CBM13) illustrated the striking resemblances between these two groups of protein domains. In this study, we report on the discovery, identification and putative biochemical characteristics of a ricin-B-like domain that is unique for GH27 enzymes from land plants, identified in the OsAPSE enzyme from Japanese rice (Oryza sativa L.

View Article and Find Full Text PDF

Hepcidin is the key hyposideremic hormone produced primarily by the liver. However, recent reports reveal extra-hepatic functional sources of hepcidin, including the intestine, the site of dietary iron absorption. To determine whether intestinal hepcidin may play a role in plasma iron lowering, we generated transgenic mice overexpressing the peptide specifically in this tissue.

View Article and Find Full Text PDF

Recombinant DNA technology is widely used to produce industrially and pharmaceutically important proteins. In silico analysis, performed before executing wet lab experiments has been greatly helpful in this connection. A shift in protein analysis has been observed over the past decade, driven by advancements in bioinformatics databases, tools, software, and web servers.

View Article and Find Full Text PDF