Expression of Recombinant Stonustoxin Alpha Subunit and Preparation of polyclonal antiserum for Stonustoxin Neutralization Studies.

Stonustoxin (SNTX) is a lethal protein found in stonefish venom, responsible for many of the symptoms associated with stonefish envenomation. To counter stonefish venom challenges, antivenom is a well-established and effective solution. In this study, we aimed to produce the recombinant alpha subunit protein of Stonustoxin from Synanceia horrida and prepare antibodies against it The SNTXα gene sequence was optimized for E.

Antibodies Produced Toward Recombinant RBD and Nucleocapsid Neutralize SARS-COV-2.

Background: The highly contagious SARS-COV-2 virus spread rapidly from China and formed a global pandemic. The virus has infected over 509 million people worldwide and killed about 6.32 million up to date.

In silico design, production and immunization evaluation of a recombinant bivalent fusion protein candidate vaccine against E. coli O157:H7.

In silico techniques are highly suited for both the discovery of new and development of available vaccines. Escherichia coli O157: H7, a main cause of food poisoning can infect humans through the consumption of contaminated water or food. Vaccination is a choice strategy to combat the bacterium.

An Design, Expression and Purification of a Chimeric Protein as an Immunogen Candidate Consisting of IpaD, StxB, and TolC Proteins from spp.

Background: spp. is the cause of dysentery and is widespread worldwide. On the other hand, antibiotic resistance is increasing in this bacterium.

Preclinical study of formulated recombinant nucleocapsid protein, the receptor binding domain of the spike protein, and truncated spike (S1) protein as vaccine candidates against COVID-19 in animal models.

Background: In this pre-clinical study, we designed a candidate vaccine based on severe acute respiratory syndrome-related -coronavirus 2 (SARS-CoV-2) antigens and evaluated its safety and immunogenicity.

Methods: SARS-CoV-2 recombinant protein antigens, including truncated spike protein (SS1, lacking the N-terminal domain of S1), receptor-binding domain (RBD), and nucleoprotein (N) were used. Immunization program was performed via injection of RBD, SS1 +RBD, and SS1 +N along with different adjuvants, Alum, AS03, and Montanide at doses of 0, 40, 80, and 120 μg at three-time points in mice, rabbits, and primates.

In silico and in vivo approaches to recombinant multi-epitope immunogen of GroEL provides efficient cross protection against S. Typhimurium, S. flexneri, and S. dysenteriae.

Objectives: Stress or Heat Shock Proteins (HSPs) have been included in various operations like protein folding, autophagy, and apoptosis. HSP families recognize as protective antigens in a wide range of bacteria because they have been conserved through evolution. Due to their homology as well as antigenicity they are competent for applying in cross-protection against bacterial diseases.

An approach to chimeric subunit immunogen provides efficient protection against toxicity, type III and type v secretion systems of Shigella.

Objectives: Shigellosis is one of the infectious diseases causing severe intestinal illness in human beings. Development of an effective vaccine against Shigella is a key to deal with this bacterium. The present study aimed at evaluation of the antibody response as well as the protection of the recombinant chimeric protein containing IpaD, IpaB, StxB, and VirG against Shigella dysentery and flexneri.

Entrapment of HETS recombinant protein onto PLGA and alginate NPs improves the immunogenicity of the protein against E. coli O157:H7.

Enterohemorrhagic Escherichia coli (EHEC) are known as the gastrointestinal pathogens and major causes of enterohemorrhagic colitis since decades ago. There is no efficient approved vaccine against EHEC O157 and non-O157. In the present study, a recombinant candidate vaccine against enterohemorrhagic E.

Recombinant HcpA-EspA-Tir-Stx2B chimeric protein induces immunity against attachment and toxicity of Escherichia coli O157:H7.

Background: It is about 4 decades from the identification of Enterohemorrhagic Escherichia coli (EHEC) as a food-borne pathogen. There are many shreds of evidence that the bacteria are significant sources of intestinal infections and outbreaks even in developed countries. Developing an effective vaccine against O157 and non-O157 serotypes of EHEC is a good strategy to combat the bacteria.

An LTB-entrapped protein in PLGA nanoparticles preserves against enterotoxin of enterotoxigenic .

Objectives: Enterotoxigenic (ETEC) is known as the most common bacterial causes of diarrheal diseases related to morbidity and mortality. Heat-labile enterotoxin (LT) is a part of major virulence factors in ETEC pathogenesis. Antigen entrapment into nanoparticles (NPs) can protect them and enhance their immunogenicity.

Entrapment of LTB protein in alginate nanoparticles protects against Enterotoxigenic Escherichia coli.

Vaccine delivery vehicles are just as important in vaccine efficiency. Through the progress in nanotechnology, various nanoparticles have been evaluated as carriers for these substances. Among them, alginate nanoparticles are a good choice because of their biodegradability, biocompatibility, ease of production, etc.