Cloning and Expression of H. influenzae 49247 IgA Protease in E. coli

Wang, Honglian; Zhong, Xia; Li, Jianchun; Zhu, Menglian; Wang, Lu; Ji, Xingli; Fan, Junming; Wang, Li

doi:10.1007/s12033-017-0054-3

Cited by 7 publications

(8 citation statements)

References 17 publications

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“…58 Gram-negative pathogenic bacteria such as Haemophilus influenzae and Neisseria gonorrhoeae also produce IgA proteases. [110][111][112] However, the amino acid sequences and protein structures of these IgA proteases are totally different from those of streptococcal IgA proteases (Figure 5). [110][111][112] Streptococcal IgA proteases are metalloproteases containing zinc-binding sequences with the cell wall-anchored motif LPxTG in their N-terminal region.…”

Section: Cell Surface Proteins and Enzymes (4): Iga Proteasementioning

confidence: 99%

“…The secretion of IgA proteases from the outer membranes of these Gram-negative bacteria requires both autocleavage site and autotransporter domain. [110][111][112] Both types of IgA proteases cleave the hinge region of IgA1; however, the cleave sites are not identical. 54,110 Regardless of the presence of IgA1 proteases, the majority of oral bacteria have antibodies bound to their surfaces.…”

Section: Cell Surface Proteins and Enzymes (4): Iga Proteasementioning

confidence: 99%

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Oral mitis group streptococci: A silent majority in our oral cavity

Okahashi

Nakata

Kuwata

et al. 2022

Microbiology and Immunology

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Members of the oral mitis group streptococci including Streptococcus oralis, Streptococcus sanguinis, and Streptococcus gordonii are the most abundant inhabitants of human oral cavity and dental plaque, and have been implicated in infectious complications such as bacteremia and infective endocarditis. Oral mitis group streptococci are genetically close to Streptococcus pneumoniae; however, they do not produce cytolysin (pneumolysin), which is a key virulence factor of S. pneumoniae. Similar to S. pneumoniae, oral mitis group streptococci possess several cell surface proteins that bind to the cell surface components of host mammalian cells. S. sanguinis expresses long filamentous pili that bind to the matrix proteins of host cells. The cell wall–anchored nuclease of S. sanguinis contributes to the evasion of the neutrophil extracellular trap by digesting its web‐like extracellular DNA. Oral mitis group streptococci produce glucosyltransferases, which synthesize glucan (glucose polymer) from sucrose of dietary origin. Neuraminidase (NA) is a virulent factor in oral mitis group streptococci. Influenza type A virus (IAV) relies on viral NA activity to release progeny viruses from infected cells and spread the infection, and NA‐producing oral streptococci elevate the risk of IAV infection. Moreover, oral mitis group streptococci produce hydrogen peroxide (H2O2) as a by‐product of sugar metabolism. Although the concentrations of streptococcal H2O2 are low (1–2 mM), they play important roles in bacterial competition in the oral cavity and evasion of phagocytosis by host macrophages and neutrophils. In this review, we intended to describe the diverse pathogenicity of oral mitis group streptococci.

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Section: Cell Surface Proteins and Enzymes (4): Iga Proteasementioning

confidence: 99%

Section: Cell Surface Proteins and Enzymes (4): Iga Proteasementioning

confidence: 99%

Oral mitis group streptococci: A silent majority in our oral cavity

Okahashi

Nakata

Kuwata

et al. 2022

Microbiology and Immunology

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“…The reason might be that higher temperature enhanced the metabolism rate of cells, as well as accelerated the target protein's synthesis, consequently, the proportion of the target protein's active conformation was decreased; induction at lower temperatures caused the low growth rate of cells as well as the production of the target protein. In T7 promoterbased expression system, IPTG was usually used to induce the working of the expression system [27][28][29][30].…”

Section: Expressing Of Choe and Production Of Choementioning

confidence: 99%

Gene cloning and molecular characterization of a thermostable chitosanase from Bacillus cereus TY24

