Serological Analysis of Immunogenic Properties of Recombinant Meningococcus IgA1 Protease-Based Proteins

Kotel’nikova, O. V.; Zinchenko, Anatoly; Vikhrov, A. A.; Alliluev, A. P.; Serova, O. V.; Гордеева, Е. А.; Zhigis, L. S.; Zueva, V. S.; Razgulyaeva, O. A.; Melikhova, T. D.; Nokel, E. A.; Drozhzhina, E. Yu.; Румш, Л. Д.

doi:10.1007/s10517-016-3422-2

Cited by 10 publications

(5 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…IgA proteases in other bacteria are components of autotransporter molecules, enhance bacterial invasion of mucosal surfaces, and assist in bacterial escape from host defenses (Mistry and Stockley, 2006). In addition, bacterial IgA proteases are immunogenic and stimulate local and systemic antibodies in infected hosts (Morelli et al ., 1994; Kirkeby et al ., 2000; Kotelnikova et al ., 2016).…”

Section: Virulence Factors and Potential Immunogensmentioning

confidence: 99%

Mannheimia haemolyticain bovine respiratory disease: immunogens, potential immunogens, and vaccines

Confer

Ayalew

2018

Anim. Health. Res. Rev.

View full text Add to dashboard Cite

Mannheimia haemolytica is the major cause of severe pneumonia in bovine respiratory disease (BRD). Early M. haemolytica bacterins were either ineffective or even enhanced disease in vaccinated cattle, which led to studies of the bacterium's virulence factors and potential immunogens to determine ways to improve vaccines. Studies have focused on the capsule, lipopolysaccharide, various adhesins, extracellular enzymes, outer membrane proteins, and leukotoxin (LKT) resulting in a strong database for understanding immune responses to the bacterium and production of more efficacious vaccines. The importance of immunity to LKT and to surface antigens in stimulating immunity led to studies of individual native or recombinant antigens, bacterial extracts, live-attenuated or mutant organisms, culture supernatants, combined bacterin-toxoids, outer membrane vesicles, and bacterial ghosts. Efficacy of several of these potential vaccines can be shown following experimental M. haemolytica challenge; however, efficacy in field trials is harder to determine due to the complexity of factors and etiologic agents involved in naturally occurring BRD. Studies of potential vaccines have led current commercial vaccines, which are composed primarily of culture supernatant, bacterin-toxoid, or live mutant bacteria. Several of those can be augmented experimentally by addition of recombinant LKT or outer membrane proteins.

show abstract

Section: Virulence Factors and Potential Immunogensmentioning

confidence: 99%

Mannheimia haemolyticain bovine respiratory disease: immunogens, potential immunogens, and vaccines

Confer

Ayalew

2018

Anim. Health. Res. Rev.

View full text Add to dashboard Cite

show abstract

“…The antibody titer to recombinant proteins in the human and animal sera was determined by ELISA [2].…”

Section: Methodsmentioning

confidence: 99%

Correction to: Specific Antibodies to the Fragments of Meningococcal IgA1 Protease during the Formation of Immunity to Bacterial Infections

et al. 2022

Self Cite

View full text Add to dashboard Cite

The features of individual fragments of IgA1 protease of Neisseria meningitidis serogroup B during the formation of immunity to bacterial infections in animals and humans were studied. The antibodies to the immunogenic regions of the studied proteins are also detected in mice infected with some bacterial pathogens and in humans with bacterial meningitis. A region of IgA1 protease was identified that is not capable of producing antibodies during immunization of animals, but that detects homologous antibodies in the blood of humans and animals recovered from bacterial infections. It has been suggested that this fragment plays a regulatory role in the process of immunogenesis.

show abstract

“…Experimental confirmation of the protective activity of IgA1 protease is shown in a small number of works. In a series of works [64][65][66][67][68][69][70][71][72][73][74] in animal experiments, it was shown that native IgA1 protease isolated from a live virulent culture of N. meningitidis serogroup A, as well as recombinant IgA1 proteases of N. meningitidis serogroup B in active or mutant forms, and some truncated analogs of these proteins have high immunogenic and protective activity.…”

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

confidence: 99%

“…It was also shown that specific antibodies formed upon immunization of animals with IgA1 protease analogs or upon infection with meningococcus are capable of binding not only to the secreted enzyme, but also to the surface of microbial cells [66].…”

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

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Serological Analysis of Immunogenic Properties of Recombinant Meningococcus IgA1 Protease-Based Proteins

Cited by 10 publications

References 8 publications

Mannheimia haemolyticain bovine respiratory disease: immunogens, potential immunogens, and vaccines

Mannheimia haemolyticain bovine respiratory disease: immunogens, potential immunogens, and vaccines

Correction to: Specific Antibodies to the Fragments of Meningococcal IgA1 Protease during the Formation of Immunity to Bacterial Infections

IgA1 Protease as a Vaccine Basis for Prevention of Bacterial Meningitis

Contact Info

Product

Resources

About