Zhang

et al. 2022

BMC Biotechnol

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Background An important conceptual advance in health and the environment has been recognized that enzymes play a key role in the green processing industries. Of particular interest, chitosanase is beneficial for recycling the chitosan resource and producing chitosan oligosaccharides. Also, chitosan gene expression and molecular characterization will promote understanding of the biological function of bacterial chitosanase as well as explore chitosanase for utilizing chitosan resources. Results A chitosanase-producing bacterium TY24 was isolated and identified as Bacillus cereus. Moreover, the chitosanase gene was cloned and expressed in Escherichia coli. Sequence analysis reveals that the recombinant chitosanase (CHOE) belongs to the glycoside hydrolases 8 family. The purified CHOE has a molecular weight of about 48 kDa and the specific activity of 1150 U/mg. The optimal pH and temperature of CHOE were 5.5 and 65 °C, respectively. The enzyme was observed stable at the pH range of 4.5–7.5 and the temperature range of 30–65 °C. Especially, the half-life of CHOE at 65 °C was 161 min. Additionally, the activity of CHOE was remarkably enhanced in the presence of Mn2+, Cu2+, Mg2+ and K+, beside Ca2+ at 5 mM. Especially, the activity of CHOE was enhanced to more than 120% in the presence of 1% of various surfactants. CHOE exhibited the highest substrate specificity toward colloid chitosan. Conclusion A bacterial chitosanase was cloned from B. cereus and successfully expressed in E. coli (BL21) DE3. The recombinant enzyme displayed good stability under acid pH and high-temperature conditions.

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“…Wang et al [55] designed and obtained a highly active recombinant IgA1 protease from H. influenzae 49247 capable of cleaving a glycosylated IgA1-containing immune complex in vitro with the aim of possibly using the enzyme as a therapeutic agent for the treatment of IgA nephropathy. The severity of impairment of renal function, such as proteinuria and hematuria, can also be reduced by injections of IgA1 protease [56].…”

Section: Iga1 Protease and Its Fragments As A Basis For The Creation Of Therapeutic And Preventive Agentsmentioning

confidence: 99%

IgA1 Protease as a Vaccine Basis for Prevention of Bacterial Meningitis

et al. 2021

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The review covers the study of the protective properties of IgA1 protease and the possibility of creating a vaccine preparation for the prevention of bacterial meningitis of various origins on its basis. Bacterial meningitis belongs to the group of socially dangerous diseases and is characterized by a severe course, numerous complications and high mortality. The approaches used at present in world practice to create antimicrobial vaccines are based on a narrow targeting against a specific pathogen. The development of a monocomponent vaccine against a wide range of bacterial pathogens with a common virulence factor is still relevant. IgA1 protease, a protein that is one of the main virulence factors of a number of gram-negative and gram-positive bacteria, can serve as such an antigen. Bacterial IgA1 protease is uniquely specific for immunoglobulins A1 (IgA1), cleaving peptide bonds in the hinge regions of the IgA1 in humans and other higher primates. Bacteria, getting on the mucous membrane, destroy IgA1, which acts as the first barrier to protect the body from infections. Neutralization of IgA1 protease at this stage can become an obstacle to the development of infection, hindering the adhesion of a number of pathogens that produce this protein. The data available in the literature on the mechanism of antibacterial protection are scattered and ambiguous. The review considers the literature data and the results of our own experiments on the protective activity of IgA1 protease. We have shown that the recombinant meningococcal IgA1 protease and some of its fragments protect mice from infection with a live virulent culture not only of meningococci of the main epidemic serogroups (A, B, C, and W135), but also of some of the most common virulent pneumococcal serotypes. The data obtained indicate the possibility of creating a monocomponent vaccine against these and, possibly, other bacterial infections. Currently, significant progress has been made in studying the structure and functions of secreted proteins in the bacteria Neisseria meningitidis and Haemophilus influenzae. In this review we describe protein translocation systems of N. meningitidis, which are related to the secretion of proteins in these bacteria, and also present modern data on the functions of these proteins. Analysis of experimental data on the structure of IgA1 protease of N. meningitidis and the formation of immunity during vaccination is of key importance in the development of prophylactic preparations.

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Cloning and Expression of H. influenzae 49247 IgA Protease in E. coli

Cited by 7 publications

References 17 publications

Oral mitis group streptococci: A silent majority in our oral cavity

Oral mitis group streptococci: A silent majority in our oral cavity

Gene cloning and molecular characterization of a thermostable chitosanase from Bacillus cereus TY24

IgA1 Protease as a Vaccine Basis for Prevention of Bacterial Meningitis

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